Faculty Opinions recommendation of Regulation of insulin signaling through reversible oxidation of the protein-tyrosine phosphatases TC45 and PTP1B.

2004 ◽  
Author(s):  
Celerino Abad-Zapatero
Keyword(s):  
Insulin Signaling ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

Modulation of insulin signaling by protein tyrosine phosphatases

2000 ◽  
Vol 78 (9) ◽  
pp. 473-482 ◽  
Author(s):  
Mounib Elchebly ◽  
Alan Cheng ◽  
Michel L. Tremblay
Keyword(s):  
Insulin Signaling ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine

scholarly journals S -nitrosylation of endogenous protein tyrosine phosphatases in endothelial insulin signaling

2016 ◽  
Vol 99 ◽  
pp. 199-213 ◽  
Author(s):  
Ming-Fo Hsu ◽  
Kuan-Ting Pan ◽  
Fan-Yu Chang ◽  
Kay-Hooi Khoo ◽  
Henning Urlaub ◽  
...  
Keyword(s):  
Insulin Signaling ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine ◽  
Endogenous Protein

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 Regulation of Insulin Signaling through Reversible Oxidation of the Protein-tyrosine Phosphatases TC45 and PTP1B

2004 ◽  
Vol 279 (36) ◽  
pp. 37716-37725 ◽  
Author(s):  
Tzu-Ching Meng ◽  
Deirdre A. Buckley ◽  
Sandra Galic ◽  
Tony Tiganis ◽  
Nicholas K. Tonks
Keyword(s):  
Insulin Signaling ◽  
Protein Tyrosine Phosphatases ◽  
Tyrosine Phosphatases ◽  
Protein Tyrosine
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