TY - JOUR
T1 - The interaction of phomopsin A with bovine brain tubulin
AU - Ludueña, Richard F.
AU - Prasad, Veena
AU - Roach, Mary Carmen
AU - Lacey, Ernest
N1 - Funding Information:
is based on work supported by Grants the National Institutes of Health and the Robert Welch Foundation to R.F.L. correspondence should be addressed.
PY - 1989/7
Y1 - 1989/7
N2 - Phomopsin A is an anti-mitotic compound from the fungus Phomopsis leptostromiformis which is a potent inhibitor of microtubule assembly in vitro; like maytansine, it is known to compete with vinblastine for binding to tubulin (E. Lacey, J. A. Edgar, and C. C. J. Culvenor (1987) Biochem. Pharmacol. 36, 2133-2138). A major difference between the effects of maytansine and vinblastine is that vinblastine is a potent inhibitor of tubulin decay, whereas maytansine has little or no effect on decay. Since phomopsin A is structurally distinct from either maytansine or vinblastine, tubulin decay may be measured by either the time-dependent loss of the ability to bind to [3H]colchicine or the time-dependent increase in the binding of bis(8-anilinonaphthalene 1-sulfonate) (BisANS) to tubulin. By either method, phomopsin A was found to be a much stronger inhibitor of tubulin decay than is vinblastine or any other drug yet tested, and, in fact, when decay is measured by the increase of BisANS binding, phomopsin A appears to stop the process entirely. This may prove to be useful in the determination of the higherorder structure of the tubulin molecule.
AB - Phomopsin A is an anti-mitotic compound from the fungus Phomopsis leptostromiformis which is a potent inhibitor of microtubule assembly in vitro; like maytansine, it is known to compete with vinblastine for binding to tubulin (E. Lacey, J. A. Edgar, and C. C. J. Culvenor (1987) Biochem. Pharmacol. 36, 2133-2138). A major difference between the effects of maytansine and vinblastine is that vinblastine is a potent inhibitor of tubulin decay, whereas maytansine has little or no effect on decay. Since phomopsin A is structurally distinct from either maytansine or vinblastine, tubulin decay may be measured by either the time-dependent loss of the ability to bind to [3H]colchicine or the time-dependent increase in the binding of bis(8-anilinonaphthalene 1-sulfonate) (BisANS) to tubulin. By either method, phomopsin A was found to be a much stronger inhibitor of tubulin decay than is vinblastine or any other drug yet tested, and, in fact, when decay is measured by the increase of BisANS binding, phomopsin A appears to stop the process entirely. This may prove to be useful in the determination of the higherorder structure of the tubulin molecule.
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U2 - 10.1016/0003-9861(89)90191-4
DO - 10.1016/0003-9861(89)90191-4
M3 - Article
C2 - 2735765
AN - SCOPUS:0024375550
SN - 0003-9861
VL - 272
SP - 32
EP - 38
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 1
ER -