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A surface NAD‐glycohydrolase of human platelets may influence their aggregation
Author(s) -
Del Principe D.,
Menichelli A.,
Casini A.,
Di Giulio S.,
Mancuso G.,
Finazzi-Agrò A.
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80867-5
Subject(s) - nad+ kinase , hydrolysis , chemistry , nicotinamide , adenosine , platelet , adenosine diphosphate , biochemistry , platelet aggregation , atp hydrolysis , biophysics , enzyme , biology , immunology , atpase
Human platelets may hydrolyze externally added NAD + yielding ADPR and nicotinamide. The extent of hydrolysis is significantly higher when the platelets are stimulated. The presence of external NAD + strongly inhibits the aggregation induced by every agonist used. It seems that adenosine or ADPR itself generated by NAD + hydrolysis may be responsible for the inhibition of aggregation. Evidence is given that some of the NAD + hydrolysis product is taken up by stimulated platelets.