Interaction of mastoparan with the low molecular mass GTP‐binding proteins rho/rac
- 21 October 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 291 (2) , 336-340
- https://doi.org/10.1016/0014-5793(91)81315-y
Abstract
Mastoparan, which has been shown to active G proteins [1], inhibits the ADP‐ribosylation of 20 kDa human platelet membrane proteins catalyzed by Clostridium botulinum exoenzyme C3 half‐maximally and maximally (90%) at 20 and 100 μM concentrations, respectively. Inhibition of ADP‐ribosylation was enhanced by GTP‐γS. Mastoparan increased GTP hydrolysis by porcine brain rho protein and stimulated GTP binding in a concentration dependent manner. The data suggest that mastoparan not only interacts with heterotrimeric G proteins but also with low molecular mass GTP‐binding proteins of the rho/rac family.Keywords
This publication has 35 references indexed in Scilit:
- Interaction of recombinant rho A GTP‐binding proteins with photoexcited rhodopsinFEBS Letters, 1990
- Mastoparan, a wasp venom, activates platelets via pertussis toxin-sensitive GTP-binding proteinsBiochemical and Biophysical Research Communications, 1990
- Purification of the 22 kDa protein substrate of botulinum ADP‐ribosyltransferase C3 from porcine brain cytosol and its characterization as a GTP‐binding protein highly homologous to the rho gene productFEBS Letters, 1989
- The rho gene product expressed in E. Coli is a substrate of botulinum ADP-ribosyltransferase C3Biochemical and Biophysical Research Communications, 1989
- Clostridium botulinum type C produces a novel ADP‐ribosyltransferase distinct from botulinum C2 toxinFEBS Letters, 1987
- High affinity binding of the mastoparans by calmodulinBiochemical and Biophysical Research Communications, 1983
- Epinephrine inhibits adenylate cyclase and stimulates a GTPase in human platelet membranes vis α‐adrenoceptorsFEBS Letters, 1981
- A new mast cell degranulating peptide "mastoparan" in the venom of Vespula lewisii.CHEMICAL & PHARMACEUTICAL BULLETIN, 1979
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970