Literature DB >> 1699453

An enzymatic assay for vitronectin based on its selective phosphorylation by protein kinase A.

B Korc-Grodzicki1, D Chain, T Kreizman, S Shaltiel.   

Abstract

The catalytic subunit (C) of cAMP-dependent protein kinase selectively phosphorylates vitronectin, a plasma protein that promotes cell adhesion and platelet aggregation, inhibits the inactivation of thrombin by antithrombin III, and participates in complement function. This specific phosphorylation is used here (a) to develop an enzymatic assay for vitronectin (with C and [gamma-32P]ATP) which can be used to identify the vitronectin-containing fractions at each stage of its purification; (b) to radioactively label vitronectin and differentiate between the intact and the nicked form of this protein in structure-function studies; and (c) to identify possible vitronectin-related proteins in the plasma of other animal species.

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Year:  1990        PMID: 1699453     DOI: 10.1016/0003-2697(90)90608-c

Source DB:  PubMed          Journal:  Anal Biochem        ISSN: 0003-2697            Impact factor:   3.365


  2 in total

1.  Endogenous cleavage of the Arg-379-Ala-380 bond in vitronectin results in a distinct conformational change which 'buries' Ser-378, its site of phosphorylation by protein kinase A.

Authors:  D Chain; B Korc-Grodzicki; T Kreizman; S Shaltiel
Journal:  Biochem J       Date:  1991-03-01       Impact factor: 3.857

Review 2.  Evidence for an extra-cellular function for protein kinase A.

Authors:  S Shaltiel; I Schvartz; B Korc-Grodzicki; T Kreizman
Journal:  Mol Cell Biochem       Date:  1993-11       Impact factor: 3.396

  2 in total

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