Specific labelling by [125I]helodermin of high-affinity VIP receptors in rat liver membranes |
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| Authors: | P Robberecht M Waelbroeck P de Neef J C Camus A Vandermeers M C Vandermeers-Piret J Christophe |
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| Affiliation: | Institute of Biochemistry, University of Warsaw, 02-089 Warsaw, Al. Z?wirki i Wigury 93, Poland |
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| Abstract: | Helodermin, a newly isolated peptide from Gila Monster venom, is structurally related to VIP and secretin. When used as radioligand, [125I]helodermin bound rapidly and reversibly to crude rat liver membranes, the dissociation being accelerated by GTP. Competition binding curves of [125I]helodermin and [125I]VIP with unlabelled peptides showed the following order of decreasing affinity: VIP greater than helodermin greater than secretin greater than hpGRF(1-29)-NH2. The shape of binding curves and of concurrent adenylate cyclase activation is compatible with the specific labelling, by [125I]helodermin, of a class of high-affinity VIP receptors that is capable to stimulate adenylate cyclase. |
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| Keywords: | Galactolipase activity Free fatty acid Chloroplast Chilling sensitivity Galactolipid CS chilling-sensitive CR chilling-resistant MGDG monogalactosyldiacylglycerol DGDG digalactosyldiacylglycerol FFA free fatty acid Chl chlorophyll |
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