Adenovirus-mediated overexpression and stimulation of the human angiotensin II type 2 receptor in porcine cardiac fibroblasts does not modulate proliferation, collagen I mRNA expression and ERK1/ERK2 activity, but inhibits protein tyrosine phosphatases

2001 ◽  
Vol 79 (9) ◽  
pp. 510-521 ◽  
Author(s):  
Christina Warnecke ◽  
Daniel Kaup ◽  
Uta Marienfeld ◽  
Wolfgang Poller ◽  
Charles Yankah ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Mrna Expression ◽  
Cardiac Fibroblasts ◽  
Protein Tyrosine Phosphatases ◽  
Collagen I ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Stimulation Of

scholarly journals Angiotensin II–Induced Insulin Resistance and Protein Tyrosine Phosphatases

2004 ◽  
Vol 24 (11) ◽  
pp. 2009-2013 ◽  
Author(s):  
Mario B. Marrero ◽  
David Fulton ◽  
David Stepp ◽  
David M. Stern
Keyword(s):  
Insulin Resistance ◽  
Angiotensin Ii ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Protein tyrosine phosphatases: the quest for negative regulators of insulin action

2003 ◽  
Vol 284 (4) ◽  
pp. E663-E670 ◽  
Author(s):  
Ernest Asante-Appiah ◽  
Brian P. Kennedy
Keyword(s):  
Type 2 Diabetes ◽  
Insulin Signaling ◽  
Insulin Action ◽  
Tyrosine Phosphatase ◽  
Critical Role ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Fed State ◽  
Protein Tyrosine

Type 2 diabetes is increasing at an alarming rate worldwide, and there has been a considerable effort in several laboratories to identify suitable targets for the design of drugs against the disease. To this end, the protein tyrosine phosphatases that attenuate insulin signaling by dephosphorylating the insulin receptor (IR) have been actively pursued. This is because inhibiting the phosphatases would be expected to prolong insulin signaling and thereby facilitate glucose uptake and, presumably, result in a lowering of blood glucose. Targeting the IR protein tyrosine phosphatase, therefore, has the potential to be a significant disease-modifying strategy. Several protein tyrosine phosphatases (PTPs) have been implicated in the dephosphorylation of the IR. These phosphatases include PTPα, LAR, CD45, PTPε, SHP2, and PTP1B. In most cases, there is evidence for and against the involvement of the phosphatases in insulin signaling. The most convincing data, however, support a critical role for PTP1B in insulin action. PTP1B knockout mice are not only insulin sensitive but also maintain euglycemia (in the fed state), with one-half the level of insulin observed in wild-type littermates. Interestingly, these mice are also resistant to diet-induced obesity when fed a high-fat diet. The insulin-sensitive phenotype of the PTP1B knockout mouse is reproduced when the phosphatase is also knocked down with an antisense oligonucleotide in obese mice. Thus PTP1B appears to be a very attractive candidate for the design of drugs for type 2 diabetes and obesity.

scholarly journals A RP-UFLC Assay for Protein Tyrosine Phosphatases: Focus on Protein Tyrosine Phosphatase Non-Receptor Type 2 (PTPN2)

2015 ◽  
Vol 5 (1) ◽  
Author(s):  
Romain Duval ◽  
Linh-Chi Bui ◽  
Jérémy Berthelet ◽  
Julien Dairou ◽  
Cécile Mathieu ◽  
...  
Keyword(s):  
Protein Tyrosine Phosphatase ◽  
Tyrosine Phosphatase ◽  
Protein Tyrosine Phosphatases ◽  
Receptor Type ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine
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