# |
PMID |
Sentence |
1 |
8033591
|
Both epidermal growth factor (EGF) and basic fibroblast growth factor (bFGF) enhanced protein accumulation in cells of diabetic origin, but not in cells of nondiabetic origin.
|
2 |
8033591
|
Analysis of radiolabeled proteins in the secreted fraction by sodium dodecyl sulfate (SDS) polyacrylamide gel electrophoresis (PAGE) revealed prominent protein bands at 220 and 49.5 kD in both diabetic and nondiabetic cultures that were identified by immunoblot analysis as fibronectin and a mixture of secreted protein acidic and rich in cysteine (SPARC) and plasminogen activator inhibitor-1 (PAI-1), respectively.
|
3 |
8033591
|
Our studies support unique differences in protein expression in cells of diabetic vs. nondiabetic origin in response to EGF and bFGF and identify two proteins exclusively expressed by cells of diabetic origin.
|
4 |
8804356
|
Using specific antibodies, we compared the immunolocalization of the vascular heparan sulfate proteoglycan (HSPG)-binding protein vitronectin (VN), HSPG, basic fibroblast growth factor, and collagen type 1 in retinae prepared from 11-month-old diabetic and nondiabetic Wistar rats.
|
5 |
8804356
|
Because binding of glycosaminoglycans, as well as interaction of type I collagen and the morphoregulatory proteins osteonectin and tenascin with AGE-VN, were reduced to at least 50% of control, alteration of basic residues in the heparin-binding domain of VN is plausible.
|
6 |
9080393
|
Characterization of IGFBP-3, PAI-1 and SPARC mRNA expression in senescent fibroblasts.
|
7 |
9080393
|
The RNA species encoded by IGFBP-3 (insulin-like growth factor binding protein-3), PAI-1 (plasminogen activator inhibitor-1) and SPARC (secreted protein-acidic and rich in cysteine; a.k.a. osteonectin) are overexpressed in senescent human diploid fibroblasts (HDF).
|
8 |
9080393
|
Characterization of the rates of transcription and the levels of message stability of these genes in early passage (young) versus late passage (old) HDF revealed that IGFBP-3, PAI-1 and SPARC are coordinately overexpressed but not regulated by a unique or simple mechanism encompassing all three transcripts.
|
9 |
9080393
|
Characterization of IGFBP-3, PAI-1 and SPARC mRNA expression in senescent fibroblasts.
|
10 |
9080393
|
The RNA species encoded by IGFBP-3 (insulin-like growth factor binding protein-3), PAI-1 (plasminogen activator inhibitor-1) and SPARC (secreted protein-acidic and rich in cysteine; a.k.a. osteonectin) are overexpressed in senescent human diploid fibroblasts (HDF).
|
11 |
9080393
|
Characterization of the rates of transcription and the levels of message stability of these genes in early passage (young) versus late passage (old) HDF revealed that IGFBP-3, PAI-1 and SPARC are coordinately overexpressed but not regulated by a unique or simple mechanism encompassing all three transcripts.
|
12 |
9080393
|
Characterization of IGFBP-3, PAI-1 and SPARC mRNA expression in senescent fibroblasts.
|
13 |
9080393
|
The RNA species encoded by IGFBP-3 (insulin-like growth factor binding protein-3), PAI-1 (plasminogen activator inhibitor-1) and SPARC (secreted protein-acidic and rich in cysteine; a.k.a. osteonectin) are overexpressed in senescent human diploid fibroblasts (HDF).
|
14 |
9080393
|
Characterization of the rates of transcription and the levels of message stability of these genes in early passage (young) versus late passage (old) HDF revealed that IGFBP-3, PAI-1 and SPARC are coordinately overexpressed but not regulated by a unique or simple mechanism encompassing all three transcripts.
|
15 |
10587515
|
Reduced bone density is accompanied by increased activity of osteoclasts and upregulation of genes that are related to osteoblast differentiation, including osteopontin, osteonectin, and osteocalcin.
|
16 |
12577314
|
Glomerular mesangial cells both synthesize and respond to insulin-like growth factor-1 (IGF-1).
|
17 |
12577314
|
We have reported that primary glomerular mesangial cells derived from SPARC-null mice exhibit an accelerated rate of proliferation and produce substantially decreased levels of transforming growth factor beta1 (TGF-beta1) in comparison to their wild-type counterparts (Francki et al. [1999] J.
|
18 |
12577314
|
SPARC-null mesangial cells produce increased amounts of IGF-1 and -2, as well as IGF-1 receptor (IGF-1R) in comparison to wild-type cells.
|
19 |
12577314
|
Addition of recombinant SPARC to SPARC-null cells inhibited IGF-1-stimulated mitogen activated protein kinase (MAPK) activation and DNA synthesis.
|
20 |
12577314
|
We also show that the observed accelerated rate of basal and IGF-1-stimulated proliferation in mesangial cells derived from SPARC-null animals is due, at least in part, to markedly diminished levels of cyclin D1 and the cyclin-dependent kinase (cdk) inhibitors p21 and p27.
|
21 |
12660331
|
SPARC (Secreted Protein, Acidic and Rich in Cysteine) is a matricellular protein that inhibits mesangial cell proliferation and also affects production of extracellular matrix (ECM) by regulating transforming growth factor-beta1 (TGF-beta1) and type I collagen in mesangial cells.
|
22 |
12660331
|
Deposition of type I and IV collagen and laminin was evaluated by IHC, and TGF-beta 1 mRNA was assessed by ISH.
|
23 |
12660331
|
Further characterization of diabetic SPARC-null mice revealed diminished glomerular deposition of type IV collagen and laminin, and diminished interstitial deposition of type I and type IV collagen correlated with decreases in TGF-beta 1 mRNA compared with WT diabetic mice.
|
24 |
12660331
|
These observations suggest that SPARC contributes to glomerulosclerosis and tubulointerstitial damage in response to hyperglycemia through increasing TGF-beta 1 expression in this model of chronic DN.
|
25 |
12660331
|
SPARC (Secreted Protein, Acidic and Rich in Cysteine) is a matricellular protein that inhibits mesangial cell proliferation and also affects production of extracellular matrix (ECM) by regulating transforming growth factor-beta1 (TGF-beta1) and type I collagen in mesangial cells.
|
26 |
12660331
|
Deposition of type I and IV collagen and laminin was evaluated by IHC, and TGF-beta 1 mRNA was assessed by ISH.
|
27 |
12660331
|
Further characterization of diabetic SPARC-null mice revealed diminished glomerular deposition of type IV collagen and laminin, and diminished interstitial deposition of type I and type IV collagen correlated with decreases in TGF-beta 1 mRNA compared with WT diabetic mice.
|
28 |
12660331
|
These observations suggest that SPARC contributes to glomerulosclerosis and tubulointerstitial damage in response to hyperglycemia through increasing TGF-beta 1 expression in this model of chronic DN.
|
29 |
19509023
|
Regulation of the fibrosis and angiogenesis promoter SPARC/osteonectin in human adipose tissue by weight change, leptin, insulin, and glucose.
|
30 |
19924377
|
MSC cultured in osteogenic medium increased expression of osteonectin, Runt-related transcription factor 2 (RUNX-2), osteocalcin, and alkaline phosphatase.
|
31 |
19924377
|
Additionally, the effect of HO-1 on osteoblasts appears different to that seen in adipocyte stem cells.
|
32 |
19924377
|
Moreover, glucose (30 mM) inhibited osteoblast differentiation, as evidenced by decreased bone morphogenetic protein (BMP)-2, osteonectin, osteocalcin, and osteoprotegerin (OPG).
|
33 |
19924377
|
Increased HO-1 expression increased the levels of osteonectin, OPG, and BMP-2.
|
34 |
19924377
|
Inhibition of HO activity prevented the increase in osteonectin and potentiated the decrease of osteocalcin and OPG in cells exposed to high glucose levels.
|
35 |
19924377
|
Furthermore, targeting HO-1 expression increased pAMPK and endothelial nitric oxide synthase (eNOS) and restored osteoblastic markers.
|
36 |
19924377
|
MSC cultured in osteogenic medium increased expression of osteonectin, Runt-related transcription factor 2 (RUNX-2), osteocalcin, and alkaline phosphatase.
|
37 |
19924377
|
Additionally, the effect of HO-1 on osteoblasts appears different to that seen in adipocyte stem cells.
|
38 |
19924377
|
Moreover, glucose (30 mM) inhibited osteoblast differentiation, as evidenced by decreased bone morphogenetic protein (BMP)-2, osteonectin, osteocalcin, and osteoprotegerin (OPG).
|
39 |
19924377
|
Increased HO-1 expression increased the levels of osteonectin, OPG, and BMP-2.
|
40 |
19924377
|
Inhibition of HO activity prevented the increase in osteonectin and potentiated the decrease of osteocalcin and OPG in cells exposed to high glucose levels.
|
41 |
19924377
|
Furthermore, targeting HO-1 expression increased pAMPK and endothelial nitric oxide synthase (eNOS) and restored osteoblastic markers.
|
42 |
19924377
|
MSC cultured in osteogenic medium increased expression of osteonectin, Runt-related transcription factor 2 (RUNX-2), osteocalcin, and alkaline phosphatase.
|
43 |
19924377
|
Additionally, the effect of HO-1 on osteoblasts appears different to that seen in adipocyte stem cells.
|
44 |
19924377
|
Moreover, glucose (30 mM) inhibited osteoblast differentiation, as evidenced by decreased bone morphogenetic protein (BMP)-2, osteonectin, osteocalcin, and osteoprotegerin (OPG).
|
45 |
19924377
|
Increased HO-1 expression increased the levels of osteonectin, OPG, and BMP-2.
|
46 |
19924377
|
Inhibition of HO activity prevented the increase in osteonectin and potentiated the decrease of osteocalcin and OPG in cells exposed to high glucose levels.
|
47 |
19924377
|
Furthermore, targeting HO-1 expression increased pAMPK and endothelial nitric oxide synthase (eNOS) and restored osteoblastic markers.
|
48 |
19924377
|
MSC cultured in osteogenic medium increased expression of osteonectin, Runt-related transcription factor 2 (RUNX-2), osteocalcin, and alkaline phosphatase.
|
49 |
19924377
|
Additionally, the effect of HO-1 on osteoblasts appears different to that seen in adipocyte stem cells.
|
50 |
19924377
|
Moreover, glucose (30 mM) inhibited osteoblast differentiation, as evidenced by decreased bone morphogenetic protein (BMP)-2, osteonectin, osteocalcin, and osteoprotegerin (OPG).
|
51 |
19924377
|
Increased HO-1 expression increased the levels of osteonectin, OPG, and BMP-2.
|
52 |
19924377
|
Inhibition of HO activity prevented the increase in osteonectin and potentiated the decrease of osteocalcin and OPG in cells exposed to high glucose levels.
|
53 |
19924377
|
Furthermore, targeting HO-1 expression increased pAMPK and endothelial nitric oxide synthase (eNOS) and restored osteoblastic markers.
|
54 |
19949837
|
High glucose stimulates adipogenic and inhibits osteogenic differentiation in MG-63 cells through cAMP/protein kinase A/extracellular signal-regulated kinase pathway.
|
55 |
19949837
|
Here, we showed that high glucose suppressed the cell growth, mineralization, and expression of osteogenic markers including Runx2, collagen I, osteocalcin, osteonectin, but inversely promoted expression of adipogenic markers including PPARgamma, aP2, resistin, and adipsin.
|
56 |
20195270
|
Notably, SPARC is linked to human obesity; SPARC derived from adipose tissue is associated with insulin resistance and secretion of SPARC by adipose tissue is increased by insulin and the adipokine leptin.
|
57 |
22317926
|
Starting 2012: Sod2, DGAT1, p53, SPARC, QTL and reprogramming in aging.
|
58 |
22802913
|
SPARC is a 43 kDa collagen-binding protein secreted from several different cell types into the extracellular matrix and has been shown to be anti-proliferative and counter-adhesive in vitro.
|
59 |
23454256
|
Interleukin-1 has opposing effects on connective tissue growth factor and tenascin-C expression in human cardiac fibroblasts.
|
60 |
23454256
|
We investigated the effects of pro-inflammatory cytokines on matricellular protein expression in cultured human CF. cDNA array analysis of matricellular proteins revealed that interleukin-1α (IL-1α, 10ng/ml, 6h) down-regulated connective tissue growth factor (CTGF/CCN2) mRNA by 80% and up-regulated tenascin-C (TNC) mRNA levels by 10-fold in human CF, without affecting expression of thrombospondins 1-3, osteonectin or osteopontin.
|
61 |
23454256
|
In contrast, tumor necrosis factor α (TNFα) did not modulate CCN2 expression and had only a modest stimulatory effect on TNC levels.
|
62 |
23454256
|
Signaling pathway inhibitor studies suggested an important role for the p38 MAPK pathway in suppressing CCN2 expression in response to IL-1α.
|
63 |
23454256
|
In contrast, multiple signaling pathways (p38, JNK, PI3K/Akt and NFκB) contributed to IL-1α-induced TNC expression.
|
64 |
23454256
|
In conclusion, IL-1α reduced CCN2 expression and increased TNC expression in human CF.
|
65 |
23670848
|
In the present study, we demonstrate a prominent yet transient increase in SPARC mRNA and protein content during skeletal muscle regeneration that correlates with the expression profile of specific muscle factors like MyoD, Myf5, Myf6, Myogenin, NCAM, CD34, and M-Cadherin, all known to be implicated in satellite cell activation/proliferation following muscle damage.
|
66 |
23670848
|
SPARC overexpression almost completely abolished myogenic differentiation in these cultures as determined by substantially reduced levels of myogenic factors (Pax7, Myf5, Myod, Mef2B, Myogenin, and Myostatin) and a lack of multinucleated myotubes.
|
67 |
23670848
|
In the present study, we demonstrate a prominent yet transient increase in SPARC mRNA and protein content during skeletal muscle regeneration that correlates with the expression profile of specific muscle factors like MyoD, Myf5, Myf6, Myogenin, NCAM, CD34, and M-Cadherin, all known to be implicated in satellite cell activation/proliferation following muscle damage.
|
68 |
23670848
|
SPARC overexpression almost completely abolished myogenic differentiation in these cultures as determined by substantially reduced levels of myogenic factors (Pax7, Myf5, Myod, Mef2B, Myogenin, and Myostatin) and a lack of multinucleated myotubes.
|
69 |
23935929
|
Microarray analysis revealed that SPARC depletion upregulated the expression of interleukin 11 (IL11), KISS1, insulin-like growth factor binding protein 4 (IGFBP4), collagen type I alpha 1 (COLIA1), matrix metallopeptidase 9 (MMP9), and downregulated the expression of the alpha polypeptide of chorionic gonadotropin (CGA), MMP1, gap junction protein alpha 1 (GJA1), et al.
|