Ignet

Gene Information

Gene symbol: PARVA

Gene name: parvin, alpha

HGNC ID: 14652

Synonyms: FLJ12254, FLJ10793

Related Genes

#	Gene Symbol	Number of hits
1	ARHGEF6	1 hits
2	ILK	1 hits
3	LIMS1	1 hits
4	LIMS2	1 hits
5	LIMS3	1 hits
6	LPP	1 hits
7	PARVB	1 hits
8	PDLIM5	1 hits
9	PIP	1 hits
10	PXN	1 hits
11	RAC1	1 hits
12	TGFA	1 hits

Related Sentences

#	PMID	Sentence
1	15872073	Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival.
2	15872073	With the use of an inducible podocyte differentiation system, it was found that the cellular levels of PINCH-1, integrin linked kinase (ILK), and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, were significantly increased during podocyte differentiation.
3	15872073	Overexpression of the PINCH-1-binding ankyrin repeat domain of ILK but not that of a PINCH-1-binding defective mutant form of the ankyrin domain effectively inhibited the formation of the PINCH-1-ILK-alpha-parvin complex.
4	15872073	Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival.
5	15872073	Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival.
6	15872073	With the use of an inducible podocyte differentiation system, it was found that the cellular levels of PINCH-1, integrin linked kinase (ILK), and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, were significantly increased during podocyte differentiation.
7	15872073	Overexpression of the PINCH-1-binding ankyrin repeat domain of ILK but not that of a PINCH-1-binding defective mutant form of the ankyrin domain effectively inhibited the formation of the PINCH-1-ILK-alpha-parvin complex.
8	15872073	Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival.
9	15872073	Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival.
10	15872073	With the use of an inducible podocyte differentiation system, it was found that the cellular levels of PINCH-1, integrin linked kinase (ILK), and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, were significantly increased during podocyte differentiation.
11	15872073	Overexpression of the PINCH-1-binding ankyrin repeat domain of ILK but not that of a PINCH-1-binding defective mutant form of the ankyrin domain effectively inhibited the formation of the PINCH-1-ILK-alpha-parvin complex.
12	15872073	Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival.
13	15872073	Formation and phosphorylation of the PINCH-1-integrin linked kinase-alpha-parvin complex are important for regulation of renal glomerular podocyte adhesion, architecture, and survival.
14	15872073	With the use of an inducible podocyte differentiation system, it was found that the cellular levels of PINCH-1, integrin linked kinase (ILK), and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, were significantly increased during podocyte differentiation.
15	15872073	Overexpression of the PINCH-1-binding ankyrin repeat domain of ILK but not that of a PINCH-1-binding defective mutant form of the ankyrin domain effectively inhibited the formation of the PINCH-1-ILK-alpha-parvin complex.
16	15872073	Mutations at the alpha-parvin N-terminal proline-directed serine phosphorylation sites reduced its complex formation with ILK and resulted in defects in podocyte adhesion, architecture, and survival.
17	16314921	Both alpha-parvin (PARVA) and beta-parvin (PARVB) localize to focal adhesions and function in cell adhesion, spreading, motility and survival through interactions with partners, such as integrin-linked kinase (ILK), paxillin, alpha-actinin and testicular kinase 1.
18	16314921	A complex of PARVA with ILK and the LIM protein PINCH-1 is critical for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes.
19	16314921	While PARVA inhibits the activities of Rac1 and testicular kinase 1 and cell spreading, PARVB binds alphaPIX and alpha-actinin, and can promote cell spreading.
20	16314921	In contrast to PARVA, PARVB inhibits ILK activity and reverses some of its oncogenic effects in cancer cells.
21	16314921	Both alpha-parvin (PARVA) and beta-parvin (PARVB) localize to focal adhesions and function in cell adhesion, spreading, motility and survival through interactions with partners, such as integrin-linked kinase (ILK), paxillin, alpha-actinin and testicular kinase 1.
22	16314921	A complex of PARVA with ILK and the LIM protein PINCH-1 is critical for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes.
23	16314921	While PARVA inhibits the activities of Rac1 and testicular kinase 1 and cell spreading, PARVB binds alphaPIX and alpha-actinin, and can promote cell spreading.
24	16314921	In contrast to PARVA, PARVB inhibits ILK activity and reverses some of its oncogenic effects in cancer cells.
25	16314921	Both alpha-parvin (PARVA) and beta-parvin (PARVB) localize to focal adhesions and function in cell adhesion, spreading, motility and survival through interactions with partners, such as integrin-linked kinase (ILK), paxillin, alpha-actinin and testicular kinase 1.
26	16314921	A complex of PARVA with ILK and the LIM protein PINCH-1 is critical for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes.
27	16314921	While PARVA inhibits the activities of Rac1 and testicular kinase 1 and cell spreading, PARVB binds alphaPIX and alpha-actinin, and can promote cell spreading.
28	16314921	In contrast to PARVA, PARVB inhibits ILK activity and reverses some of its oncogenic effects in cancer cells.
29	16314921	Both alpha-parvin (PARVA) and beta-parvin (PARVB) localize to focal adhesions and function in cell adhesion, spreading, motility and survival through interactions with partners, such as integrin-linked kinase (ILK), paxillin, alpha-actinin and testicular kinase 1.
30	16314921	A complex of PARVA with ILK and the LIM protein PINCH-1 is critical for cell survival in a variety of cells, including certain cancer cells, kidney podocytes and cardiac myocytes.
31	16314921	While PARVA inhibits the activities of Rac1 and testicular kinase 1 and cell spreading, PARVB binds alphaPIX and alpha-actinin, and can promote cell spreading.
32	16314921	In contrast to PARVA, PARVB inhibits ILK activity and reverses some of its oncogenic effects in cancer cells.
33	17167118	TGF-beta1 regulates the PINCH-1-integrin-linked kinase-alpha-parvin complex in glomerular cells.
34	17167118	Recent studies suggest that a ternary protein complex that consists of PINCH-1, integrin-linked kinase, and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, plays pivotal roles in regulation of glomerular cell behavior.
35	17167118	It is reported here that TGF-beta1, a key factor in the progression of glomerular failure, regulates the PINCH-1-integrin-linked kinase-alpha-parvin (PIP) complex formation in glomerular podocytes and mesangial cells.
36	17167118	TGF-beta1 regulates the PINCH-1-integrin-linked kinase-alpha-parvin complex in glomerular cells.
37	17167118	Recent studies suggest that a ternary protein complex that consists of PINCH-1, integrin-linked kinase, and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, plays pivotal roles in regulation of glomerular cell behavior.
38	17167118	It is reported here that TGF-beta1, a key factor in the progression of glomerular failure, regulates the PINCH-1-integrin-linked kinase-alpha-parvin (PIP) complex formation in glomerular podocytes and mesangial cells.
39	17167118	TGF-beta1 regulates the PINCH-1-integrin-linked kinase-alpha-parvin complex in glomerular cells.
40	17167118	Recent studies suggest that a ternary protein complex that consists of PINCH-1, integrin-linked kinase, and alpha-parvin, cytoplasmic components of cell-extracellular matrix adhesions, plays pivotal roles in regulation of glomerular cell behavior.
41	17167118	It is reported here that TGF-beta1, a key factor in the progression of glomerular failure, regulates the PINCH-1-integrin-linked kinase-alpha-parvin (PIP) complex formation in glomerular podocytes and mesangial cells.
42	18480182	Roles of PINCH-2 in regulation of glomerular cell shape change and fibronectin matrix deposition.
43	18480182	The PINCH-1-integrin-linked kinase (ILK)-alpha-parvin (PIP) complex plays important roles in the regulation of glomerular cell behavior, including podocyte shape change, apoptosis, and mesangial fibronectin matrix deposition.
44	18480182	In this study, we show that PINCH-2, a protein that is structurally related to PINCH-1 but encoded by a different gene, is coexpressed with PINCH-1 in podocytes.
45	18480182	Treatment of podocytes with transforming growth factor (TGF)-beta1 elevated the level of PINCH-2, resulting in increased association of PINCH-2 with ILK and alpha-parvin and concomitant displacement of PINCH-1 from the PIP complex.
46	18480182	To gain insights into the functional consequences of elevated PINCH-2 expression, we overexpressed PINCH-2 in podocytes by infection with an adenovirus encoding PINCH-2.
47	18480182	Overexpression of PINCH-2 resulted in displacement of PINCH-1 from the PIP complex and compromised podocyte spreading.
48	18480182	The PINCH-2-mediated displacement of PINCH-1, however, did not prompt apoptosis.
49	18480182	Interestingly, the effect of PINCH-2 on podocyte spreading depends on differentiation status, as overexpression of PINCH-2 in podocytes that were not fully differentiated did not alter cell spreading.
50	18480182	Finally, we show that overexpression of PINCH-2 in mesangial cells resulted in displacement of PINCH-1 from the PIP complex but impaired neither mesangial cell spreading nor fibronectin matrix deposition.
51	18480182	These studies suggest that PINCH-2 can substitute for PINCH-1 in at least certain processes in glomerular cells (e.g., podocyte survival signaling and mesangial fibronectin matrix deposition), albeit that an aberrantly high level of PINCH-2 may contribute to TGF-beta1-induced alteration in podocyte shape modulation.
52	18480182	Roles of PINCH-2 in regulation of glomerular cell shape change and fibronectin matrix deposition.
53	18480182	The PINCH-1-integrin-linked kinase (ILK)-alpha-parvin (PIP) complex plays important roles in the regulation of glomerular cell behavior, including podocyte shape change, apoptosis, and mesangial fibronectin matrix deposition.
54	18480182	In this study, we show that PINCH-2, a protein that is structurally related to PINCH-1 but encoded by a different gene, is coexpressed with PINCH-1 in podocytes.
55	18480182	Treatment of podocytes with transforming growth factor (TGF)-beta1 elevated the level of PINCH-2, resulting in increased association of PINCH-2 with ILK and alpha-parvin and concomitant displacement of PINCH-1 from the PIP complex.
56	18480182	To gain insights into the functional consequences of elevated PINCH-2 expression, we overexpressed PINCH-2 in podocytes by infection with an adenovirus encoding PINCH-2.
57	18480182	Overexpression of PINCH-2 resulted in displacement of PINCH-1 from the PIP complex and compromised podocyte spreading.
58	18480182	The PINCH-2-mediated displacement of PINCH-1, however, did not prompt apoptosis.
59	18480182	Interestingly, the effect of PINCH-2 on podocyte spreading depends on differentiation status, as overexpression of PINCH-2 in podocytes that were not fully differentiated did not alter cell spreading.
60	18480182	Finally, we show that overexpression of PINCH-2 in mesangial cells resulted in displacement of PINCH-1 from the PIP complex but impaired neither mesangial cell spreading nor fibronectin matrix deposition.
61	18480182	These studies suggest that PINCH-2 can substitute for PINCH-1 in at least certain processes in glomerular cells (e.g., podocyte survival signaling and mesangial fibronectin matrix deposition), albeit that an aberrantly high level of PINCH-2 may contribute to TGF-beta1-induced alteration in podocyte shape modulation.