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Titolo:
Proteolytic fragments of anti-HIV and anti-tumor proteins MAP30 and GAP31 are biologically active
Autore:
Huang, PL; Sun, YT; Chen, HC; Kung, HF; Huang, PL; Lee-Huang, S;
Indirizzi:
NYU, Sch Med, Dept Biochem, New York, NY 10016 USA NYU New York NY USA 10016 , Sch Med, Dept Biochem, New York, NY 10016 USA Amer Biosci, New York, NY 10021 USA Amer Biosci New York NY USA 10021Amer Biosci, New York, NY 10021 USA NICHHD, Endocrinol & Reprod Res Branch, NIH, Bethesda, MD 20892 USA NICHHD Bethesda MD USA 20892 prod Res Branch, NIH, Bethesda, MD 20892 USA Univ Hong Kong, Inst Mol Biol, Hong Kong, Hong Kong Univ Hong Kong Hong Kong Hong Kong Inst Mol Biol, Hong Kong, Hong Kong Massachusetts Gen Hosp, Dept Med, Boston, MA 02114 USA Massachusetts Gen Hosp Boston MA USA 02114 Dept Med, Boston, MA 02114 USA Harvard Univ, Sch Med, Boston, MA 02114 USA Harvard Univ Boston MA USA 02114 vard Univ, Sch Med, Boston, MA 02114 USA
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 3, volume: 262, anno: 1999,
pagine: 615 - 623
SICI:
0006-291X(19990907)262:3<615:PFOAAA>2.0.ZU;2-Z
Fonte:
ISI
Lingua:
ENG
Soggetto:
POKEWEED ANTIVIRAL PROTEIN; RICIN-A-CHAIN; INHIBITION; ANGSTROM; GAP-31; DNA; REPLICATION; INFECTION; TYPE-1; MAP-30;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
28
Recensione:
Indirizzi per estratti:
Indirizzo: Lee-Huang, S NYU, Sch Med, Dept Biochem, New York, NY 10016 USA NYU New York NY USA 10016 pt Biochem, New York, NY 10016 USA
Citazione:
P.L. Huang et al., "Proteolytic fragments of anti-HIV and anti-tumor proteins MAP30 and GAP31 are biologically active", BIOC BIOP R, 262(3), 1999, pp. 615-623

Abstract

We analyzed the structural and functional organization of anti-HIV and anti-tumor proteins MAP30 and GAP31 by limited proteolysis with endopeptidasesLys-C and Glu-C (V8), MAP30 and GAP31 are resistant to proteolytic digestion under conditions of as much as 5% (w/w) proteases. In the presence of 10% (w/w) protease, the central regions of the proteins are still. resistant to proteolysis, whereas the N- and C-termini are accessible. Peptide fragments were purified by FPLC on Superdex 75 columns, characterized by gel electrophoresis, identified by amino acid sequencing, and analyzed for anti-HIV, anti-tumor, and other biochemical activities. We report here that limitedproteolysis yields biologically active fragments of both MAP30 and GAP31. These fragments are active against HIV-1 and tumor cells with EC(50)s in the sub-nanomolar ranges, 0.2-0.4 nM. At the dose levels used in the assays, little cytotoxicity to normal cells was observed. In addition, these fragments remain fully active in HIV-integrase inhibition and HIV-LTR topologicalinactivation, but not ribosome inactivation. These results demonstrate that the antiviral and anti-tumor activities of MAP30 and GAP31 are independent of ribosome inactivation activity. In addition, we demonstrate that portions of the N- and C-termini are not essential for antiviral and anti-tumor activities, but do appear to be required for ribosome inactivation. These results may provide novel strategies for rational design and targeted development of mimetic antiviral and anti-tumor therapeutics, (C) 1999 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/01/20 alle ore 20:42:25