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Musclide‐A1: A novel Ca 2+ ‐dependent protein kinase activator derived from musk and its cardiotonic potentiating action in guinea‐pig cardiac muscles
Author(s) -
Kimura Masayasu,
Kimura Ikuko,
Uwano Teruko,
Isoi Yukiko,
Kadota Shigetoshi,
Kikuchi Tohru
Publication year - 1991
Publication title -
phytotherapy research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.019
H-Index - 129
eISSN - 1099-1573
pISSN - 0951-418X
DOI - 10.1002/ptr.2650050404
Subject(s) - staurosporine , protein kinase c , protein kinase a , activator (genetics) , chemistry , long term potentiation , guinea pig , kinase , mechanism of action , endocrinology , medicine , biology , biochemistry , receptor , in vitro
Musclide‐A1 (6‐methyl‐2, 5‐heptanediol 5‐(hydrogen sulfate)) was isolated from musk, a dried secretion from the preputial follicle of musk deer, Moschus moschiferus Linn. Musclide (100 μg/mL), a water‐soluble extract, and musclide‐A1 (30 μg/mL) potentiated β‐adrenergic cardiotonic action in guinea‐pig papillary muscles. Musclide‐A1 at 130 μM or 1,2‐dioctanoylglycerol at 200 μM potentiated the positive inotropic action induced by the maximal concentration of isoproterenol (258 nM). The potentiation was suppressed by 3 nM staurosporine or 1 μM H‐7, an inhibitor of Ca 2+ ‐dependent protein kinase. Musclide‐A1 at 4 and 8 μM activated protein kinase C and other Ca 2+ ‐dependent protein kinase in ventricular muscles of guinea‐pig. The activation of Ca 2+ ‐dependent protein kinase was completely suppressed by 3 nM saturosporine. The activity of musclide‐A1 (4 μM) was comparable to that of 1,2‐dioctanoylglycerol (4 μM, the optimum concentration to stimulate protein kinase C), and were inhibited completely by 30 nM staurosporine. These results indicate that one mechanism of cardiotonic potentiation induced by musk, may be in part due to the activation of protein kinase C and other Ca 2+ ‐dependent protein kinases.