Literature DB >> 7937345

Glycosylation of the GLP-1 receptor is a prerequisite for regular receptor function.

R Göke1, R Just, B Lankat-Buttgereit, B Göke.   

Abstract

The GLP-1 receptor on RINm5F cells is a glycoprotein with a M(r) of 63,000. Treatment of the receptor with glycopeptidase F generated a protein with a M(r) of 51,000, indicating that the GLP-1 receptor contains N-linked glycans. Tunicamycin pretreatment concentration-dependently decreased GLP-1 binding to RINm5F cells due to a decreased receptor number without change of receptor affinity. Tunicamycin exerted no effect on the GLP-1 receptor mRNA expression. The stimulation of cAMP production was decreased in tunicamycin-treated cells. Our data show that glycosylation of the GLP-1 receptor is a precondition for regular receptor function.

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Year:  1994        PMID： 7937345     DOI： 10.1016/0196-9781(94)90095-7

Source DB:  PubMed          Journal:  Peptides        ISSN： 0196-9781            Impact factor:   3.750


  11 in total

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