Ignet

Gene Information

Gene symbol: GORASP1

Gene name: golgi reassembly stacking protein 1, 65kDa

HGNC ID: 16769

Synonyms: GRASP65, P65, FLJ23443

Related Genes

#	Gene Symbol	Number of hits
1	ACTN4	1 hits
2	AGT	1 hits
3	AKT1	1 hits
4	BCL2L1	1 hits
5	CASP3	1 hits
6	CASP8	1 hits
7	CCL2	1 hits
8	CD40	1 hits
9	CD68	1 hits
10	CTSL1	1 hits
11	FAS	1 hits
12	FASLG	1 hits
13	FOXO4	1 hits
14	HPS1	1 hits
15	ICAM1	1 hits
16	IL17A	1 hits
17	IL1B	1 hits
18	IL6	1 hits
19	IL8	1 hits
20	MAPK1	1 hits
21	NFATC3	1 hits
22	NFKB1	1 hits
23	NOTCH4	1 hits
24	NPHS1	1 hits
25	PPARA	1 hits
26	PPARGC1A	1 hits
27	RELA	1 hits
28	SIRT1	1 hits
29	SMAD2	1 hits
30	SMAD3	1 hits
31	STAT3	1 hits
32	SYNPO	1 hits
33	TGFA	1 hits
34	TLR2	1 hits
35	TLR9	1 hits
36	TNF	1 hits
37	TNS1	1 hits
38	TP53	1 hits
39	UCHL1	1 hits

Related Sentences

#	PMID	Sentence
1	33359498	Mechanistically, diabetes and HIV-1 synergistically increased the glomerular expression of microRNA-34a (miR-34a), thereby reducing the expression of Sirtuin-1 (SIRT1) deacetylase.
2	33359498	These changes were also associated with increased acetylation and activation of p53 and p65 NF-κB and with enhanced expression of senescence and inflammatory markers.
3	32657157	We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys.
4	32657157	We have previously shown that the acetylation and activation of key inflammatory regulators, NF-κB p65 and STAT3, were increased in HIVAN kidneys.
5	32657157	Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN.
6	32657157	Here, we demonstrate the key role of sirtuin 1 (SIRT1) deacetylase in the regulation of NF-κB and STAT3 activity in HIVAN.
7	32657157	We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes.
8	32657157	We found that SIRT1 expression was reduced in the glomeruli of human and mouse HIVAN kidneys and that HIV-1 gene expression was associated with reduced SIRT1 expression and increased acetylation of NF-κB p65 and STAT3 in cultured podocytes.
9	32657157	Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression.
10	32657157	Finally, we showed that the reduction in SIRT1 expression by HIV-1 is in part mediated through miR-34a expression.
11	32657157	Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease.
12	32657157	Together, our data provide a new mechanism of SIRT1 regulation and its downstream effects in HIV-1-infected kidney cells and indicate that SIRT1/miR-34a are potential drug targets to treat HIV-related kidney disease.
13	32537005	In vitro, IL-17 induced podocyte apoptosis and reduced the expression of markers associated with podocytes, including Wilm's tumor 1, nephrin, synaptopodin and podocalyxin, whilst increasing the levels of Fas, Fas ligand (FasL), active-caspase-8, active-caspase-3 and phosphorylated-p65.
14	32537005	However, treatment with helenalin, a NF-κB inhibitor, decreased p65 phosphorylation, attenuated IL-17-induced podocyte apoptosis and suppressed the IL-17-activated Fas/FasL/caspase-8/caspase-3 apoptotic pathway.
15	32537005	Taken together, these observations suggest that IL-17 was highly expressed in renal tissues from patients with PNS, where it induced podocyte apoptosis by activating the Fas/FasL/caspase-8/caspase-3 apoptotic pathway in a NF-κB-dependent manner.
16	31798708	In vitro treatment with OV on LPS-stimulated mouse podocyte cell line MPC5 did not affect TLR2 expression but interrupted the interaction between TLR2 and its downstream adaptor MyD88, resulting in the reduction of inflammatory cytokines IL-6 and TNF-α expression.
17	31798708	Additionally, inflammatory cytokines TNF-α, IL-6 and IL-1β expression were also significantly reduced in mice with OV treatment.
18	31798708	Signaling pathway analysis further demonstrated that OV treatment did not affect the expression of TLR2 and p65 but suppressed p65 phosphorylation.
19	31727625	Using luciferase reporter assays, we did not observe activation of the NOTCH4 promoter with the HIV protein Nef in podocytes.
20	31727625	Further, we observed upregulated expression of a gamma secretase complex protein, presenilin 1, but not Notch4, in podocytes infected with an HIV-1 expression construct.
21	31727625	Consistent with the diminished inflammation, kidneys from Notch4^d1/Tg26⁺ mice also showed a significant decrease in expression of the inflammatory cytokine transcripts Il-6 and Ccl2, as well as the master inflammatory transcription factor NF-κB (Nfkb1 transcripts and p65 protein).
22	31638199	Critical roles of PI3K/Akt/NF‑κB survival axis in angiotensin II‑induced podocyte injury.
23	31638199	Critical roles of PI3K/Akt/NF‑κB survival axis in angiotensin II‑induced podocyte injury.
24	31638199	Numerous studies have reported that angiotensin (Ang) II, nephrin, and podocin serve pivotal roles in podocyte injury, and thus can lead to the occurrence of proteinuria and the progression of kidney diseases.
25	31638199	Numerous studies have reported that angiotensin (Ang) II, nephrin, and podocin serve pivotal roles in podocyte injury, and thus can lead to the occurrence of proteinuria and the progression of kidney diseases.
26	31638199	This study aimed to investigate the effects of Ang II on the production of nephrin and podocin, and their relationship with podocyte injury.
27	31638199	This study aimed to investigate the effects of Ang II on the production of nephrin and podocin, and their relationship with podocyte injury.
28	31638199	We also aimed to determine whether nephrin, podocin and caspase‑9 production depends on the PI3K/Akt/nuclear factor (NF)‑κB signaling pathway in cultured mouse podocytes.
29	31638199	We also aimed to determine whether nephrin, podocin and caspase‑9 production depends on the PI3K/Akt/nuclear factor (NF)‑κB signaling pathway in cultured mouse podocytes.
30	31638199	Cells were treated with 10‑6 mol/l of Ang II and/or LY294002 (inhibitor of Akt) or 740Y‑P (activator of PI3K) for 48 h to detect Akt, phosphorylated (phospho)‑Akt, p65 NF‑κB, and phospho‑p65 NF‑κB, nephrin, podocin and caspase‑9 expression, and podocyte apoptosis.
31	31638199	Cells were treated with 10‑6 mol/l of Ang II and/or LY294002 (inhibitor of Akt) or 740Y‑P (activator of PI3K) for 48 h to detect Akt, phosphorylated (phospho)‑Akt, p65 NF‑κB, and phospho‑p65 NF‑κB, nephrin, podocin and caspase‑9 expression, and podocyte apoptosis.
32	31638199	Ang II decreased phospho‑Akt, phospho‑p65 NF‑κB, nephrin, and podocin and increased caspase‑9 expression, while podocyte apoptosis was promoted.
33	31638199	Ang II decreased phospho‑Akt, phospho‑p65 NF‑κB, nephrin, and podocin and increased caspase‑9 expression, while podocyte apoptosis was promoted.
34	31638199	LY294002 further enhanced Ang II‑induced downregulation of Akt and p65 NF‑κB activation, as well as upregulation of caspase‑9 mRNA and protein, and promoted the apoptosis of podocytes.
35	31638199	LY294002 further enhanced Ang II‑induced downregulation of Akt and p65 NF‑κB activation, as well as upregulation of caspase‑9 mRNA and protein, and promoted the apoptosis of podocytes.
36	31638199	Of note, 740Y‑P restored Ang II‑induced downregulation of Akt and p65 NF‑κB activation, and upregulation of caspase‑9, and decreased podocyte apoptosis.
37	31638199	Of note, 740Y‑P restored Ang II‑induced downregulation of Akt and p65 NF‑κB activation, and upregulation of caspase‑9, and decreased podocyte apoptosis.
38	31638199	The data suggested that Ang II could regulate the expression of nephrin, podocin and caspase‑9.
39	31638199	The data suggested that Ang II could regulate the expression of nephrin, podocin and caspase‑9.
40	31638199	Collectively, our findings suggested that the PI3K/Akt/NF‑κB survival axis may serve a pivotal role in podocyte injury.
41	31638199	Collectively, our findings suggested that the PI3K/Akt/NF‑κB survival axis may serve a pivotal role in podocyte injury.
42	29860655	Cisplatin increased serum urea and serum creatinine levels and caused an increase in tubular necrosis scores (TNS), HPS, NF-κB/p65, 8-OHdG, and caspase-3 expressions (p < 0.05).
43	29860655	Cisplatin increased serum urea and serum creatinine levels and caused an increase in tubular necrosis scores (TNS), HPS, NF-κB/p65, 8-OHdG, and caspase-3 expressions (p < 0.05).
44	29860655	Amifostine, curcumin, and melatonin reduced the increases in serum urea and serum creatinine levels following cisplatin administration and reduced the levels of TNS, HPS, NF-κB/p65, 8-OHdG, and caspase-3 expressions (p < 0.05).
45	29860655	Amifostine, curcumin, and melatonin reduced the increases in serum urea and serum creatinine levels following cisplatin administration and reduced the levels of TNS, HPS, NF-κB/p65, 8-OHdG, and caspase-3 expressions (p < 0.05).
46	29218112	Consistently, Triptolide also prevented TGF-β-induced signaling activation of MAPK p38, NFkB (p65) and calcineurin/NFATC3, which are known to be downstream mediators of podocyte injury.
47	28615249	Finally, we confirmed that Pod-Sirt1^RNAi glomeruli were associated with reduced activation of the transcription factors peroxisome proliferator-activated receptor (PPAR)-α coactivador-1 (PGC1α)/PPARγ, forkhead box O (FOXO)3, FOXO4, and p65 NF-κB, through SIRT1-mediated deacetylation.
48	26934958	Since TLR9 activates p38 MAPK and NFkB that are known to mediate podocyte apoptosis, we hypothesized that TLR9 induces podocyte apoptosis in glomerular diseases.
49	26934958	Since TLR9 activates p38 MAPK and NFkB that are known to mediate podocyte apoptosis, we hypothesized that TLR9 induces podocyte apoptosis in glomerular diseases.
50	26934958	Prevention of TLR9 upregulation by siRNA significantly attenuated NFκB p65 or p38 activity and apoptosis, demonstrating that TLR9 mediates podocyte apoptosis.
51	26934958	Prevention of TLR9 upregulation by siRNA significantly attenuated NFκB p65 or p38 activity and apoptosis, demonstrating that TLR9 mediates podocyte apoptosis.
52	26934958	We next showed that endogenous mitochondrial DNA (mtDNA), whose CpG motifs are also unmethylated, is the ligand for TLR9, because PAN induced mtDNA accumulation in endolysosomes where TLR9 is localized, overexpression of endolysosomal DNase 2 attenuated PAN-induced p38 or p65 activity and podocyte apoptosis, and DNase 2 silencing was sufficient to activate p38 or p65 and induce apoptosis.
53	26934958	We next showed that endogenous mitochondrial DNA (mtDNA), whose CpG motifs are also unmethylated, is the ligand for TLR9, because PAN induced mtDNA accumulation in endolysosomes where TLR9 is localized, overexpression of endolysosomal DNase 2 attenuated PAN-induced p38 or p65 activity and podocyte apoptosis, and DNase 2 silencing was sufficient to activate p38 or p65 and induce apoptosis.
54	26931472	In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation.
55	26931472	In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation.
56	26931472	In podocytes, SIRT1 regulates the expression of important genes such as PGC-1α, Foxo4, p65 and STAT3, which act to maintain podocyte function by modulating the levels of histone acetylation.
57	26931472	Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes.
58	26931472	Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes.
59	26931472	Here, we confirmed that SIRT1 protects podocytes by maintaining PGC-1α via its deacetylase-activated transcriptional activity in mitochondria and podocytes.
60	26931472	We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy.
61	26931472	We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy.
62	26931472	We then showed that the alteration of Foxo4 (forkhead box O4) acetylation and decrease in SIRT1 promote podocyte apoptosis in diabetic nephropathy, resulting in the gradual development of diabetic nephropathy.
63	26931472	Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes.
64	26931472	Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes.
65	26931472	Next, we showed that advanced glycation end products (AGEs) induced p65 and STAT3 acetylation in human podocytes.
66	26931472	Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3.
67	26931472	Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3.
68	26931472	Decreased Sirt1 activity in podocytes results in the development of proteinuria and kidney injury via the acetylation of p65 and STAT3.
69	26931472	SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton.
70	26931472	SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton.
71	26931472	SIRT1 protects podocytes and prevents glomerular injury by deacetylating cortactin and changing cortactin localization, thereby maintaining the integrity of the actin cytoskeleton.
72	26876299	In addition, GSK3β knockout diminished ADR-induced NFκB RelA/p65 phosphorylation selectively at serine 467; suppressed de novo expression by podocytes of NFκB-dependent podocytopathic mediators, including B7-1, cathepsin L, and MCP-1; but barely affected the induction of NFκB target pro-survival factors, such as Bcl-xL.
73	25976522	It has been demonstrated that the expression of ubiquitin carboxy-terminal hydrolase L1 (UCH-L1) is increased in injured podocytes in a number of types of glomerulonephritis.
74	25976522	Increases in the expression of phosphorylated NF-κB at p65 and UCH-L1 were detected using immunohistochemical analysis of kidney biopsy tissues from 56 cases of nephritis, including immunoglobulin A nephropathy, membranous glomerulonephritis and lupus nephritis.
75	25879629	These were associated with upregulation of tumor necrosis factor (TNF)-α and transforming growth factor (TGF)-β/activins mRNAs and activation of nuclear factor (NF)-κB p65 and Smad2/3.
76	25629551	In vitro, lipopolysaccharide (LPS) or adriamycin (ADR) elicited podocyte injury and cytoskeletal disruption, associated with NFκB activation and induced expression of NFκB target molecules, including pro-survival Bcl-xL and podocytopathic mediators like MCP-1, cathepsin L, and B7-1.
77	25629551	Mechanistically, GSK3β was sufficient and essential for RelA/p65 phosphorylation, specifically at serine 467, which specifies the expression of selective NFκB target molecules, including podocytopathic mediators, but not Bcl-xL.
78	25411248	We demonstrate here that stable knockdown of ACTN4 in podocytes significantly reduces TNFα-mediated induction of NF-κB target genes, including IL-1β and NPHS1, and activation of an NF-κB-driven reporter without interfering with p65 nuclear translocation.
79	25411248	We demonstrate here that stable knockdown of ACTN4 in podocytes significantly reduces TNFα-mediated induction of NF-κB target genes, including IL-1β and NPHS1, and activation of an NF-κB-driven reporter without interfering with p65 nuclear translocation.
80	25411248	Mechanistically, IκBα blocks the association of ACTN4 and p65 in the cytosol.
81	25411248	Mechanistically, IκBα blocks the association of ACTN4 and p65 in the cytosol.
82	25411248	In response to TNFα, both NF-κB subunits p65 and p50 translocate to the nucleus, where they bind and recruit ACTN4 to their targeted promoters, IL-1β and IL-8.
83	25411248	In response to TNFα, both NF-κB subunits p65 and p50 translocate to the nucleus, where they bind and recruit ACTN4 to their targeted promoters, IL-1β and IL-8.
84	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
85	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
86	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
87	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
88	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
89	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
90	24608443	Here, we determined the roles of Sirt1 and the effect of NF-κB (p65) and STAT3 acetylation in DN.
91	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
92	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
93	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
94	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
95	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
96	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
97	24608443	We found that acetylation of p65 and STAT3 was increased in both mouse and human diabetic kidneys.
98	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
99	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
100	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
101	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
102	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
103	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
104	24608443	In human podocytes, advanced glycation end products (AGEs) induced p65 and STAT3 acetylation and overexpression of acetylation-incompetent mutants of p65 and STAT3 abrogated AGE-induced expression of NF-κB and STAT3 target genes.
105	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
106	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
107	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
108	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
109	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
110	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
111	24608443	Inhibition of AGE formation in db/db mice by pyridoxamine treatment attenuated proteinuria and podocyte injury, restored SIRT1 expression, and reduced p65 and STAT3 acetylation.
112	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
113	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
114	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
115	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
116	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
117	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
118	24608443	Diabetic db/db mice with conditional deletion of SIRT1 in podocytes developed more proteinuria, kidney injury, and acetylation of p65 and STAT3 compared with db/db mice without SIRT1 deletion.
119	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
120	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
121	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
122	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
123	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
124	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
125	24608443	Treatment of db/db mice with a bromodomain and extraterminal (BET)-specific bromodomain inhibitor (MS417) which blocks acetylation-mediated association of p65 and STAT3 with BET proteins, attenuated proteinuria, and kidney injury.
126	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
127	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
128	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
129	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
130	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
131	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
132	24608443	Our findings strongly support a critical role for p65 and STAT3 acetylation in DN.
133	21220918	TGF-β1 induces podocyte injury through Smad3-ERK-NF-κB pathway and Fyn-dependent TRPC6 phosphorylation.
134	21220918	TGF-β1 induces podocyte injury through Smad3-ERK-NF-κB pathway and Fyn-dependent TRPC6 phosphorylation.
135	21220918	In addition, Western blot showed that TGF-β1 induced significant activation of p-Smad3, p-ERK and RelA/p65.
136	21220918	In addition, Western blot showed that TGF-β1 induced significant activation of p-Smad3, p-ERK and RelA/p65.
137	21220918	Importantly, obvious translocation of ERK and RelA/p65 to nuclei was observed in TGF-β1-treated podocyte, which was reduced by ERK inhibitor U0126.
138	21220918	Importantly, obvious translocation of ERK and RelA/p65 to nuclei was observed in TGF-β1-treated podocyte, which was reduced by ERK inhibitor U0126.
139	21220918	Together, we provide evidences that TGF-β1 induces podocyte damage by upregulating TRPC6 protein most possibly through Smad3-ERK-NF-κB pathway, in which Fyn-dependent tyrosine phosphorylation of TRPC6 might exert a crucial role on the activation of its channel function.
140	21220918	Together, we provide evidences that TGF-β1 induces podocyte damage by upregulating TRPC6 protein most possibly through Smad3-ERK-NF-κB pathway, in which Fyn-dependent tyrosine phosphorylation of TRPC6 might exert a crucial role on the activation of its channel function.
141	19507273	The expressions of nephrin, tumor necrosis factor-alpha (TNF-alpha), NF-kappaB p65 and 3-nitrotyrosine (3-NT) protein were determined by immunoinfluorescence or Western blot analysis in the kidneys.
142	19507273	The expressions of nephrin, tumor necrosis factor-alpha (TNF-alpha), NF-kappaB p65 and 3-nitrotyrosine (3-NT) protein were determined by immunoinfluorescence or Western blot analysis in the kidneys.
143	19507273	The expressions of TNF-alpha, NF-kappaB p65 and 3-NT protein were significantly increased in the kidneys of diabetic rats, which were all significantly inhibited by TGP treatment.
144	19507273	The expressions of TNF-alpha, NF-kappaB p65 and 3-NT protein were significantly increased in the kidneys of diabetic rats, which were all significantly inhibited by TGP treatment.
145	19193728	Our previous studies demonstrated that 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] plays a renoprotective role by suppressing the RAS, with renin and angiotensinogen (AGT) as the main targets.
146	19193728	Our previous studies demonstrated that 1,25-dihydroxyvitamin D(3) [1,25(OH)(2)D(3)] plays a renoprotective role by suppressing the RAS, with renin and angiotensinogen (AGT) as the main targets.
147	19193728	The mechanism whereby 1,25(OH)(2)D(3) transcriptionally suppresses renin gene expression has been elucidated; however, how vitamin D regulates AGT remains unknown.
148	19193728	The mechanism whereby 1,25(OH)(2)D(3) transcriptionally suppresses renin gene expression has been elucidated; however, how vitamin D regulates AGT remains unknown.
149	19193728	In mesangial cells, the stimulation was inhibited by 1,25(OH)(2)D(3) (20 nM) or NF-kappaB inhibitor BAY 11-7082, suggesting the involvement of NF- kappaB in HG-induced AGT expression and the interaction between 1,25(OH)(2)D(3) and NF-kappaB in the regulation.
150	19193728	In mesangial cells, the stimulation was inhibited by 1,25(OH)(2)D(3) (20 nM) or NF-kappaB inhibitor BAY 11-7082, suggesting the involvement of NF- kappaB in HG-induced AGT expression and the interaction between 1,25(OH)(2)D(3) and NF-kappaB in the regulation.
151	19193728	EMSA and ChIP assays demonstrated increased p65/p50 binding to a NF-kappaB binding site at -1734 in the AGT gene promoter upon high glucose stimulation, and the binding was disrupted by 1,25(OH)(2)D(3) treatment.
152	19193728	EMSA and ChIP assays demonstrated increased p65/p50 binding to a NF-kappaB binding site at -1734 in the AGT gene promoter upon high glucose stimulation, and the binding was disrupted by 1,25(OH)(2)D(3) treatment.
153	19193728	Overexpression of p65/p50 overcame 1,25(OH)(2)D(3) suppression, and mutation of this NF-kappaB binding site blunted 1,25(OH)(2)D(3) suppression of the promoter activity.
154	19193728	Overexpression of p65/p50 overcame 1,25(OH)(2)D(3) suppression, and mutation of this NF-kappaB binding site blunted 1,25(OH)(2)D(3) suppression of the promoter activity.
155	19193728	In mice lacking the vitamin D receptor, AGT mRNA expression in the kidney was markedly increased compared with wild-type mice, and AGT induction in diabetic mice was suppressed by treatment with a vitamin D analog.
156	19193728	In mice lacking the vitamin D receptor, AGT mRNA expression in the kidney was markedly increased compared with wild-type mice, and AGT induction in diabetic mice was suppressed by treatment with a vitamin D analog.
157	19193728	These data indicate that 1,25(OH)(2)D(3) suppresses hyperglycemia-induced AGT expression by blocking NF-kappaB-mediated pathway.
158	19193728	These data indicate that 1,25(OH)(2)D(3) suppresses hyperglycemia-induced AGT expression by blocking NF-kappaB-mediated pathway.
159	16205945	The expression of NF-kappaB subunits p65 and p50, and the NF-kappaB regulated proinflammatory mediators tumor necrosis factor-alpha (TNF-alpha), interleukin-1beta (IL-1beta), interleukin-6 (IL-6) and intercellular adhesion molecule-1 (ICAM-1) as well as CD68 and synaptopodin was examined by Southwestern histochemistry (SWH) or immunohistochemistry.
160	16205945	The expression of NF-kappaB subunits p65 and p50, and the NF-kappaB regulated proinflammatory mediators tumor necrosis factor-alpha (TNF-alpha), interleukin-1beta (IL-1beta), interleukin-6 (IL-6) and intercellular adhesion molecule-1 (ICAM-1) as well as CD68 and synaptopodin was examined by Southwestern histochemistry (SWH) or immunohistochemistry.
161	16205945	The expression of NF-kappaB subunits p65 and p50, and the NF-kappaB regulated proinflammatory mediators tumor necrosis factor-alpha (TNF-alpha), interleukin-1beta (IL-1beta), interleukin-6 (IL-6) and intercellular adhesion molecule-1 (ICAM-1) as well as CD68 and synaptopodin was examined by Southwestern histochemistry (SWH) or immunohistochemistry.
162	16205945	In contrast to non-proliferative glomerulopathy and normal controls, NF-kappaB activation (both p65 and p50) was enhanced in glomerular endothelial, mesangial cells or infiltrating cells in class IV LN, along with upregulation of TNF-alpha, IL-1beta, IL-6 and ICAM-1 expression.
163	16205945	In contrast to non-proliferative glomerulopathy and normal controls, NF-kappaB activation (both p65 and p50) was enhanced in glomerular endothelial, mesangial cells or infiltrating cells in class IV LN, along with upregulation of TNF-alpha, IL-1beta, IL-6 and ICAM-1 expression.
164	16205945	In contrast to non-proliferative glomerulopathy and normal controls, NF-kappaB activation (both p65 and p50) was enhanced in glomerular endothelial, mesangial cells or infiltrating cells in class IV LN, along with upregulation of TNF-alpha, IL-1beta, IL-6 and ICAM-1 expression.
165	16205945	Glomerular endothelial and mesangial activation of NF-kappaB and mesangial ICAM-1 expression correlated with disease activity and the level of glomerular macrophage infiltration.
166	16205945	Glomerular endothelial and mesangial activation of NF-kappaB and mesangial ICAM-1 expression correlated with disease activity and the level of glomerular macrophage infiltration.
167	16205945	Glomerular endothelial and mesangial activation of NF-kappaB and mesangial ICAM-1 expression correlated with disease activity and the level of glomerular macrophage infiltration.
168	16205945	Podocyte NF-kappaB overactivation (predominantly p65) paralleled podocyte expression of TNF-alpha and IL-1beta in patients with LN and non-proliferative glomerulopathy.
169	16205945	Podocyte NF-kappaB overactivation (predominantly p65) paralleled podocyte expression of TNF-alpha and IL-1beta in patients with LN and non-proliferative glomerulopathy.
170	16205945	Podocyte NF-kappaB overactivation (predominantly p65) paralleled podocyte expression of TNF-alpha and IL-1beta in patients with LN and non-proliferative glomerulopathy.
171	16205945	Podocyte staining scores of NF-kappaB and p65 were positively correlated with the severity of proteinuria in LN and non-proliferative glomerulopathy.
172	16205945	Podocyte staining scores of NF-kappaB and p65 were positively correlated with the severity of proteinuria in LN and non-proliferative glomerulopathy.
173	16205945	Podocyte staining scores of NF-kappaB and p65 were positively correlated with the severity of proteinuria in LN and non-proliferative glomerulopathy.