Functional Role for Glycosylated Subtypes of Rat Endothelin Receptors

• Published in: Biochemical and biophysical research communications Vol. 246; no. 2; pp. 495 - 500
• Main Authors: Shraga-Levine, Z., Sokolovsky, M.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 19.05.1998
• 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
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1998.8646

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.