Skip to main content

The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety.

Publication ,  Journal Article
Benovic, JL; Staniszewski, C; Cerione, RA; Codina, J; Lefkowitz, RJ; Caron, MG
Published in: J Recept Res
1987

Mammalian beta-adrenergic receptors are glycoproteins consisting of a single polypeptide chain of Mr approximately 64,000. Treatment of purified [125I]-labeled hamster lung beta-adrenergic receptor with alpha-mannosidase reveals two discrete populations of receptor consistent with previous studies using membrane bound photoaffinity-labeled receptor. Treatment of the [125I]-labeled receptor with endoglycosidase F results initially in the formation of a Mr approximately 57,000 peptide which is further converted to Mr approximately 49,000 suggesting that there are two N-linked carbohydrate chains per receptor polypeptide. Exoglycosidase treatments and lectin chromatography of the [125I]-labeled receptor reveals the presence of two complex type carbohydrate chains (approximately 10% of which are fucosylated) on approximately 45% of the receptors. The remaining approximately 55% of the receptors appear to contain a mixture of carbohydrate chains (possibly high mannose, hybrid and complex type chains). Deglycosylation of the receptor by endoglycosidase F does not appear to alter the binding affinity of the receptor for a variety of beta-adrenergic agonists and antagonists. Moreover, the ability of control, alpha-mannosidase sensitive or insensitive (fractionated on immobilized wheat germ agglutinin) and neuraminidase, alpha-mannosidase or endoglycosidase F treated receptors to interact with the stimulatory guanine nucleotide regulatory protein in a reconstituted system were virtually identical. The deglycosylated receptor was also unaltered in its heat lability as well as its susceptibility to a variety of proteases. These findings demonstrate that the carbohydrate portion of the beta-receptor does not contribute to determining either its specificity of ligand binding or coupling to the adenylate cyclase system.

Duke Scholars

Published In

J Recept Res

DOI

ISSN

0197-5110

Publication Date

1987

Volume

7

Issue

1-4

Start / End Page

257 / 281

Location

United States

Related Subject Headings

  • Temperature
  • Receptors, Adrenergic, beta
  • Protein Binding
  • Peptide Hydrolases
  • Membrane Proteins
  • Lung
  • Lectins
  • Glycoside Hydrolases
  • Glycoproteins
  • GTP Phosphohydrolases
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Benovic, J. L., Staniszewski, C., Cerione, R. A., Codina, J., Lefkowitz, R. J., & Caron, M. G. (1987). The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety. J Recept Res, 7(1–4), 257–281. https://doi.org/10.3109/10799898709054989
Benovic, J. L., C. Staniszewski, R. A. Cerione, J. Codina, R. J. Lefkowitz, and M. G. Caron. “The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety.J Recept Res 7, no. 1–4 (1987): 257–81. https://doi.org/10.3109/10799898709054989.
Benovic JL, Staniszewski C, Cerione RA, Codina J, Lefkowitz RJ, Caron MG. The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety. J Recept Res. 1987;7(1–4):257–81.
Benovic, J. L., et al. “The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety.J Recept Res, vol. 7, no. 1–4, 1987, pp. 257–81. Pubmed, doi:10.3109/10799898709054989.
Benovic JL, Staniszewski C, Cerione RA, Codina J, Lefkowitz RJ, Caron MG. The mammalian beta-adrenergic receptor: structural and functional characterization of the carbohydrate moiety. J Recept Res. 1987;7(1–4):257–281.

Published In

J Recept Res

DOI

ISSN

0197-5110

Publication Date

1987

Volume

7

Issue

1-4

Start / End Page

257 / 281

Location

United States

Related Subject Headings

  • Temperature
  • Receptors, Adrenergic, beta
  • Protein Binding
  • Peptide Hydrolases
  • Membrane Proteins
  • Lung
  • Lectins
  • Glycoside Hydrolases
  • Glycoproteins
  • GTP Phosphohydrolases