Document Detail


Investigation of the mechanism of the interaction of tubulin with derivatives of 2-styrylquinazolin-4(3H)-one.
MedLine Citation:
PMID:  1944246     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A new class of antimitotic agents, derivatives of 2-styrylquinazolin-4(3H)-one (SQZ), was recently described [J. Med. Chem. 33:1721-1728 (1990)]. Because they appeared to interact at a new ligand binding site on tubulin, we attempted to determine their mechanism of action as inhibitors of tubulin polymerization. Although in initial studies inhibition of colchicine binding was negligible, substantial and competitive inhibition of this reaction could be demonstrated with very short incubation times (less than 5 min), provided that a relatively low colchicine to tubulin ratio was used. The initial apparent failure to inhibit colchicine binding resulted from extremely rapid binding to tubulin and dissociation from tubulin by the SQZ derivatives, in comparison with the slow, temperature-dependent, poorly reversible binding of colchicine. The most inhibitory of the SQZ derivatives in the colchicine binding assay was 6-methyl-2-styrylquinazolin-4(3H)-one (NSC 379310), and its interaction with tubulin, particularly as an inhibitor of colchicine binding, was compared with that of 2-methoxy-5-(2',3',4'-trimethoxyphenyl)tropone (MTPT), because the binding parameters of MTPT with tubulin have been well described. The data indicate that NSC 379310 binds to tubulin and dissociates from the protein about 3 times as rapidly as MTPT. The other SQZ derivatives with equal or greater potency as inhibitors of tubulin polymerization but apparently less potency as inhibitors of colchicine binding presumably bind to and/or dissociate from tubulin even more rapidly than does NSC 379310.
Authors:
C M Lin; G J Kang; M C Roach; J B Jiang; D P Hesson; R F Luduena; E Hamel
Related Documents :
1567846 - Colchicine photosensitizes covalent tubulin dimerization.
19409876 - Adp-ribosylation factor like 7 (arl7) interacts with alpha-tubulin and modulates intrac...
18763866 - Nbs1 prevents chromatid-type aberrations through atm-dependent interactions with smc1.
6098966 - Studies on the property of sulfhydryl binding site on the lung normal and cancer cell m...
7526146 - Pcp/nmda receptor-channel complex and brain development.
9100026 - Auxilin-induced interaction of the molecular chaperone hsc70 with clathrin baskets.
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Molecular pharmacology     Volume:  40     ISSN:  0026-895X     ISO Abbreviation:  Mol. Pharmacol.     Publication Date:  1991 Nov 
Date Detail:
Created Date:  1991-12-19     Completed Date:  1991-12-19     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  0035623     Medline TA:  Mol Pharmacol     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  827-32     Citation Subset:  IM    
Affiliation:
Laboratory of Molecular Pharmacology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Antineoplastic Agents / metabolism*
Binding Sites
Colchicine / metabolism
Guanosine Triphosphate / metabolism
Quinazolines / metabolism*
Styrenes / metabolism*
Tropolone / analogs & derivatives,  metabolism
Tubulin / metabolism*
Chemical
Reg. No./Substance:
0/Antineoplastic Agents; 0/Quinazolines; 0/Styrenes; 0/Tubulin; 4765-58-6/2-styrylquinazolin-4(3H)-one; 533-75-5/Tropolone; 60423-21-4/2-methoxy-5-(2',3',4'-trimethoxyphenyl)tropone; 64-86-8/Colchicine; 86-01-1/Guanosine Triphosphate

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Estrogen receptor stereochemistry: ligand binding orientation and influence on biological activity.
Next Document:  Species differences in the toxicity and cytochrome P450 IIIA-dependent metabolism of digitoxin.