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Mammalian beta-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains.

Publication ,  Journal Article
Stiles, GL; Benovic, JL; Caron, MG; Lefkowitz, RJ
Published in: J Biol Chem
July 10, 1984

Mammalian beta-adrenergic receptor binding peptides can be visualized by covalently labeling them with the photoaffinity reagent p-azido-m-[125I]iodobenzylcarazolol followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The receptor peptides migrate as broad bands of Mr approximately equal to 62,000. In the present study, we examined the carbohydrate composition of the mammalian beta receptor through the use of specific exo- and endoglycosidases and lectin affinity chromatography. Treatment of p-azido-m-[125I]iodobenzylcarazolol-labeled beta2-adrenergic receptors from hamster lung or rat erythrocyte with the exoglycosidases neuraminidase and alpha-mannosidase provided evidence for the existence of both high mannose and complex type carbohydrate chains on beta 2-adrenergic receptors. The nonadditivity of the effect of sequential treatments with these enzymes suggested discrete populations of beta-adrenergic receptors containing either complex or high mannose type chains. Deglycosylation of receptor with endoglycosidase F results in a single labeled polypeptide at Mr = 49,000 for both systems. The same two populations of the beta receptors (high mannose or complex type chain) could also be fractionated by lectin affinity chromatography of solubilized p-azido-m-[125I]iodobenzylcarazolol-labeled receptors. The high mannose-containing receptors could be absorbed to and specifically eluted from concanavalin A-agarose. Those containing complex type carbohydrates could be adsorbed to and eluted from wheat germ agglutinin-agarose. Taken together, these data suggest that mammalian beta-adrenergic receptors contain both complex and high mannose type carbohydrate chains and that microheterogeneity of these chains likely explains the broad band pattern typically obtained on sodium dodecyl sulfate-polyacrylamide gel electrophoresis.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

July 10, 1984

Volume

259

Issue

13

Start / End Page

8655 / 8663

Location

United States

Related Subject Headings

  • Receptors, Adrenergic, beta
  • Rats
  • Propanolamines
  • Neuraminidase
  • Molecular Weight
  • Mannose
  • Lung
  • Glycoproteins
  • Erythrocytes
  • Cricetinae
 

Citation

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Stiles, G. L., Benovic, J. L., Caron, M. G., & Lefkowitz, R. J. (1984). Mammalian beta-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains. J Biol Chem, 259(13), 8655–8663.
Stiles, G. L., J. L. Benovic, M. G. Caron, and R. J. Lefkowitz. “Mammalian beta-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains.J Biol Chem 259, no. 13 (July 10, 1984): 8655–63.
Stiles GL, Benovic JL, Caron MG, Lefkowitz RJ. Mammalian beta-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains. J Biol Chem. 1984 Jul 10;259(13):8655–63.
Stiles GL, Benovic JL, Caron MG, Lefkowitz RJ. Mammalian beta-adrenergic receptors. Distinct glycoprotein populations containing high mannose or complex type carbohydrate chains. J Biol Chem. 1984 Jul 10;259(13):8655–8663.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

July 10, 1984

Volume

259

Issue

13

Start / End Page

8655 / 8663

Location

United States

Related Subject Headings

  • Receptors, Adrenergic, beta
  • Rats
  • Propanolamines
  • Neuraminidase
  • Molecular Weight
  • Mannose
  • Lung
  • Glycoproteins
  • Erythrocytes
  • Cricetinae