Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2
Autore:
Schimmer, AD; Hedley, DW; Chow, S; Pham, NA; Chakrabartty, A; Bouchard, D; Mak, TW; Trus, MR; Minden, MD;
Indirizzi:
Univ Hlth Network, Princess Margaret Hosp, Toronto, ON M5G 2M9, Canada Univ Hlth Network Toronto ON Canada M5G 2M9 , Toronto, ON M5G 2M9, Canada Amgen Inst, Toronto, ON, Canada Amgen Inst Toronto ON CanadaAmgen Inst, Toronto, ON, Canada
Titolo Testata:
CELL DEATH AND DIFFERENTIATION
fascicolo: 7, volume: 8, anno: 2001,
pagine: 725 - 733
SICI:
1350-9047(200107)8:7<725:TBDOBF>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
MITOCHONDRIAL PERMEABILITY TRANSITION; P-GLYCOPROTEIN; CELL-DEATH; LEUKEMIA-CELLS; MULTIDRUG TRANSPORTER; HYDROPHOBIC PEPTIDES; FLOW-CYTOMETRY; DRUG TRANSPORT; 3RD HELIX; EXPRESSION;
Keywords:
apoptosis; alpha helix; mitochondria; Bcl-2; caspases;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Minden, MD Univ Hlth Network, Princess Margaret Hosp, Room 9-111,610 Univ Ave, Toronto, ON M5G 2M9, Canada Univ Hlth Network Room 9-111,610 Univ Ave Toronto ON Canada M5G 2M9
Citazione:
A.D. Schimmer et al., "The BH3 domain of BAD fused to the Antennapedia peptide induces apoptosis via its alpha helical structure and independent of Bcl-2", CELL DEAT D, 8(7), 2001, pp. 725-733

Abstract

Since the over-expression of Bcl-2 is a common cause of multi-drug resistance, cytotoxic peptides that overcome the effects of Bcl-2 may be clinically useful. We harnessed the death-promoting alpha helical properties of the BH3 domain of BAD by fusing it to the Antennapedia (ANT) domain, which allows for cell entry (ANTBH3BAD). Treatment of 32D cells with the ANTBH3BAD peptide results in a 99% inhibition of colony formation. No significant toxicity is observed after treatment with ANT or BH3BAD alone. A mutant fusion peptide unable to bind Bcl-2 induces cell death as effectively as the wild-type ANTBH3BAD, Furthermore, 32D cells over-expressing Bcl-2 show no resistance to the ANTBH3BAD peptide, Therefore, the toxicity of the peptide was independent of the Bcl-2 pathway, We demonstrate that the toxicity of the peptide is due to its alpha helicity that disrupts mitochondrial function. Since this peptide overcomes major forms of drug resistance, it may be therapeutically useful if appropriately targeted to malignant cells.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/07/20 alle ore 10:01:43