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• W2087018355 startingPage "123" @default.
• W2087018355 abstract "Protein tyrosyl phosphorylation and dephosphorylation play essential roles in regulating cellular events such as proliferation and differentiation, and their involvement in the lens development and transparency is also suggested. The level of tyrosine phosphorylation in a given protein is regulated by the opposing actions of protein-tyrosine kinases (Tyr kinases) and protein-tyrosine phosphatases (TyrPases). Recent studies have revealed that some Tyr kinases, such as platelet-derived growth factor receptor and fibroblast growth factor receptor, are present in the lens, however, little is known about TyrPases in the lens. In this study, we found a 18 kDa protein tyrosine phosphatase (18 kDa TyrPase) predominantly present in the ocular lens of various animals. We purified the phosphatase from the lens of chick embryo and characterized its activity.Phosphatase activity was determined in chick embryo, mouse, rabbit and bovine lenses using p -nitrophenyl phosphate (p NPP) as substrate. All lenses examined dephosphorylated p NPP under acidic conditions, and a large portion of the activity resided in a low molecular weight protein, ca. 18 kDa, following high-resolution gel permeation column chromatography. The brain and liver showed high dephosphorylation activities, but most of their activity was present in high molecular weight fractions, unlike that in the lens. The 18 kDa phosphatase was purified from the lens of 17 day old chick embryos to near-homogeneity with two-step rapid chromatography. This phosphatase showed strict substrate specificity for phosphotyrosine and phosphotyrosyl peptides, suggesting that it was a kind of protein tyrosine phosphatases (TyrPases). Several known inhibitors of TyrPases, such as SH blockers, vanadate and phenylarsine oxide, strongly inhibited the enzyme activity. The molecular weight, substrate specificity, and responses to various inhibitors and activators coincide well with those reported for the low molecular weight protein tyrosine phosphatase (LMW-TyrPase), belonging to the TyrPase superfamily. These results suggest that the 18 kDa phosphatase found in the lens is a LMW-TyrPase. The 18 kDa TyrPase is the predominant phosphatase in the ocular lens. It may be involved in regulation of lens cell proliferation, differentiation and/or lens transparency." @default.
• W2087018355 created "2016-06-24" @default.
• W2087018355 creator A5021679085 @default.
• W2087018355 creator A5033772191 @default.
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• W2087018355 date "2001-07-01" @default.
• W2087018355 modified "2023-09-26" @default.
• W2087018355 title "18 kDa protein tyrosine phosphatase in the ocular lens." @default.
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• W2087018355 doi "https://doi.org/10.1006/exer.2001.1018" @default.
• W2087018355 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/11428869" @default.
• W2087018355 hasPublicationYear "2001" @default.
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