Ignet

Gene Information

Gene symbol: DCN

Gene name: decorin

HGNC ID: 2705

Synonyms: DSPG2, SLRR1B

Related Genes

#	Gene Symbol	Number of hits
1	ACE	1 hits
2	ADIPOQ	1 hits
3	AKT1	1 hits
4	ALB	1 hits
5	BGN	1 hits
6	CD36	1 hits
7	CDKN1B	1 hits
8	COL1A1	1 hits
9	COL4A4	1 hits
10	CSF2	1 hits
11	F2	1 hits
12	FBN1	1 hits
13	FCGR1A	1 hits
14	FHL2	1 hits
15	FMOD	1 hits
16	GRHL1	1 hits
17	HSPG2	1 hits
18	ICAM1	1 hits
19	IDDM2	1 hits
20	IGF1	1 hits
21	IL10	1 hits
22	IL2	1 hits
23	INS	1 hits
24	ISG20	1 hits
25	LUM	1 hits
26	MARK2	1 hits
27	MRXS5	1 hits
28	MT-CO2	1 hits
29	NOX4	1 hits
30	PDLIM5	1 hits
31	PPARA	1 hits
32	PPARG	1 hits
33	PTGS2	1 hits
34	PVR	1 hits
35	RETN	1 hits
36	RPS6KB1	1 hits
37	SDC1	1 hits
38	SDC4	1 hits
39	SERPINE1	1 hits
40	SGK1	1 hits
41	SMAD2	1 hits
42	SMAD4	1 hits
43	TGFA	1 hits
44	TGFB1	1 hits
45	TGFBR3	1 hits
46	TNF	1 hits
47	TRO	1 hits
48	UBASH3B	1 hits
49	VCAN	1 hits

Related Sentences

#	PMID	Sentence
1	7593228	Biglycan but not decorin mRNAs were detected by Northern analysis and by PCR.
2	7679595	We conclude that both tenascin and decorin play a role in the development of epiretinal PVR and PDR membranes by controlling cell adhesion and regulating ECM formation.
3	7713310	Immunohistochemically an increase of laminin, collagen III and IV staining was observed in the mesangium and in the glomerular basement membrane, without alterations in glomerular basement membrane staining of heparan sulphate proteoglycan core protein or heparan sulphate.
4	7850412	Recently, the proteoglycan decorin was shown to neutralize TGF-beta.
5	7850412	Thus, decorin offers hope as a treatment for progressive kidney diseases caused by the overproduction of TGF-beta.
6	7850412	Recently, the proteoglycan decorin was shown to neutralize TGF-beta.
7	7850412	Thus, decorin offers hope as a treatment for progressive kidney diseases caused by the overproduction of TGF-beta.
8	8645702	It is possible that the two proteoglycans represent two populations, one with two dermatan sulfate side chains (120 kDa) and the other with only one side chain (85 kDa), presumably fitting in the decorin/biglycan family of small proteoglycans.
9	9162605	Patients with insulin-dependent diabetes mellitus (IDDM) and albuminuria are at high risk for severe micro- and macrovascular complications.
10	9162605	Diabetic vascular complications are characterized by structural alterations of extracellular matrix (ECM) components in glomeruli and large vessel walls, namely, accumulation of collagen IV, collagen VI and fibronectin and relative decrease of heparan sulphate proteoglycan (HSPG).
11	9162605	TGF-beta stimulates production of ECM components such as collagen IV, fibronectin, proteoglycans (decorin and biglycan) without increasing HSPG.
12	9162605	TGF-beta antagonists, such as decorin, betaglycan, and possibly also heparin, might be potential candidates for future therapy to prevent diabetic vascular disease.
13	9162605	Patients with insulin-dependent diabetes mellitus (IDDM) and albuminuria are at high risk for severe micro- and macrovascular complications.
14	9162605	Diabetic vascular complications are characterized by structural alterations of extracellular matrix (ECM) components in glomeruli and large vessel walls, namely, accumulation of collagen IV, collagen VI and fibronectin and relative decrease of heparan sulphate proteoglycan (HSPG).
15	9162605	TGF-beta stimulates production of ECM components such as collagen IV, fibronectin, proteoglycans (decorin and biglycan) without increasing HSPG.
16	9162605	TGF-beta antagonists, such as decorin, betaglycan, and possibly also heparin, might be potential candidates for future therapy to prevent diabetic vascular disease.
17	9815141	The core protein of the proteoglycan decorin binds and neutralizes transforming growth factor-beta (TGF-beta).
18	9815141	Activation of TGF-beta is crucial to tissue injury in diabetic nephropathy, but it is not currently known whether decorin plays a role in this disease.
19	9815141	When mouse mesangial and proximal tubular cells are exposed to TGF-beta1 (1 ng/ml), decorin mRNA is significantly decreased.
20	9815141	Our findings suggest that the increased decorin expression in the diabetic kidney may counteract the hypertrophic and prosclerotic effects of increased TGF-beta levels and that a negative feedback loop may exist between decorin and TGF-beta.
21	9815141	The core protein of the proteoglycan decorin binds and neutralizes transforming growth factor-beta (TGF-beta).
22	9815141	Activation of TGF-beta is crucial to tissue injury in diabetic nephropathy, but it is not currently known whether decorin plays a role in this disease.
23	9815141	When mouse mesangial and proximal tubular cells are exposed to TGF-beta1 (1 ng/ml), decorin mRNA is significantly decreased.
24	9815141	Our findings suggest that the increased decorin expression in the diabetic kidney may counteract the hypertrophic and prosclerotic effects of increased TGF-beta levels and that a negative feedback loop may exist between decorin and TGF-beta.
25	9815141	The core protein of the proteoglycan decorin binds and neutralizes transforming growth factor-beta (TGF-beta).
26	9815141	Activation of TGF-beta is crucial to tissue injury in diabetic nephropathy, but it is not currently known whether decorin plays a role in this disease.
27	9815141	When mouse mesangial and proximal tubular cells are exposed to TGF-beta1 (1 ng/ml), decorin mRNA is significantly decreased.
28	9815141	Our findings suggest that the increased decorin expression in the diabetic kidney may counteract the hypertrophic and prosclerotic effects of increased TGF-beta levels and that a negative feedback loop may exist between decorin and TGF-beta.
29	9815141	The core protein of the proteoglycan decorin binds and neutralizes transforming growth factor-beta (TGF-beta).
30	9815141	Activation of TGF-beta is crucial to tissue injury in diabetic nephropathy, but it is not currently known whether decorin plays a role in this disease.
31	9815141	When mouse mesangial and proximal tubular cells are exposed to TGF-beta1 (1 ng/ml), decorin mRNA is significantly decreased.
32	9815141	Our findings suggest that the increased decorin expression in the diabetic kidney may counteract the hypertrophic and prosclerotic effects of increased TGF-beta levels and that a negative feedback loop may exist between decorin and TGF-beta.
33	10078565	SMCs expressed 2-10 times more mRNA for the core proteins of the proteoglycans versican, decorin, and syndecan 4 compared with control cells.
34	10078565	Darglitazone, a peroxisome proliferator-activated receptor (PPAR)-gamma ligand, neutralized the NEFA-mediated induction of the decorin gene.
35	10078565	SMCs expressed 2-10 times more mRNA for the core proteins of the proteoglycans versican, decorin, and syndecan 4 compared with control cells.
36	10078565	Darglitazone, a peroxisome proliferator-activated receptor (PPAR)-gamma ligand, neutralized the NEFA-mediated induction of the decorin gene.
37	10449443	In this report, we demonstrate aberrant constitutive expression of the normally inducible cyclooxygenase PG synthase 2 (PGS(2)/ COX-2) in nonactivated monocytes of humans with insulin-dependent diabetes mellitus (IDDM) and those with islet autoantibodies at increased risk of developing this disease.
38	10449443	Constitutive PGS(2) appears to characterize a high risk for diabetes as it correlates with and predicts a low first-phase insulin response in autoantibody-positive subjects.
39	10449443	Abnormal PGS(2) expression in at-risk subjects affected immune response in vitro, as the presence of a specific PGS(2) inhibitor, NS398, significantly increased IL-2 receptor alpha-chain (CD25) expression on phytohemagglutinin-stimulated T cells.
40	10449443	The effect of PGS(2) on CD25 expression was most profound in subjects expressing both DR04 and DQbeta0302 high-risk alleles, suggesting that this cyclooxygenase interacts with diabetes-associated MHC class II antigens to limit T-cell activation.
41	10449443	These results indicate that constitutive PGS(2) expression in monocytes defines an antigen-presenting cell defect affecting immune response, and that this expression is a novel cell-associated risk marker for IDDM.
42	10449443	In this report, we demonstrate aberrant constitutive expression of the normally inducible cyclooxygenase PG synthase 2 (PGS(2)/ COX-2) in nonactivated monocytes of humans with insulin-dependent diabetes mellitus (IDDM) and those with islet autoantibodies at increased risk of developing this disease.
43	10449443	Constitutive PGS(2) appears to characterize a high risk for diabetes as it correlates with and predicts a low first-phase insulin response in autoantibody-positive subjects.
44	10449443	Abnormal PGS(2) expression in at-risk subjects affected immune response in vitro, as the presence of a specific PGS(2) inhibitor, NS398, significantly increased IL-2 receptor alpha-chain (CD25) expression on phytohemagglutinin-stimulated T cells.
45	10449443	The effect of PGS(2) on CD25 expression was most profound in subjects expressing both DR04 and DQbeta0302 high-risk alleles, suggesting that this cyclooxygenase interacts with diabetes-associated MHC class II antigens to limit T-cell activation.
46	10449443	These results indicate that constitutive PGS(2) expression in monocytes defines an antigen-presenting cell defect affecting immune response, and that this expression is a novel cell-associated risk marker for IDDM.
47	10449443	In this report, we demonstrate aberrant constitutive expression of the normally inducible cyclooxygenase PG synthase 2 (PGS(2)/ COX-2) in nonactivated monocytes of humans with insulin-dependent diabetes mellitus (IDDM) and those with islet autoantibodies at increased risk of developing this disease.
48	10449443	Constitutive PGS(2) appears to characterize a high risk for diabetes as it correlates with and predicts a low first-phase insulin response in autoantibody-positive subjects.
49	10449443	Abnormal PGS(2) expression in at-risk subjects affected immune response in vitro, as the presence of a specific PGS(2) inhibitor, NS398, significantly increased IL-2 receptor alpha-chain (CD25) expression on phytohemagglutinin-stimulated T cells.
50	10449443	The effect of PGS(2) on CD25 expression was most profound in subjects expressing both DR04 and DQbeta0302 high-risk alleles, suggesting that this cyclooxygenase interacts with diabetes-associated MHC class II antigens to limit T-cell activation.
51	10449443	These results indicate that constitutive PGS(2) expression in monocytes defines an antigen-presenting cell defect affecting immune response, and that this expression is a novel cell-associated risk marker for IDDM.
52	10449443	In this report, we demonstrate aberrant constitutive expression of the normally inducible cyclooxygenase PG synthase 2 (PGS(2)/ COX-2) in nonactivated monocytes of humans with insulin-dependent diabetes mellitus (IDDM) and those with islet autoantibodies at increased risk of developing this disease.
53	10449443	Constitutive PGS(2) appears to characterize a high risk for diabetes as it correlates with and predicts a low first-phase insulin response in autoantibody-positive subjects.
54	10449443	Abnormal PGS(2) expression in at-risk subjects affected immune response in vitro, as the presence of a specific PGS(2) inhibitor, NS398, significantly increased IL-2 receptor alpha-chain (CD25) expression on phytohemagglutinin-stimulated T cells.
55	10449443	The effect of PGS(2) on CD25 expression was most profound in subjects expressing both DR04 and DQbeta0302 high-risk alleles, suggesting that this cyclooxygenase interacts with diabetes-associated MHC class II antigens to limit T-cell activation.
56	10449443	These results indicate that constitutive PGS(2) expression in monocytes defines an antigen-presenting cell defect affecting immune response, and that this expression is a novel cell-associated risk marker for IDDM.
57	10495473	ACE, PAI-1, decorin and Werner helicase genes are not associated with the development of renal disease in European patients with type 1 diabetes.
58	10652025	Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease.
59	10812497	Aberrant proteolytic digestion of biglycan and decorin by saliva and exocrine gland lysates from the NOD mouse model for autoimmune exocrinopathy.
60	11122703	In smooth muscle cells, NEFA-albumin complex increased the expression of the genes for the core proteins of the proteoglycans syndecan, decorin and perlecan.
61	11259366	Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin.
62	11259366	Small leucine-rich proteoglycans (SLRPs), for example, decorin, biglycan, fibromodulin, and lumican, are extracellular matrix organizers and binding partners of TGF-b.
63	11259366	Biglycan was expressed by glomerular endothelial cells and, together with fibromodulin, by distal tubular cells and in collecting ducts.
64	11259366	Decorin and lumican became expressed in tubuli.
65	11259366	In severe glomerulosclerosis, increased decorin concentrations were found in plasma and urine, and urinary TGF-b/decorin complexes could be demonstrated indirectly.
66	11259366	Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin.
67	11259366	Small leucine-rich proteoglycans (SLRPs), for example, decorin, biglycan, fibromodulin, and lumican, are extracellular matrix organizers and binding partners of TGF-b.
68	11259366	Biglycan was expressed by glomerular endothelial cells and, together with fibromodulin, by distal tubular cells and in collecting ducts.
69	11259366	Decorin and lumican became expressed in tubuli.
70	11259366	In severe glomerulosclerosis, increased decorin concentrations were found in plasma and urine, and urinary TGF-b/decorin complexes could be demonstrated indirectly.
71	11259366	Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin.
72	11259366	Small leucine-rich proteoglycans (SLRPs), for example, decorin, biglycan, fibromodulin, and lumican, are extracellular matrix organizers and binding partners of TGF-b.
73	11259366	Biglycan was expressed by glomerular endothelial cells and, together with fibromodulin, by distal tubular cells and in collecting ducts.
74	11259366	Decorin and lumican became expressed in tubuli.
75	11259366	In severe glomerulosclerosis, increased decorin concentrations were found in plasma and urine, and urinary TGF-b/decorin complexes could be demonstrated indirectly.
76	11259366	Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin.
77	11259366	Small leucine-rich proteoglycans (SLRPs), for example, decorin, biglycan, fibromodulin, and lumican, are extracellular matrix organizers and binding partners of TGF-b.
78	11259366	Biglycan was expressed by glomerular endothelial cells and, together with fibromodulin, by distal tubular cells and in collecting ducts.
79	11259366	Decorin and lumican became expressed in tubuli.
80	11259366	In severe glomerulosclerosis, increased decorin concentrations were found in plasma and urine, and urinary TGF-b/decorin complexes could be demonstrated indirectly.
81	11561166	The three principal CSPGs in the arterial wall are versican, which is part of the hyalectan gene family; and decorin and biglycan, which are members of a separate gene family, the small leucine-rich proteoglycans.
82	11879191	Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.
83	11879191	One of the main target cells for TGFbeta in the kidney are glomerular mesangial cells, which respond by increasing expression of ECM proteins, such as collagens, laminin and fibronectin, while suppressing the expression of ECM-degrading proteases and increasing the synthesis of ECM protease inhibitors, including plasminogen activator inhibitor-1.
84	11879191	While the mechanism by which TGFbeta stimulates gene expression via the Smad signal-transduction pathway is becoming clear, the precise mechanism by which decorin may impinge upon TGFbeta activity remains to be established.
85	11879191	In this study, for the first time we provide evidence that decorin can disrupt glucose- and TGFbeta/Smad-dependent transcriptional events in human mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and ensuing phosphorylation of Smad2 at Ser-240.
86	11879191	We show that decorin also induces Ser-240 phospho-Smad hetero-oligomerization with Smad4 and the nuclear localization of this complex independently of TGFbeta receptor activation.
87	11879191	Thus, in human mesangial cells, the mechanism of decorin-mediated inhibition of TGFbeta signalling may involve activation of Ca(2+) signalling, the subsequent phosphorylation of Smad2 at a key regulatory site, and the sequestration of Smad4 in the nucleus.
88	11879191	Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.
89	11879191	One of the main target cells for TGFbeta in the kidney are glomerular mesangial cells, which respond by increasing expression of ECM proteins, such as collagens, laminin and fibronectin, while suppressing the expression of ECM-degrading proteases and increasing the synthesis of ECM protease inhibitors, including plasminogen activator inhibitor-1.
90	11879191	While the mechanism by which TGFbeta stimulates gene expression via the Smad signal-transduction pathway is becoming clear, the precise mechanism by which decorin may impinge upon TGFbeta activity remains to be established.
91	11879191	In this study, for the first time we provide evidence that decorin can disrupt glucose- and TGFbeta/Smad-dependent transcriptional events in human mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and ensuing phosphorylation of Smad2 at Ser-240.
92	11879191	We show that decorin also induces Ser-240 phospho-Smad hetero-oligomerization with Smad4 and the nuclear localization of this complex independently of TGFbeta receptor activation.
93	11879191	Thus, in human mesangial cells, the mechanism of decorin-mediated inhibition of TGFbeta signalling may involve activation of Ca(2+) signalling, the subsequent phosphorylation of Smad2 at a key regulatory site, and the sequestration of Smad4 in the nucleus.
94	11879191	Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.
95	11879191	One of the main target cells for TGFbeta in the kidney are glomerular mesangial cells, which respond by increasing expression of ECM proteins, such as collagens, laminin and fibronectin, while suppressing the expression of ECM-degrading proteases and increasing the synthesis of ECM protease inhibitors, including plasminogen activator inhibitor-1.
96	11879191	While the mechanism by which TGFbeta stimulates gene expression via the Smad signal-transduction pathway is becoming clear, the precise mechanism by which decorin may impinge upon TGFbeta activity remains to be established.
97	11879191	In this study, for the first time we provide evidence that decorin can disrupt glucose- and TGFbeta/Smad-dependent transcriptional events in human mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and ensuing phosphorylation of Smad2 at Ser-240.
98	11879191	We show that decorin also induces Ser-240 phospho-Smad hetero-oligomerization with Smad4 and the nuclear localization of this complex independently of TGFbeta receptor activation.
99	11879191	Thus, in human mesangial cells, the mechanism of decorin-mediated inhibition of TGFbeta signalling may involve activation of Ca(2+) signalling, the subsequent phosphorylation of Smad2 at a key regulatory site, and the sequestration of Smad4 in the nucleus.
100	11879191	Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.
101	11879191	One of the main target cells for TGFbeta in the kidney are glomerular mesangial cells, which respond by increasing expression of ECM proteins, such as collagens, laminin and fibronectin, while suppressing the expression of ECM-degrading proteases and increasing the synthesis of ECM protease inhibitors, including plasminogen activator inhibitor-1.
102	11879191	While the mechanism by which TGFbeta stimulates gene expression via the Smad signal-transduction pathway is becoming clear, the precise mechanism by which decorin may impinge upon TGFbeta activity remains to be established.
103	11879191	In this study, for the first time we provide evidence that decorin can disrupt glucose- and TGFbeta/Smad-dependent transcriptional events in human mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and ensuing phosphorylation of Smad2 at Ser-240.
104	11879191	We show that decorin also induces Ser-240 phospho-Smad hetero-oligomerization with Smad4 and the nuclear localization of this complex independently of TGFbeta receptor activation.
105	11879191	Thus, in human mesangial cells, the mechanism of decorin-mediated inhibition of TGFbeta signalling may involve activation of Ca(2+) signalling, the subsequent phosphorylation of Smad2 at a key regulatory site, and the sequestration of Smad4 in the nucleus.
106	11879191	Decorin suppresses transforming growth factor-beta-induced expression of plasminogen activator inhibitor-1 in human mesangial cells through a mechanism that involves Ca2+-dependent phosphorylation of Smad2 at serine-240.
107	11879191	One of the main target cells for TGFbeta in the kidney are glomerular mesangial cells, which respond by increasing expression of ECM proteins, such as collagens, laminin and fibronectin, while suppressing the expression of ECM-degrading proteases and increasing the synthesis of ECM protease inhibitors, including plasminogen activator inhibitor-1.
108	11879191	While the mechanism by which TGFbeta stimulates gene expression via the Smad signal-transduction pathway is becoming clear, the precise mechanism by which decorin may impinge upon TGFbeta activity remains to be established.
109	11879191	In this study, for the first time we provide evidence that decorin can disrupt glucose- and TGFbeta/Smad-dependent transcriptional events in human mesangial cells through a mechanism that involves an increase in Ca(2+) signalling, the activation of Ca(2+)/calmodulin-dependent protein kinase II and ensuing phosphorylation of Smad2 at Ser-240.
110	11879191	We show that decorin also induces Ser-240 phospho-Smad hetero-oligomerization with Smad4 and the nuclear localization of this complex independently of TGFbeta receptor activation.
111	11879191	Thus, in human mesangial cells, the mechanism of decorin-mediated inhibition of TGFbeta signalling may involve activation of Ca(2+) signalling, the subsequent phosphorylation of Smad2 at a key regulatory site, and the sequestration of Smad4 in the nucleus.
112	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
113	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
114	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
115	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
116	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
117	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
118	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
119	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
120	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
121	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
122	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
123	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
124	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
125	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
126	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
127	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
128	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
129	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
130	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
131	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
132	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
133	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
134	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
135	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
136	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
137	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
138	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
139	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
140	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
141	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
142	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
143	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
144	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
145	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
146	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
147	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
148	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
149	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
150	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
151	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
152	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
153	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
154	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
155	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
156	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
157	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
158	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
159	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
160	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
161	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
162	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
163	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
164	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
165	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
166	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
167	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
168	15041043	IL10 resistant PGS2 expression in at-risk/Type 1 diabetic human monocytes.
169	15041043	Aberrant prostaglandin synthase 2 (PGS2/COX2) expression constitutes an antigen presenting cell (APC) dysfunction seen in monocytes of humans at risk for or with Type 1 diabetes.
170	15041043	During endotoxin activation of PGS2 expression in healthy monocytes, granulocyte-monocyte colony stimulating factor (GM-CSF) is activated and, in turn, promotes PGS2 gene activation.
171	15041043	GM-CSF is considered a major target the action for IL10 in its suppression of PGS2.
172	15041043	We found that the PGS2 expression in monocytes from 47% of at-risk and diabetic humans tested were highly resistant to suppression by IL10 (maintaining > or =50% of their untreated expression), and had significantly increased GM-CSF production in vitro (1043+/-SD2798 pg/10(6)cells, subject n=35, vs 29.7+/-SD91 pg/10(6)cells, control n=20; P=0.0165).
173	15041043	The PGS2 insensitivity to IL10 of these cells was not due to a lack of IL10 functionality or its suppression of GM-CSF.
174	15041043	In contrast to its effects on PGS2, IL10 regulation of GM-CSF and other monocyte factors (i.e., DR, IL1beta, TNFalpha, IL12, CD54, and CD64) remained intact.
175	15041043	These findings suggest that the inability of IL10 to properly downregulate PGS2 gene expression may contribute to its dysregulation in Type 1 diabetes.
176	15661861	Dihydrotestosterone (10 nm) and testosterone (100 nm) treatment of VSMCs resulted in the synthesis of biglycan and decorin that showed reduced electrophoretic mobility by SDS-PAGE, indicating an increase in GAG length.
177	15713786	Particularly interesting cases of common or tissue-specific regulation included decorin and CD36, which were upregulated in several tissues, and serum/glucocorticoid-regulated kinase and four and a half LIM domains 2, which were upregulated only in the renal cortex.
178	15761618	Immunoblotting of these proteins was positive for the small proteoglycans fibromodulin and decorin, respectively.
179	16380460	In diabetic mgR/+ and mgR/mgR, but not in wild-type mice, an induction of glomerular decorin expression was observed.
180	16630654	Immunohistochemistry indicated intensive staining of decorin and biglycan in the diabetic placenta with different localizations.
181	16630654	Additionally, the basement membrane HSPG, perlecan was found to contain both CS/DS and HS in GDM placentas and plain HS in controls.
182	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
183	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
184	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
185	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
186	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
187	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
188	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
189	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
190	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
191	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
192	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
193	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
194	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
195	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
196	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
197	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
198	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
199	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
200	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
201	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
202	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
203	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
204	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
205	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
206	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
207	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
208	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
209	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
210	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
211	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
212	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
213	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
214	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
215	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
216	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
217	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
218	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
219	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
220	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
221	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
222	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
223	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
224	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
225	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
226	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
227	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
228	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
229	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
230	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
231	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
232	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
233	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
234	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
235	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
236	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
237	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
238	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
239	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
240	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
241	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
242	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
243	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
244	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
245	17200203	Decorin-mediated regulation of fibrillin-1 in the kidney involves the insulin-like growth factor-I receptor and Mammalian target of rapamycin.
246	17200203	Decorin, a small leucine-rich proteoglycan, affects the synthesis of the elastic fiber component fibrillin-1 in the kidney via hitherto unknown mechanisms.
247	17200203	Here, we show that decorin binds to and induces phosphorylation of insulin-like growth factor-I (IGF-I) receptor in renal fibroblasts.
248	17200203	Inhibition of the IGF-I receptor tyrosine kinase and its downstream target phosphoinositide-3 kinase prevented decorin-mediated synthesis of fibrillin-1.
249	17200203	Furthermore, decorin induced phosphorylation of phosphoinositide-dependent kinase 1, protein kinase B/Akt, mammalian target of rapamycin (mTOR), and p70 S6 kinase.
250	17200203	Notably, IGF-I, which signals through the same pathway, also stimulated fibrillin-1 synthesis.
251	17200203	In streptozotocin-induced diabetes, IGF-I receptor was up-regulated in the kidneys from decorin-null mice.
252	17200203	However, this could not compensate for the decorin deficiency, resulting ultimately in decreased fibrillin-1 content.
253	17200203	This study provides evidence for the involvement of decorin and the IGF-I receptor/mTOR/p70 S6 kinase signaling pathway in the translational regulation of fibrillin-1.
254	17331859	Only one BG, phenformin, caused a concentration-related inhibition of proteoglycan synthesis under basal conditions and in the presence of transforming growth factor-beta1 (TGF-beta1), caused by an inhibition of proteoglycan core protein synthesis secondary to a reduction in total protein synthesis.
255	17331859	The TZDs--troglitazone (TRO), rosiglitazone (ROS), and pioglitazone (PIO) (10, 30, and 30 micromol/l, respectively)--inhibited proteoglycan biosynthesis and stimulated total proteoglycan core protein synthesis, while TRO alone inhibited overall protein synthesis.
256	17331859	Only one BG, phenformin, caused a concentration-related inhibition of proteoglycan synthesis under basal conditions and in the presence of transforming growth factor-beta1 (TGF-beta1), caused by an inhibition of proteoglycan core protein synthesis secondary to a reduction in total protein synthesis.
257	17331859	The TZDs--troglitazone (TRO), rosiglitazone (ROS), and pioglitazone (PIO) (10, 30, and 30 micromol/l, respectively)--inhibited proteoglycan biosynthesis and stimulated total proteoglycan core protein synthesis, while TRO alone inhibited overall protein synthesis.
258	17884968	Decorin, a proteoglycan that inhibits active transforming growth factor-beta, is increased in diabetic nephropathy; however, its functional significance is unclear.
259	17884968	In contrast to wild-type diabetic mice, which failed to develop significant nephropathy, the Dcn(-/-) diabetic mice developed a significant increase in albuminuria and plasma creatinine and a concurrent decrease in circulating adiponectin levels.
260	17884968	By immunohistochemistry, Dcn(-/-) diabetic mice exhibited significant increases in glomerular transforming growth factor-beta, type I collagen, macrophage infiltration, and Nox4.
261	17884968	Decorin, a proteoglycan that inhibits active transforming growth factor-beta, is increased in diabetic nephropathy; however, its functional significance is unclear.
262	17884968	In contrast to wild-type diabetic mice, which failed to develop significant nephropathy, the Dcn(-/-) diabetic mice developed a significant increase in albuminuria and plasma creatinine and a concurrent decrease in circulating adiponectin levels.
263	17884968	By immunohistochemistry, Dcn(-/-) diabetic mice exhibited significant increases in glomerular transforming growth factor-beta, type I collagen, macrophage infiltration, and Nox4.
264	17884968	Decorin, a proteoglycan that inhibits active transforming growth factor-beta, is increased in diabetic nephropathy; however, its functional significance is unclear.
265	17884968	In contrast to wild-type diabetic mice, which failed to develop significant nephropathy, the Dcn(-/-) diabetic mice developed a significant increase in albuminuria and plasma creatinine and a concurrent decrease in circulating adiponectin levels.
266	17884968	By immunohistochemistry, Dcn(-/-) diabetic mice exhibited significant increases in glomerular transforming growth factor-beta, type I collagen, macrophage infiltration, and Nox4.
267	18348167	By affinity coelectrophoresis (ACE), we found reduced affinities of heparin and KSPGs for glycated but not normal collagen, whereas the dermatan sulfate (DS)PGs decorin and biglycan bound similarly to both, and that the affinity of heparin for normal collagen decreased with increasing pH.
268	18348167	B-cells expressing the cell surface heparan sulfate PG syndecan-1 adhered well to normal but not glycated collagen, and endothelial cell migration was delayed on glycated collagen.
269	18484279	All agents decreased (35)S-SO(4) incorporation and reduced the size of the proteoglycans, decorin and biglycan as assessed by SDS-PAGE.
270	20083846	We discovered that streptozotocin-induced diabetes in Dcn(-/-) mice led to increased proteinuria associated with enhanced cyclin-dependent kinase inhibitor p27Kip1 in podocytes and tubular epithelial cells.
271	20083846	Notably, diabetic Dcn(-/-) kidneys revealed marked upregulation of the proinflammatory proteoglycan biglycan and enhanced infiltration of mononuclear cells.
272	20083846	We discovered that streptozotocin-induced diabetes in Dcn(-/-) mice led to increased proteinuria associated with enhanced cyclin-dependent kinase inhibitor p27Kip1 in podocytes and tubular epithelial cells.
273	20083846	Notably, diabetic Dcn(-/-) kidneys revealed marked upregulation of the proinflammatory proteoglycan biglycan and enhanced infiltration of mononuclear cells.
274	20136517	Recombinant decorin ameliorates the pulmonary structure alterations by down-regulating transforming growth factor-beta1/SMADS signaling in the diabetic rats.
275	20136517	This study investigated the role of transforming growth factor-beta1 (TGF-beta1)/Smads signaling in the alterations of lung structure and the effect of the exogenous decorin on lung structure modification in streptozotocin (STZ)-induced diabetic rats.
276	20136517	At 8, 16, and 28 weeks after STZ treatment, haematoxylin-eosin (H&E) and Masson's trichrome staining were performed to investigate the histological changes of diabetic lungs; Expressions of TGF-beta1 and collagen type IV in the diabetic lung were measured by Western blot and immunohistochemistry.
277	20136517	Phosphorylated Smad2 (P-Smad2), one of the major TGF-beta1 receptor substrates, was also detected using Western blot.
278	20136517	Exogenous decorin effectively suppressed the increased activities of TGF-beta1/Smads signaling and partly attenuated collagen deposits in the alveolar septum.
279	20136517	Increased activity of TGF-beta1/Smads signaling might play a critical role in the accumulation of collagen in the diabetic lung.
280	20136517	The protective effect of decorin in the diabetic lung is at least partly because of the down-regulation of the TGF-beta1/Smads signaling.
281	20136517	Recombinant decorin ameliorates the pulmonary structure alterations by down-regulating transforming growth factor-beta1/SMADS signaling in the diabetic rats.
282	20136517	This study investigated the role of transforming growth factor-beta1 (TGF-beta1)/Smads signaling in the alterations of lung structure and the effect of the exogenous decorin on lung structure modification in streptozotocin (STZ)-induced diabetic rats.
283	20136517	At 8, 16, and 28 weeks after STZ treatment, haematoxylin-eosin (H&E) and Masson's trichrome staining were performed to investigate the histological changes of diabetic lungs; Expressions of TGF-beta1 and collagen type IV in the diabetic lung were measured by Western blot and immunohistochemistry.
284	20136517	Phosphorylated Smad2 (P-Smad2), one of the major TGF-beta1 receptor substrates, was also detected using Western blot.
285	20136517	Exogenous decorin effectively suppressed the increased activities of TGF-beta1/Smads signaling and partly attenuated collagen deposits in the alveolar septum.
286	20136517	Increased activity of TGF-beta1/Smads signaling might play a critical role in the accumulation of collagen in the diabetic lung.
287	20136517	The protective effect of decorin in the diabetic lung is at least partly because of the down-regulation of the TGF-beta1/Smads signaling.
288	20136517	Recombinant decorin ameliorates the pulmonary structure alterations by down-regulating transforming growth factor-beta1/SMADS signaling in the diabetic rats.
289	20136517	This study investigated the role of transforming growth factor-beta1 (TGF-beta1)/Smads signaling in the alterations of lung structure and the effect of the exogenous decorin on lung structure modification in streptozotocin (STZ)-induced diabetic rats.
290	20136517	At 8, 16, and 28 weeks after STZ treatment, haematoxylin-eosin (H&E) and Masson's trichrome staining were performed to investigate the histological changes of diabetic lungs; Expressions of TGF-beta1 and collagen type IV in the diabetic lung were measured by Western blot and immunohistochemistry.
291	20136517	Phosphorylated Smad2 (P-Smad2), one of the major TGF-beta1 receptor substrates, was also detected using Western blot.
292	20136517	Exogenous decorin effectively suppressed the increased activities of TGF-beta1/Smads signaling and partly attenuated collagen deposits in the alveolar septum.
293	20136517	Increased activity of TGF-beta1/Smads signaling might play a critical role in the accumulation of collagen in the diabetic lung.
294	20136517	The protective effect of decorin in the diabetic lung is at least partly because of the down-regulation of the TGF-beta1/Smads signaling.
295	20136517	Recombinant decorin ameliorates the pulmonary structure alterations by down-regulating transforming growth factor-beta1/SMADS signaling in the diabetic rats.
296	20136517	This study investigated the role of transforming growth factor-beta1 (TGF-beta1)/Smads signaling in the alterations of lung structure and the effect of the exogenous decorin on lung structure modification in streptozotocin (STZ)-induced diabetic rats.
297	20136517	At 8, 16, and 28 weeks after STZ treatment, haematoxylin-eosin (H&E) and Masson's trichrome staining were performed to investigate the histological changes of diabetic lungs; Expressions of TGF-beta1 and collagen type IV in the diabetic lung were measured by Western blot and immunohistochemistry.
298	20136517	Phosphorylated Smad2 (P-Smad2), one of the major TGF-beta1 receptor substrates, was also detected using Western blot.
299	20136517	Exogenous decorin effectively suppressed the increased activities of TGF-beta1/Smads signaling and partly attenuated collagen deposits in the alveolar septum.
300	20136517	Increased activity of TGF-beta1/Smads signaling might play a critical role in the accumulation of collagen in the diabetic lung.
301	20136517	The protective effect of decorin in the diabetic lung is at least partly because of the down-regulation of the TGF-beta1/Smads signaling.
302	20571025	Thrombin stimulation of proteoglycan synthesis in vascular smooth muscle is mediated by protease-activated receptor-1 transactivation of the transforming growth factor beta type I receptor.
303	20571025	One component of classical G-protein-coupled receptor (GPCR) signaling invokes transactivation of protein tyrosine kinase receptors such as the epidermal growth factor receptor.
304	20571025	We have used the model of proteoglycan synthesis to demonstrate that the signaling paradigm of GPCR signaling can be extended to include the transactivation of serine/threonine receptor, specifically the TGF-beta type I receptor (TbetaRI) also known as activin-like kinase (ALK) V.
305	20571025	Thrombin stimulated elongation of GAG chains and increased proteoglycan core protein expression and these responses were blocked by the TbetaRI antagonist, SB431542 and TbetaRI siRNA knockdown, as well as several protease-activated receptor (PAR)-1 antagonists.
306	20571025	The canonical downstream response to TGF-beta is increased C-terminal phosphorylation of the transcription factor Smad2 generating phospho-Smad2C (phosphorylation of Smad2 C-terminal region).
307	20571025	The proteolytically inactive thrombin mimetic thrombin-receptor activating peptide also stimulated an increase in cytosolic phospho-Smad2C.
308	21723246	The renal proteoglycans biglycan and decorin were detectable in glomeruli, with a significant increase in renal biglycan content in diabetic mice on the high-cholesterol diet.
309	21723246	Renal biglycan and renal apolipoprotein B were colocalized, and regression analyses showed a significant relation between renal biglycan and renal apolipoprotein B content.
310	22074948	Mouse resistin modulates adipogenesis and glucose uptake in 3T3-L1 preadipocytes through the ROR1 receptor.
311	22074948	Mouse resistin, a cysteine-rich protein primarily secreted from mature adipocytes, is involved in insulin resistance and type 2 diabetes.
312	22074948	Human resistin, however, is mainly secreted by immune mononuclear cells, and it competes with lipopolysaccharide for the binding to Toll-like receptor 4, which could mediate some of the well-known proinflammatory effects of resistin in humans.
313	22074948	Thus, a recent work identifies an isoform of Decorin (Δ Decorin) as a functional resistin receptor in adipocyte progenitors that may regulate white adipose tissue expansion.
314	22074948	We have demonstrated an interaction of mouse resistin with specific domains of the extracellular region of the ROR1 receptor.
315	22074948	This interaction results in the inhibition of ROR1 phosphorylation, modulates ERK1/2 phosphorylation, and regulates suppressor of cytokine signaling 3, glucose transporter 4, and glucose transporter 1 expression.
316	22074948	Moreover, mouse resistin modulates glucose uptake and promotes adipogenesis of 3T3-L1 cells through ROR1.
317	22074948	In summary, our results identify mouse resistin as a potential inhibitory ligand for the receptor ROR1 and demonstrate, for the first time, that ROR1 plays an important role in adipogenesis and glucose homeostasis in 3T3-L1 cells.
318	22074948	These data open a new line of research that could explain important questions about the resistin mechanism of action in adipogenesis and in the development of insulin resistance.
319	22532774	Biglycan is highly similar in structure to decorin, therefore we hypothesized it would have a similar expression profile and role to decorin in adipose tissue.
320	22532774	Collectively, our data suggest that the small leucine-rich proteoglycan family proteins biglycan and decorin may play a role in the development of obesity and T2D, possibly by facilitating expansion of adipose tissue mass.
321	22532774	Biglycan is highly similar in structure to decorin, therefore we hypothesized it would have a similar expression profile and role to decorin in adipose tissue.
322	22532774	Collectively, our data suggest that the small leucine-rich proteoglycan family proteins biglycan and decorin may play a role in the development of obesity and T2D, possibly by facilitating expansion of adipose tissue mass.
323	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
324	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
325	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
326	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
327	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
328	23193185	The possibility that human decorin is a human resistin receptor should be pursued.
329	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
330	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
331	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
332	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
333	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
334	23193185	The possibility that human decorin is a human resistin receptor should be pursued.
335	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
336	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
337	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
338	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
339	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
340	23193185	The possibility that human decorin is a human resistin receptor should be pursued.
341	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
342	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
343	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
344	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
345	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
346	23193185	The possibility that human decorin is a human resistin receptor should be pursued.
347	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
348	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
349	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
350	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
351	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
352	23193185	The possibility that human decorin is a human resistin receptor should be pursued.
353	23193185	Plasma resistin is associated with single nucleotide polymorphisms of a possible resistin receptor, the decorin gene, in the general Japanese population.
354	23193185	Decorin is a multifunctional proteoglycan, and its isoform, lacking 14 amino acids from the N terminal region of mature core decorin, recently was identified as a resistin receptor in mice.
355	23193185	To examine whether SNPs in the vicinity of the human decorin gene (DCN) are associated with plasma resistin, we cross-sectionally analyzed six tag SNPs selected around DCN in the same linkage disequilibrium block in 2,078 community-dwelling Japanese subjects.
356	23193185	Plasma resistin was associated with the rs7139228, rs7956537, rs516115, and rs3138167 genotypes in DCN.
357	23193185	Therefore, plasma resistin was associated with some tag SNPs around DCN in the general Japanese population.
358	23193185	The possibility that human decorin is a human resistin receptor should be pursued.