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. 1972 Nov;69(11):3175–3179. doi: 10.1073/pnas.69.11.3175

Biochemical Characterization and Cytochemical Localization of a Catecholamine-Sensitive Adenylate Cyclase in Isolated Capillary Endothelium

Roger C Wagner *, Peter Kreiner , Russell J Barrnett *, Mark W Bitensky
PMCID: PMC389729  PMID: 4564206

Abstract

Capillaries were isolated from epididymal fat, and a catecholamine-sensitive adenylate cyclase found in these capillaries was characterized. The effect of various hormones on the accumulation of adenosine 3′:5′-cyclic monophosphate in capillary endothelial cells was determined and the cyclase was found to exhibit mixed alpha and beta characteristics. Cyclase was cytochemically localized in these endothelial cells with 5′-adenylyl-imidodiphosphate as a specific cyclase substrate and alloxan as a specific cyclase inhibitor. Lead imidodiphosphate was precipitated at or near the site of cyclase activity upon hydrolysis of 5′-adenylyl-imidodiphosphate by cyclase. This reaction product was observed primarily on the luminal surface of intact capillaries, in micropinocytic invaginations, in free vesicles within the cytoplasm, and in the intracellular junctions.

Keywords: micropinocytosis, AMP-PNP, alloxan, intercellular junctions

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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