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
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Diphosphate Ribose / metabolism*
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Adenosine Triphosphate / metabolism
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Animals
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Antibodies, Monoclonal
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Blood Platelets / drug effects
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Blood Platelets / physiology
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Botulinum Toxins / pharmacology*
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Cell Line
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GTP-Binding Proteins / metabolism
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Humans
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Mice
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Molecular Weight
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Platelet Membrane Glycoproteins / metabolism*
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Precipitin Tests
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Proto-Oncogene Proteins / immunology
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Proto-Oncogene Proteins / isolation & purification
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins p21(ras)
Substances
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Antibodies, Monoclonal
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Platelet Membrane Glycoproteins
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Proto-Oncogene Proteins
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Adenosine Diphosphate Ribose
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Adenosine Triphosphate
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Botulinum Toxins
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GTP-Binding Proteins
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HRAS protein, human
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Proto-Oncogene Proteins p21(ras)