Advanced glycosylation end products stimulate collagen mRNA synthesis in mesangial cells mediated by protein kinase C and transforming growth factor–beta

2001 ◽  
Vol 138 (1) ◽  
pp. 59-68 ◽  
Author(s):  
Young Sook Kim ◽  
Bong Cho Kim ◽  
Chi Young Song ◽  
Hye Kyoung Hong ◽  
Kyung Chul Moon ◽  
...  
Keyword(s):  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Mesangial Cells ◽  
Mrna Synthesis ◽  
Advanced Glycosylation End Products ◽  
Collagen Mrna ◽  
Kinase C ◽  
End Products ◽  
Growth Factor Beta ◽  
Advanced Glycosylation

scholarly journals PDGF and TGF-β mediate collagen production by mesangial cells exposed to advanced glycosylation end products

1995 ◽  
Vol 48 (1) ◽  
pp. 111-117 ◽  
Author(s):  
Douglas C. Throckmorton ◽  
Anne P. Brogden ◽  
Brian Min ◽  
Howard Rasmussen ◽  
Michael Kashgarian
Keyword(s):  
Mesangial Cells ◽  
Collagen Production ◽  
Advanced Glycosylation End Products ◽  
End Products ◽  
Advanced Glycosylation

scholarly journals Transforming growth factor beta regulates cyclooxygenase-2 in glomerular mesangial cells

2006 ◽  
Vol 69 (9) ◽  
pp. 1578-1585 ◽  
Author(s):  
P. Harding ◽  
L. Balasubramanian ◽  
J. Swegan ◽  
A. Stevens ◽  
W.F. Glass
Keyword(s):  
Growth Factor ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
Mesangial Cells ◽  
Cyclooxygenase 2 ◽  
Glomerular Mesangial Cells ◽  
Growth Factor Beta

scholarly journals Evidence for the involvement of protein kinase activity in transforming growth factor-beta signal transduction.

1992 ◽  
Vol 12 (1) ◽  
pp. 261-265 ◽  
Author(s):  
M Ohtsuki ◽  
J Massagué
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
G1 Phase ◽  
Tgf Beta ◽  
Kinase C ◽  
Growth Factor Beta ◽  
Pai 1

Transforming growth factor-beta 1 (TGF-beta 1) rapidly increases the expression of junB transcription factor and plasminogen activator inhibitor-1 (PAI-1) and prevents the cell cycle-dependent phosphorylation of the RB retinoblastoma susceptibility gene product during late G1 phase in Mv1Lu lung epithelial cells. These responses are shown in this report to be blocked by the potent serine/threonine protein kinase inhibitor, H7, added with TGF-beta 1. Added alone, H7 does not alter the basal junB or PAI-1 mRNA levels, the deposition of PAI-1 into the extracellular matrix, or the phosphorylation of RB in late G1 phase, suggesting that this inhibitor does not have a general nonspecific effect on the cell. The analogs H8 and H9, which are preferential inhibitors of cyclic nucleotide-dependent protein kinases, are fivefold less potent than H7 as inhibitors of the TGF-beta response. The PAI-1 response to TGF-beta 1 is not affected by the simultaneous addition of staurosporine, which is a protein kinase C inhibitor, or by the prolonged preincubation of cells with phorbol 12-myristate 13-acetate, which down-regulates protein kinase C. The results suggest the possibility that H7 and its analogs block various early TGF-beta responses by inhibiting a protein serine/threonine kinase(s).

Evidence for the involvement of protein kinase activity in transforming growth factor-beta signal transduction

1992 ◽  
Vol 12 (1) ◽  
pp. 261-265
Author(s):  
M Ohtsuki ◽  
J Massagué
Keyword(s):  
Protein Kinase C ◽  
Growth Factor ◽  
Protein Kinase ◽  
Transforming Growth Factor Beta ◽  
Transforming Growth Factor ◽  
G1 Phase ◽  
Tgf Beta ◽  
Kinase C ◽  
Growth Factor Beta ◽  
Pai 1

Transforming growth factor-beta 1 (TGF-beta 1) rapidly increases the expression of junB transcription factor and plasminogen activator inhibitor-1 (PAI-1) and prevents the cell cycle-dependent phosphorylation of the RB retinoblastoma susceptibility gene product during late G1 phase in Mv1Lu lung epithelial cells. These responses are shown in this report to be blocked by the potent serine/threonine protein kinase inhibitor, H7, added with TGF-beta 1. Added alone, H7 does not alter the basal junB or PAI-1 mRNA levels, the deposition of PAI-1 into the extracellular matrix, or the phosphorylation of RB in late G1 phase, suggesting that this inhibitor does not have a general nonspecific effect on the cell. The analogs H8 and H9, which are preferential inhibitors of cyclic nucleotide-dependent protein kinases, are fivefold less potent than H7 as inhibitors of the TGF-beta response. The PAI-1 response to TGF-beta 1 is not affected by the simultaneous addition of staurosporine, which is a protein kinase C inhibitor, or by the prolonged preincubation of cells with phorbol 12-myristate 13-acetate, which down-regulates protein kinase C. The results suggest the possibility that H7 and its analogs block various early TGF-beta responses by inhibiting a protein serine/threonine kinase(s).

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