ArticleThe Biochemical journal1995
Regulation of purified hepatic PC-1 (phosphodiesterase-I/nucleotide pyrophosphatase) by threonine auto(de)phosphorylation and by binding of acidic fibroblast growth factor.
Article in The Biochemical journal, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
4 citing papers in PubMed, 22 citations in OpenAlex.
- The role of membrane glycoprotein plasma cell antigen 1/ectonucleotide pyrophosphatase phosphodiesterase 1 in the pathogenesis of insulin resistance and related abnormalities.Endocrine reviews · 2008Review
- L-histidine inhibits production of lysophosphatidic acid by the tumor-associated cytokine, autotaxin.Lipids in health and disease · 2005Article
- Functional characterization of the non-catalytic ectodomains of the nucleotide pyrophosphatase/phosphodiesterase NPP1.The Biochemical journal · 2003Article
- Rat liver nucleotide pyrophosphatase/phosphodiesterase is an efficient adenylyl transferase.The Biochemical journal · 2000Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
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.
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Registered trials
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