Effect of glycosylation on cloned ANF-sensitive guanylyl cyclase.
Cloned ANF-sensitive guanylyl cyclase (GC-A) and ANF-sensitive guanylyl cyclase from adrenal cortex differ in their sensitivity to the ANF analogs atriopeptin 1 and urodilatin. To test the hypothesis that these differences are due to different glycosylation, we investigated the effect of the N-glycosylation inhibitor tunicamycin on GC-A. Tunicamycin altered the response of GC-A to atriopeptin 1 and urodilatin, whereas the sensitivity to ANF remained unchanged. These data indicate that agonist specificities of different ANF-sensitive guanylyl cyclases are influenced by carbohydrate moieties.
Heim
J M
JM
Abteilung für Klinische Pharmakologie, Klinikum Innenstadt der Universität, München, Germany.
Singh
S
S
Gerzer
R
R
D000302:Adrenal Cortex / Q000201:enzymology*; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000494:pharmacology*; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D003001:Cloning, Molecular; D005910:Glioma; D006031:Glycosylation; D006162:Guanylate Cyclase / Q000096:biosynthesis / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D010446:Peptide Fragments / Q000494:pharmacology; D051381:Rats; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000378:metabolism; D014162:Transfection; D014415:Tunicamycin / Q000494:pharmacology
D010446:Peptide Fragments; D011994:Recombinant Proteins; D014415:Tunicamycin; C056452:Ularitide; D009320:Atrial Natriuretic Factor; C062522:atrial natriuretic factor prohormone (103-123); D006162:Guanylate Cyclase