Abstract:
:Glycosylation of endothelin (ET) receptors was found to occur in rat cerebellar and atrial membranes. Specifically, we investigated whether the ETA and ETB receptor subtypes differed in their sensitivity to deglycosylation treatment and whether the two affinity states (nanomolar and picomolar) observed in each receptor subtype reflect differences in glycosylation states. Pretreatment of cerebellar or atrial membranes with endoglycosidase H (endo H) caused a marked decrease in the number of maximal binding sites that bind ligand with nanomolar affinity, whereas ligand affinity remained the same. The picomolar-affinity binding sites were not affected by endo H. The use of specific antagonists indicated that the receptor subtype most likely to be influenced by glycosylation is ETA. We suggest that in both cerebellar and atrial membranes, the carbohydrate chains of the ETA receptor contribute to the binding of ligand to the nanomolar-affinity binding sites, but not to the picomolar-affinity binding sites.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Shraga-Levine Z,Sokolovsky Mdoi
10.1006/bbrc.1998.8646subject
Has Abstractpub_date
1998-05-19 00:00:00pages
495-500issue
2eissn
0006-291Xissn
1090-2104pii
S0006-291X(98)98646-6journal_volume
246pub_type
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