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Titolo:
STRUCTURAL AND FUNCTIONAL-RELATIONSHIPS OF TOYOCAMYCIN ON NPM-TRANSLOCATION
Autore:
FINCH RA; REVANKAR GR; CHAN PK;
Indirizzi:
BAYLOR COLL MED,DEPT PHARMACOL HOUSTON TX 77030 BAYLOR COLL MED,DEPT PHARMACOL HOUSTON TX 77030 ARONEX PHARMACEUT INC THE WOODLANDS TX 77380
Titolo Testata:
Anti-cancer drug design
fascicolo: 3, volume: 12, anno: 1997,
pagine: 205 - 215
SICI:
0266-9536(1997)12:3<205:SAFOTO>2.0.ZU;2-2
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOLAR PROTEIN-B23 TRANSLOCATION; POLYACRYLAMIDE-GEL ELECTROPHORESIS; NUCLEAR MATRIX PROTEIN; HEPATOMA ASCITES-CELLS; MURINE TUMOR-CELLS; HELA-CELLS; NUCLEOSIDES; B23; PHOSPHOPROTEIN-B23; B23-TRANSLOCATION;
Keywords:
NPM-TRANSLOCATION; NUCLEOPHOSMIN; B23; TOYOCAMYCIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
39
Recensione:
Indirizzi per estratti:
Citazione:
R.A. Finch et al., "STRUCTURAL AND FUNCTIONAL-RELATIONSHIPS OF TOYOCAMYCIN ON NPM-TRANSLOCATION", Anti-cancer drug design, 12(3), 1997, pp. 205-215

Abstract

Toyocamycin is an antitumor antibiotic which has a pyrrolo[2,3-D]pyrimidine aglycone with a -CN substituent on the 5-carbon. Treatment of HeLa cells with toyocamycin induces redistribution of the nuclear phosphoprotein nucleophosmin/B23 (NPM) from nudeoli to nucleoplasm (NPM-translocation) which can be detected by immunofluorescence. NPM-translocation is useful in showing drug effects and in detecting drug-resistantcancer cells. To study which structural features of toyocamycin are important for NPM-translocation, we used toyocamycin analogs in which the 5-position -CN was either deleted (tubercidin) or replaced with a -CONH2 (sangivamycin) or -C(NOH)NH2. HeLa cells were incubated with these analogs for 4 h and assayed for NPM-translocation by immunofluorescence. We found that the analog with the deletion of the -CN group (tubercidin) did not induce translocation while those with replacement of the -CN group with -CONH2 or -C(NOR)NH2 retained the NPM-translocationactivity. When these or similar modifications were applied to 7-deazaguanosine, none of the guanosine analogs were effective. These resultsindicate that modifications at the 5-position of the pyrrolo[2,3-D]pyrimidine ring and a structure similar to adenine rather than guanine are essential for NPM-translocation. Since inhibition of RNA synthesis did not induce NPM-translocation, our results suggest that interference with NPM's binding in nucleoli by these analogs causes NPM-translocation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/09/20 alle ore 16:07:26