The roles of phospholipase D and a GTP-binding protein in guanosine 5'-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylcholine in rat liver plasma membranes

K. M. Hurst, B. P. Hughes, G. J. Barritt

    Research output: Contribution to journalArticle

    20 Citations (Scopus)

    Abstract

    1. Guanosine 5'-[γ-thio]triphosphate (GTP[S]) stimulated by 50% the rate of release of [3H]choline and [3H]phosphorylcholine in rat liver plasma membranes labelled with [3H]choline. About 70% of the radioactivity released in the presence of GTP[S] was [3H]choline and 30% was [3H]phosphorylcholine. 2. The hydrolysis of phosphorylcholine to choline and the conversion of choline to phosphorylcholine did not contribute to the formation of [3H]choline and [3H]phosphorylcholine respectively. 3. The release of [3H]choline from membranes was inhibited by low concentrations of SDS or Triton X-100. Considerably higher concentrations of the detergents were required to inhibit the release of [3H]phosphorylcholine. 4. Guanosine 5'-[βγ-imido]triphosphate and guanosine 5'-[αβ-methylene]triphosphate, but not adenosine 5'-[γ-thio]triphosphate, stimulated [3H]choline release to the same extent as did GTP[S]. The GTP[S]-stimulated [3H]choline release was inhibited by guanosine 5'-[β-thio]diphosphate, GDP and GTP but not by GMP. 5. It is concluded that, in rat live plasma membranes, (a) GTP[S]-stimulated hydrolysis of phosphatidylcholine is catalysed predominantly by phospholipase D with some contribution from phospholipase C, and (b) the stimulation of phosphatidylcholine hydrolysis by GTP[s] occurs via a GTP-binding regulatory protein.

    Original languageEnglish
    Pages (from-to)749-753
    Number of pages5
    JournalBiochemical Journal
    Volume272
    Issue number3
    DOIs
    Publication statusPublished - 15 Dec 1990

    Fingerprint Dive into the research topics of 'The roles of phospholipase D and a GTP-binding protein in guanosine 5'-[γ-thio]triphosphate-stimulated hydrolysis of phosphatidylcholine in rat liver plasma membranes'. Together they form a unique fingerprint.

  • Cite this