Abstract
Extracellular ATP is found to produce a variety of important biological responses. Ecto-ATPases are located on numerous cell types in many different species, regulate extracellular ATP levels and can be a key step in generating adenosine. Studies conducted on chicken ecto-ATPases from liver and cardiac and smooth muscle show a variety of differing properties including (1) different apparent Km's, (2) lectin sensitivity, (3) responses to detergents, (4) responses to lipid mediators, and (5) responsiveness to nucleotide-mimetic affinity labels. These results suggest that although each enzyme hydrolyzes extracellular ATP, they should each be viewed as a distinct subtype of the whole ecto-ATPase family due to their differential responses, largely linked to proposed regulatory phenomenon.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenosine Triphosphatases / drug effects
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Adenosine Triphosphatases / metabolism
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Adenosine Triphosphatases / physiology*
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Adenosine Triphosphate / pharmacology
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Animals
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Chickens
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Concanavalin A / pharmacology
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Detergents
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Diacylglycerol Kinase / antagonists & inhibitors
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Erythrosine / pharmacology
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Kinetics
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Lipid Metabolism
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Microsomes, Liver / drug effects
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Microsomes, Liver / enzymology
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Muscle Proteins / drug effects
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Muscle Proteins / metabolism
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Muscle Proteins / physiology*
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Muscle, Smooth / drug effects
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Muscle, Smooth / enzymology
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Myocardium / enzymology
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Octoxynol
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Solubility
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Sphingosine / analogs & derivatives
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Sphingosine / pharmacology
Substances
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Detergents
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Muscle Proteins
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Concanavalin A
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Adenosine Triphosphate
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Octoxynol
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Diacylglycerol Kinase
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Adenosine Triphosphatases
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ectoATPase
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N,N-dimethylsphingosine
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Sphingosine
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Erythrosine