Interactions of cryptosin with mammalian cardiac dihydropyridine-specific calcium channels

Journal Article · Mon Jan 01 04:00:00 EST 1990 · Life Sciences; (USA)

DOI:https://doi.org/10.1016/0024-3205(90)90373-Y· OSTI ID:6254267

Rao, V R; Banning, J W ^[1]

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1. Wayne State Univ., Detroit, MI (USA)

Cryptosin, a new cardenolide, was found to be a potent inhibitor of cardiac Na{sup +} and K{sup +} dependent Adenosinetri-phosphatase. In experiments with dog heart ex vivo, development of inotropic and toxic effect correlated with changes in the cardiac dihydropyridine-specific calcium channels as measured by the binding of {sup 3}(H)PN 200-110. A significant change in the PN 200-110 binding was observed when guinea pig and dog heart sarcolemmal membranes were pre-incubated with cryptosin in vitro. Binding analysis of {sup 3}(H)PN 200-110 (Isradipine), a 1,4-dihydropyridine analog with very specific calcium channel binding properties, in both in vitro and ex vivo studies were consistent and indicated a non-specific type of interaction of cryptosin with mammalian cardiac 1,4-dihydropyridine-specific calcium channels.

• OSTI ID: 6254267
• Journal Information: Life Sciences; (USA), Journal Name: Life Sciences; (USA) Vol. 47:18; ISSN 0024-3205; ISSN LIFSA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
ACID ANHYDRASES
ALKALINE EARTH METALS
ANIMALS
ATP-ASE
AZINES
BIOCHEMICAL REACTION KINETICS
BODY
CALCIUM
CARDIOVASCULAR SYSTEM
CELL CONSTITUENTS
CELL MEMBRANES
DOGS
ELEMENTS
ENZYME INHIBITORS
ENZYMES
GUINEA PIGS
HEART
HETEROCYCLIC COMPOUNDS
HYDROGEN COMPOUNDS
HYDROLASES
ISOTOPE APPLICATIONS
KINETICS
MAMMALS
MEMBRANE PROTEINS
MEMBRANES
METALS
ORGANIC COMPOUNDS
ORGANIC NITROGEN COMPOUNDS
ORGANS
PHOSPHOHYDROLASES
PORINS
PROTEINS
PYRIDINES
REACTION KINETICS
RECEPTORS
RODENTS
TRACER TECHNIQUES
TRITIUM COMPOUNDS
VERTEBRATES