Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adrenal Cortex / enzymology*
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Animals
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Atrial Natriuretic Factor / pharmacology*
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Cell Line
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Cell Membrane / enzymology
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Cloning, Molecular
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Glioma
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Glycosylation
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Guanylate Cyclase / biosynthesis
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Guanylate Cyclase / metabolism*
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Kinetics
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Molecular Weight
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Peptide Fragments / pharmacology
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Rats
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / metabolism
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Transfection
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Tunicamycin / pharmacology
Substances
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Peptide Fragments
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Recombinant Proteins
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Tunicamycin
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Ularitide
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Atrial Natriuretic Factor
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atrial natriuretic factor prohormone (103-123)
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Guanylate Cyclase