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A high-affinity bradykinin receptor in membranes from rat myometrium is coupled to pertussis toxin-sensitive G-proteins of the Gi family

Item Type:Article
Title:A high-affinity bradykinin receptor in membranes from rat myometrium is coupled to pertussis toxin-sensitive G-proteins of the Gi family
Creators Name:Liebmann, C. and Offermanns, S. and Spicher, K. and Hinsch, K.D. and Schnittler, M. and Morgat, J.L. and Reissmann, S. and Schultz, G. and Rosenthal, W.
Abstract:In rat myometrial membranes, two 3H-Bradykinin binding sites with KD values of 16 pM and 1.0 nM were identified. Employed at pM concentrations, bradykinin stimulated high affinity GTPases. This effect was abolished by the bradykinin antagonist, [D-Arg(Hyp3-Thi5,8, D-Phe7)]bradykinin (10 microM), and by treatment of membranes with pertussis toxin. Myometrial membranes contained two pertussis toxin substrates of 40 and 41 kDa, which corresponded immunologically to alpha-subunits of Gi-type G-proteins. The faster migrating substrate was tentatively identified as Gi2 alpha-subunit. The electrophoretic mobility of the slower migrating Gi alpha-subunit was very similar to that of the Gi3 alpha-subunit. Go alpha-subunits were not detected. Thus, in uterine smooth muscle, G-proteins of the Gi-family (Gi2, Gi3) couple high-affinity bradykinin receptors to their effector enzymes.
Keywords:Adenosine Diphosphate Ribose, Bradykinin, Cell Membrane, Cholera Toxin, GTP Phosphohydrolases, GTP-Binding Proteins, Kinetics, Macromolecular Substances, Molecular Weight, Myometrium, Pertussis Toxin, Bradykinin Receptors, Neurotransmitter Receptors, Bordetella Virulence Factors, Animals, Rats
Source:Biochemical and Biophysical Research Communications
ISSN:0006-291X
Publisher:Academic Press (U.S.A.)
Volume:167
Number:3
Page Range:910-917
Date:30 March 1990
Official Publication:https://doi.org/10.1016/0006-291X(90)90610-Y
PubMed:View item in PubMed

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