Functional Role for Glycosylated Subtypes of Rat Endothelin Receptors

Glycosylation of endothelin (ET) receptors was found to occur in rat cerebellar and atrial membranes. Specifically, we investigated whether the ETAand ETBreceptor subtypes differed in their sensitivity to deglycosylation treatment and whether the two affinity states (nanomolar and picomolar) observe...

Full description

Saved in:
Bibliographic Details
Published in:Biochemical and biophysical research communications 1998-05, Vol.246 (2), p.495-500
Main Authors: Shraga-Levine, Z., Sokolovsky, M.
Format: Article
Language:English
Subjects:
Amidohydrolases
Animals
Binding Sites
Cerebellum - metabolism
Endothelin-1 - metabolism
Glycosylation
Heart Atria - metabolism
Hexosaminidases
In Vitro Techniques
Kinetics
Lectins
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase
Rats
Receptor, Endothelin A
Receptor, Endothelin B
Receptors, Endothelin - chemistry
Receptors, Endothelin - classification
Receptors, Endothelin - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Glycosylation of endothelin (ET) receptors was found to occur in rat cerebellar and atrial membranes. Specifically, we investigated whether the ETAand ETBreceptor 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 ETAreceptor contribute to the binding of ligand to the nanomolar-affinity binding sites, but not to the picomolar-affinity binding sites.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.1998.8646