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• W1776095151 abstract "The plasma cell differentiation antigen PC-1 was purified to homogeneity from rat liver membranes. Denaturing electrophoresis revealed polypeptides of 118 and 128 kDa, which were both recognized by antibodies against recombinant murine PC-1. During gel filtration PC-1 migrated as a protein of about 500 kDa, suggesting a tetrameric structure. Purified PC-1 displayed a phosphodiesterase-I/nucleotide pyrophosphatase activity that could be completely blocked by EDTA, dithiothreitol and acidic fibroblast growth factor (extrapolated Ki = 1.3 nM). Purified PC-1 was also capable of threonine autophosphorylation and of phosphorylation of histone IIa. The autophosphorylation of PC-1 was inhibited by addition of histone IIa, and it was blocked by phosphodiesterase-I inhibitors (acidic fibroblast growth factor, dithiothreitol), by nucleotides (ATP, ADP, AMP), and by vanadate. When added to autophosphorylated PC-1, these compounds caused a prompt dephosphorylation. However, the same agents did not affect the (de)phosphorylation of histone IIa, which is not a substrate for the PC-1 phosphatase. These data indicate that phosphodiesterase-I inhibitors, nucleotides and vanadate affect the (de)phosphorylation of PC-1 by stimulating the PC-1 phosphatase and/or by shielding the autophosphorylation site from the PC-1 kinase. The rate of dephosphorylation of PC-1 was independent of the dilution, suggesting an autocatalytic intramolecular process. We propose that the autophosphorylation of PC-1 serves to block its nucleotide pyrophosphatase activity when extracellular ATP becomes scarce." @default.
• W1776095151 created "2016-06-24" @default.
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• W1776095151 date "1995-02-15" @default.
• W1776095151 modified "2023-09-27" @default.
• W1776095151 title "Regulation of purified hepatic PC-1 (phosphodiesterase-I/nucleotide pyrophosphatase) by threonine auto(de)phosphorylation and by binding of acidic fibroblast growth factor" @default.
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• W1776095151 doi "https://doi.org/10.1042/bj3060271" @default.
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