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Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity.

Publication ,  Journal Article
Benovic, JL; Stiles, GL; Lefkowitz, RJ; Caron, MG
Published in: Biochem Biophys Res Commun
January 27, 1983

The beta-adrenergic receptors in membranes from rat and hamster lungs have been studies using the photoaffinity label p-azido-m-[125I]-iodobenzyl-carazolol. Previous work with several beta adrenergic photoaffinity probes has suggested heterogeneity of the labelled beta adrenergic receptor peptides with 2-3 receptor peptides generally being identified. We now report that rat and hamster lung membranes prepared either in the presence or absence of protease inhibitors reveal striking differences in the ratios of photoaffinity labelled peptides. In the rat lung the inclusion of protease inhibitors in the membrane preparation changes the ratios of the 64,000, 53,000 and 44,000 molecular weight peptides from 28:42:30 to 72:16:12. Similarly, in hamster lung membranes there is evidence of multiple photoaffinity labelled peptides in preparations without protease inhibitors while only one peptide (app. Mr = 64,000) is labelled in preparations with protease inhibitors. Of the inhibitors tested EDTA and EGTA were the most active in preventing appearance of multiple labelled peptides suggesting that metal-dependent proteolysis may be involved in the generation of apparent receptor peptide heterogeneity.

Duke Scholars

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

January 27, 1983

Volume

110

Issue

2

Start / End Page

504 / 511

Location

United States

Related Subject Headings

  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rats, Inbred Strains
  • Rats
  • Protease Inhibitors
  • Propanolamines
  • Photochemistry
  • Peptides
  • Molecular Weight
  • Membranes
 

Citation

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Benovic, J. L., Stiles, G. L., Lefkowitz, R. J., & Caron, M. G. (1983). Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity. Biochem Biophys Res Commun, 110(2), 504–511. https://doi.org/10.1016/0006-291x(83)91178-6
Benovic, J. L., G. L. Stiles, R. J. Lefkowitz, and M. G. Caron. “Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity.Biochem Biophys Res Commun 110, no. 2 (January 27, 1983): 504–11. https://doi.org/10.1016/0006-291x(83)91178-6.
Benovic JL, Stiles GL, Lefkowitz RJ, Caron MG. Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity. Biochem Biophys Res Commun. 1983 Jan 27;110(2):504–11.
Benovic, J. L., et al. “Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity.Biochem Biophys Res Commun, vol. 110, no. 2, Jan. 1983, pp. 504–11. Pubmed, doi:10.1016/0006-291x(83)91178-6.
Benovic JL, Stiles GL, Lefkowitz RJ, Caron MG. Photoaffinity labelling of mammalian beta-adrenergic receptors: metal-dependent proteolysis explains apparent heterogeneity. Biochem Biophys Res Commun. 1983 Jan 27;110(2):504–511.
Journal cover image

Published In

Biochem Biophys Res Commun

DOI

ISSN

0006-291X

Publication Date

January 27, 1983

Volume

110

Issue

2

Start / End Page

504 / 511

Location

United States

Related Subject Headings

  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rats, Inbred Strains
  • Rats
  • Protease Inhibitors
  • Propanolamines
  • Photochemistry
  • Peptides
  • Molecular Weight
  • Membranes