Botulinum toxin D ADP-ribosylates a 22-24 KDa membrane protein in platelets and HL-60 cells that is distinct from p21N-ras

Biochem Biophys Res Commun. 1988 Aug 30;155(1):263-9. doi: 10.1016/s0006-291x(88)81078-7.

Abstract

Botulinum toxin D ADP-ribosylates a 22-24 KDa protein in platelets, GH3 and HL-60 cells, and a mouse T-cell line CTLL. In platelet homogenates the protein is localized to the membrane fraction, and ADP-ribosylation can also be produced in saponin-permeabilized and intact cells. In the latter, the toxin also potentiates secretion caused by a variety of agonists. In platelets and HL-60 cells the toxin substrate is shown, by use of anti-ras monoclonal antibody, to be distinct from the ras family of proteins. This toxin substrate may represent an additional class of proteins involved in stimulus-response coupling.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Adenosine Triphosphate / metabolism
  • Animals
  • Antibodies, Monoclonal
  • Blood Platelets / drug effects
  • Blood Platelets / physiology
  • Botulinum Toxins / pharmacology*
  • Cell Line
  • GTP-Binding Proteins / metabolism
  • Humans
  • Mice
  • Molecular Weight
  • Platelet Membrane Glycoproteins / metabolism*
  • Precipitin Tests
  • Proto-Oncogene Proteins / immunology
  • Proto-Oncogene Proteins / isolation & purification
  • Proto-Oncogene Proteins / metabolism*
  • Proto-Oncogene Proteins p21(ras)

Substances

  • Antibodies, Monoclonal
  • Platelet Membrane Glycoproteins
  • Proto-Oncogene Proteins
  • Adenosine Diphosphate Ribose
  • Adenosine Triphosphate
  • Botulinum Toxins
  • GTP-Binding Proteins
  • HRAS protein, human
  • Proto-Oncogene Proteins p21(ras)