Functional reconstitution of receptors for bradykinin and des argZ-bradykinin from pulmonary artery membranes
Bradykinin (BK) is a vasoactive peptide which mediates a number of vascular functions, including activation of prostaglandin biosynthesis and modulation of vasomotor tone. BK and its kinase II metabolite, des argZ-BK, have been reported to activate the B2 and B1 receptors, respectively. The authors prepared membranes from the bovine pulmonary artery and solubilized membrane proteins using the zwitterionic detergent CHAPS (3-((3-cholamidopropyl) dimethylammonio)-1-propanesulfonate). The solubilized proteins were reconstituted into liposomes via a gel filtration method. The vesicles specifically bound both TH-BK and TH-des argZ-BK, although the latter bound with significantly lower affinity. The binding of TH-BK was inhibited 65% by guanosine 5'-0-thiotriphosphate S while the binding of TH-des argZ-BK was unaffected. This suggests that the receptor for BK was associated with a guanine-nucleotide binding protein whereas the receptor for des argZ-BK was not. Since des argZ-BK has recently been reported to be considerably less potent than BK at activating the turnover of phosphatidylinositol, the authors data suggest that this is due to the des argZ-BK receptor not being coupled to a G-protein. Further work towards characterizing these receptors is now underway.
- Research Organization:
- Boston Univ. Medical Center, MA
- OSTI ID:
- 6360258
- Report Number(s):
- CONF-870644-; TRN: 87-028643
- Journal Information:
- Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 46:6; Conference: 78. annual meeting of the American Society of Biological Chemists conference, Philadelphia, PA, USA, 7 Jun 1987
- Country of Publication:
- United States
- Language:
- English
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550201* - Biochemistry- Tracer Techniques