Protein-tyrosine Phosphatase 1B Is a Negative Regulator of Insulin- and Insulin-like Growth Factor-I-stimulated Signaling

Kenner, Kathleen A.; Anyanwu, Ezenta; Olefsky, Jerrold M.; Kusari, Jyotirmoy

doi:10.1074/jbc.271.33.19810

Cited by 413 publications

(282 citation statements)

References 53 publications

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“…Studies with other mediators of apoptotic signaling (such as cytochrome C) or inhibitors of these processes may be useful in determining the precise role of iron in this response and the mechanism of PTP activation in vitro. The in vitro properties of the putative TNFactivated PTP and the recently described involvement of PTP1B in both EGF and insulin signaling pathways (Kenner et al, 1996;Flint et al, 1997;Bandyopadhyay et al, 1997;Liu and Cherno , 1997), supported investigation of a role for PTP1B in TNF action. A protein:protein interaction between tyrosine phosphorylated EGFr and PTP1B was suggested by in vitro coprecipitation studies (Figure 6).…”

Section: Discussionmentioning

confidence: 87%

“…PTP1B has been implicated in the control and modulation of several tyrosine phosphorylation-controlled signaling pathways (Frangioni et al, 1993;Kenner et al, 1996;Wiener et al, 1994;Zhai et al, 1993;Woodford-Thomas et al, 1992) and recent studies suggest a speci®c role for PTP1B modulation of EGFr phosphotyrosine levels through direct association of these proteins in a phosphotyrosinedependent fashion (Flint et al, 1997). Since initial studies suggested membrane-association of a TNFstimulated PTP with properties similar to that of PTP1B, its potential role in dephosphorylation of EGFr was investigated.…”

Section: Resultsmentioning

confidence: 99%

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Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

1999

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Section: Discussionmentioning

confidence: 87%

Section: Resultsmentioning

confidence: 99%

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

1999

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“…For example, tyrosine phosphorylation is a key reaction in the initiation and propagation of insulin action (Myers and White, 1996;White and Kahn, 1994). Thus, PTP1B (Ahmad et al, 1995;Kenner et al, 1996;Kole et al, 1996), LAR (Kulas et al, 1995;Zhang et al, 1996) and PTBa (Lammers et al, 1997;Moller et al, 1995) have been implicated as negative regulators of insulin receptor signaling. Consequently, protein phosphatase inhibitors may have use in the treatment of diabetes and obesity.…”

Section: Introductionmentioning

confidence: 99%

Small molecule inhibitors of dual specificity protein phosphatases

et al. 2000

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“…Early studies suggest that PTP1B blocks insulininduced S6 peptide phosphorylation and inhibits insulin-induced maturation of Xenopus oocytes (10,41). Intracellular delivery of neutralizing antibodies against PTP1B augments IR and IRS-1 phosphorylation and, conversely, overexpression of PTP1B in transfected cells inhibits IR and IRS-1 phosphorylation (4,24). Recent studies show that PTP1B-deficient mice exhibit hypersensitivity to insulin, suggesting that PTP1B is the major tyrosine phosphatase that regulates IR sensitivity (18,28).…”

mentioning

confidence: 99%

Protein-tyrosine-phosphatase 1B activation is regulated developmentally in muscle of neonatal pigs

Suryawan

Davis

2003

American Journal of Physiology-Endocrinology and Metabolism

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Suryawan, Agus, and Teresa A. Davis. Protein-tyrosine-phosphatase 1B activation is regulated developmentally in muscle of neonatal pigs. Am J Physiol Endocrinol Metab 284: E47-E54, 2003. First published September 11, 2002 10.1152/ajpendo.00210.2002The high activity of the insulin-signaling pathway contributes to the enhanced feeding-induced stimulation of translation initiation in skeletal muscle of neonatal pigs. Protein-tyrosine-phosphatase 1B (PTP1B) is a negative regulator of the tyrosine phosphorylation of the insulin receptor (IR) and insulin receptor substrate 1 (IRS-1). The activity of PTP1B is determined mainly by its association with IR and Grb2. We examined the level of PTP1B activity, PTP1B protein abundance, PTP1B tyrosine phosphorylation, and the association of PTP1B with IR and Grb2 in skeletal muscle and liver of fasted and fed 7-and 26-day-old pigs. PTP1B activity in skeletal muscle was lower (P Ͻ 0.05) in 7-compared with 26-day-old pigs but in liver was similar in the two age groups. PTP1B abundances were similar in muscle but lower (P Ͻ 0.05) in liver of 7-compared with 26-day-old pigs. PTP1B tyrosine phosphorylation in muscle was lower (P Ͻ 0.05) in 7-than in 26-day-old pigs. The associations of PTP1B with IR and with Grb2 were lower (P Ͻ 0.05) at 7 than at 26 days of age in muscle, but there were no age effects in liver. Finally, in both age groups, fasting did not have any effect on these parameters. These results indicate that basal PTP1B activation is developmentally regulated in skeletal muscle of neonatal pigs, consistent with the developmental changes in the activation of the insulin-signaling pathway reported previously. Reduced PTP1B activation in neonatal muscle likely contributes to the enhanced insulin sensitivity of skeletal muscle in neonatal pigs.neonate; insulin signaling; insulin sensitivity; protein synthesis THE ENHANCED ACTIVATION of the insulin-signaling pathway leading to translation initiation in skeletal muscle of the neonate after food consumption has an important role in the enhanced responsiveness of muscle protein synthesis to feeding in the neonate (13,16,26,27,37). We have shown that the feeding-induced activation of the insulin receptor (IR), insulin receptor substrate-1 (IRS-1), and phosphatidylinositol 3-kinase (PI 3-kinase), as well as the abundance of the IR, is enhanced in skeletal muscle of the neonatal pig and decreases markedly with development. This developmental decline in the feeding-induced activation of early insulin-signaling components parallels the developmental decline in the feeding-induced activation of downstream signaling proteins, leading to the stimulation of protein synthesis in skeletal muscle and the developmental decrease in the ability of insulin to stimulate muscle protein synthesis. However, the molecular mechanism that regulates the developmental decline in the insulin sensitivity of skeletal muscle in neonatal pigs has not been elucidated.When insulin binds to its receptor, it induces autophosphorylation of the receptor on its ty...

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Protein-tyrosine Phosphatase 1B Is a Negative Regulator of Insulin- and Insulin-like Growth Factor-I-stimulated Signaling

Cited by 413 publications

References 53 publications

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor

Small molecule inhibitors of dual specificity protein phosphatases

Protein-tyrosine-phosphatase 1B activation is regulated developmentally in muscle of neonatal pigs

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