Skip to main content

Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps.

Publication ,  Journal Article
Stiles, GL; Strasser, RH; Caron, MG; Lefkowitz, RJ
Published in: J Biol Chem
September 10, 1983

Photoaffinity labeling techniques using p-azido-m-[125I]iodobenzylcarazolol have recently demonstrated that both the beta 1- and beta 2-adrenergic receptor-binding subunits from mammalian tissues including heart, lung, and erythrocytes reside on peptides of Mr approximately equal to 62,000-64,000. In this study, a two-dimensional gel electrophoresis method for peptide mapping was used to investigate and compare the structure of beta 1 - and beta 2-adrenergic receptor subtypes. When the photoaffinity labeled Mr approximately equal to 62,000 peptides from the beta 2-adrenergic receptors of rat lung and erythrocyte are subjected to simultaneous proteolysis using Staphylococcus aureus V8 proteinase or papain, exactly the same peptide fragments are generated from each subunit. In contrast, when the Mr approximately equal to 62,000 peptide containing the beta 1-adrenergic receptor-binding subunit derived from the rat heart is proteolyzed simultaneously with the Mr approximately equal to 62,000 peptide containing the beta 2-adrenergic receptors from either lung or erythrocyte, the peptide fragments generated are distinctly different. Peptide maps of beta 1-adrenergic receptors from the myocardial tissue of different species (pig versus rat) yield slightly different maps while the maps derived from the beta 2-adrenergic receptors of hamster lung and rat lung or erythrocytes reveal no interspecies differences. These data suggest: 1) alterations in the primary structure of the beta-adrenergic receptor may be responsible for the pharmacological specificities characteristic of beta 1- and beta 2-adrenergic receptor subtypes; and 2) alterations in the primary structure of similar beta-adrenergic receptor subtypes across different species may relate to the magnitude of their phylogenetic differences.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

September 10, 1983

Volume

258

Issue

17

Start / End Page

10689 / 10694

Location

United States

Related Subject Headings

  • Swine
  • Serine Endopeptidases
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rats, Inbred Strains
  • Rats
  • Propanolamines
  • Papain
  • Myocardium
  • Molecular Weight
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Stiles, G. L., Strasser, R. H., Caron, M. G., & Lefkowitz, R. J. (1983). Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps. J Biol Chem, 258(17), 10689–10694.
Stiles, G. L., R. H. Strasser, M. G. Caron, and R. J. Lefkowitz. “Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps.J Biol Chem 258, no. 17 (September 10, 1983): 10689–94.
Stiles GL, Strasser RH, Caron MG, Lefkowitz RJ. Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps. J Biol Chem. 1983 Sep 10;258(17):10689–94.
Stiles, G. L., et al. “Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps.J Biol Chem, vol. 258, no. 17, Sept. 1983, pp. 10689–94.
Stiles GL, Strasser RH, Caron MG, Lefkowitz RJ. Mammalian beta-adrenergic receptors. Structural differences in beta 1 and beta 2 subtypes revealed by peptide maps. J Biol Chem. 1983 Sep 10;258(17):10689–10694.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

September 10, 1983

Volume

258

Issue

17

Start / End Page

10689 / 10694

Location

United States

Related Subject Headings

  • Swine
  • Serine Endopeptidases
  • Receptors, Adrenergic, beta
  • Receptors, Adrenergic
  • Rats, Inbred Strains
  • Rats
  • Propanolamines
  • Papain
  • Myocardium
  • Molecular Weight