1-o-sulfatobastadins-1 and -2 from ianthella basta (pallas).antagonists of the yr1-fkbp12 ca2+ channel1-o-sulfatobastadins-1和2从ianthella basta(雅典娜)。.pdfVIP

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1-o-sulfatobastadins-1 and -2 from ianthella basta (pallas).antagonists of the yr1-fkbp12 ca2+ channel1-o-sulfatobastadins-1和2从ianthella basta(雅典娜)。.pdf

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1-o-sulfatobastadins-1and-2fromianthellabasta(pallas).antagonistsoftheyr1-fkbp12ca2channel1-o-sulfatobastadins-1和2从ianthellabasta(雅典娜)。

Marine Drugs 2004, 2, 176-184 Marine Drugs ISSN 1660-3397 /marinedrugs/ 1-O-Sulfatobastadins-1 and -2 from Ianthella basta (Pallas). Antagonists of the RyR1-FKBP12 Ca2+ Channel Makoto N. Masuno 1, Alexander C. Hoepker 1, Isaac N. Pessah 2 and Tadeusz F. Molinski 1,* 1Department of Chemistry, University of California, Davis, CA 95616, USA. 2Department of Molecular Biosciences, University of California, Davis, CA 95616, USA. * Author to whom correspondence should be addressed; Tel. +1 (530) 752-6358, Fax (530) 752-8995. E-mail: tfmolinski@ Received: 29 July 2004 / Accepted: 14 October 2004 / Published: 25 November 2004 Abstract: Two new sulfate monoesters of hemibastadins-1 and -2 were isolated from the marine sponge Ianthella basta (Pallas) from Guam. A third new compound was tentatively assigned the structure 34-O-sulfatobastadin-9. The 1-O-sulfatohemibastadins-1 and –2 were antagonists of the RyR1-FKBP12 Ca2+ channel under conditions where the known compound bastadin-5 exhibits potent agonism (EC50 2 µM). Keywords: Bromotyrosine, calcium channel, Porifera, ryanodine receptor. Introduction The release of Ca2+ from stores of the sarcoplasmic reticulum (SR) stimulates contraction of striated muscle fibers through ATP hydrolysis coupled to induced conformational changes of the actin-myosin protein complex. In 1994, we discovered that the known bromotyrosine tetramer, bastadin-5 (1)[1] from the marine sponge Ianthella basta (Pallas), is a potent modulator of Ca2+ release from the SR[2]. Bastadin-5 stimulates release of Ca2+ from the SR by binding to the RyR1-FKB