scholarly journals SirT1 enhances survival of human osteoarthritic chondrocytes by repressing protein tyrosine phosphatase 1B and activating the insulin-like growth factor receptor pathway

2010 ◽  
Vol 62 (5) ◽  
pp. 1383-1392 ◽  
Author(s):  
Viktoria Gagarina ◽  
Odile Gabay ◽  
Mona Dvir-Ginzberg ◽  
Eun Jin Lee ◽  
Jillian K. Brady ◽  
...  
Keyword(s):  
Growth Factor ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Growth Factor Receptor ◽  
Protein Tyrosine Phosphatase 1B ◽  
Insulin Like Growth Factor ◽  
Protein Tyrosine ◽  
Osteoarthritic Chondrocytes

scholarly journals Polycystin-1 is required for insulin-like growth factor 1-induced cardiomyocyte hypertrophy

PLoS ONE ◽  
2021 ◽  
Vol 16 (8) ◽  
pp. e0255452
Author(s):  
Carolina Fernández ◽  
Natalia Torrealba ◽  
Francisco Altamirano ◽  
Valeria Garrido-Moreno ◽  
César Vásquez-Trincado ◽  
...  
Keyword(s):  
Growth Factor ◽  
Cardiac Hypertrophy ◽  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Pressure Overload ◽  
Cardiomyocyte Hypertrophy ◽  
Protein Tyrosine Phosphatase 1B ◽  
Insulin Like Growth Factor ◽  
Protein Tyrosine

Cardiac hypertrophy is the result of responses to various physiological or pathological stimuli. Recently, we showed that polycystin-1 participates in cardiomyocyte hypertrophy elicited by pressure overload and mechanical stress. Interestingly, polycystin-1 knockdown does not affect phenylephrine-induced cardiomyocyte hypertrophy, suggesting that the effects of polycystin-1 are stimulus-dependent. In this study, we aimed to identify the role of polycystin-1 in insulin-like growth factor-1 (IGF-1) signaling in cardiomyocytes. Polycystin-1 knockdown completely blunted IGF-1-induced cardiomyocyte hypertrophy. We then investigated the molecular mechanism underlying this result. We found that polycystin-1 silencing impaired the activation of the IGF-1 receptor, Akt, and ERK1/2 elicited by IGF-1. Remarkably, IGF-1-induced IGF-1 receptor, Akt, and ERK1/2 phosphorylations were restored when protein tyrosine phosphatase 1B was inhibited, suggesting that polycystin-1 knockdown deregulates this phosphatase in cardiomyocytes. Moreover, protein tyrosine phosphatase 1B inhibition also restored IGF-1-dependent cardiomyocyte hypertrophy in polycystin-1-deficient cells. Our findings provide the first evidence that polycystin-1 regulates IGF-1-induced cardiomyocyte hypertrophy through a mechanism involving protein tyrosine phosphatase 1B.

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