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Titolo:
Non-natural CBP2 binding peptides and peptomers modulate carcinoma cell adhesion and invasion
Autore:
Hebert, C; Coletta, RD; Norris, K; Nikitakis, N; Lopes, M; Sauk, JJ;
Indirizzi:
Univ Maryland, Sch Dent, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 d, Sch Dent, Baltimore, MD 21201 USA Univ Maryland, Dept Pathol, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 Dept Pathol, Baltimore, MD 21201 USA Univ Maryland, UMB Greenebaum Canc Ctr, Baltimore, MD 21201 USA Univ Maryland Baltimore MD USA 21201 um Canc Ctr, Baltimore, MD 21201 USA Univ Campinas Piracicaba, Dept Oral Pathol, Sao Paulo, Brazil Univ Campinas Piracicaba Sao Paulo Brazil ral Pathol, Sao Paulo, Brazil
Titolo Testata:
JOURNAL OF CELLULAR BIOCHEMISTRY
fascicolo: 1, volume: 82, anno: 2001,
pagine: 145 - 154
SICI:
0730-2312(2001)82:1<145:NCBPAP>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
CATION-PI INTERACTIONS; VASOACTIVE-INTESTINAL-PEPTIDE; SHOCK PROTEIN HSP47; IV COLLAGEN; ALPHA(3)BETA(1) INTEGRIN; C4 DOMAIN; RECEPTOR; PROCOLLAGEN; ALPHA-1(IV)531-543; EXPRESSION;
Keywords:
CBP2; colligin2; Hsp47; integrin; carcinoma; bacteriophage; targeting;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Sauk, JJ Univ Maryland, Sch Dent, 666 W Baltimore St, Baltimore, MD 21201 USA Univ Maryland 666 W Baltimore St Baltimore MD USA 21201 21201 USA
Citazione:
C. Hebert et al., "Non-natural CBP2 binding peptides and peptomers modulate carcinoma cell adhesion and invasion", J CELL BIOC, 82(1), 2001, pp. 145-154

Abstract

A combinatorial approach that utilized a repertoire of bacteriophage-peptides has identified a number of non-natural CBP2 binding peptides. Moreover,co-localization of some of these peptides with CBP2 in a number of tumor cell lines demonstrated that the peptides were directed to an intracellular location spatially coincident with the normal distribution of CBP2 [Sauk etat., 2000]. From among these sequences WHYPWFQNWAMA and LDSRYSLQAAMY were the most effective CBP2 binding peptides and best fulfilled the combinatorial motif containing deep hydrophobic pockets. When the hydropathic profilesof collagen alpha1(IV) and alpha2(IV) were compared with these dodecapeptides, the hydropathic profiles of WHYPWFQNWAMA and LDSRYSLQAAMY closely matched those of alpha1(IV) 414-452 and alpha1(IV)531-543. These peptides were shown to be functional peptidomimics and possessed the ability to alter cell adhesion and invasion of human squamous cell carcinoma cell lines. Peptomers were formed of these non-natural peptides to explore the role that a repetitive peptide may have on cell adhesion. The enhanced cell adhesion observed with the peptomers required both CBP2 antibodies and integrin antibodies for inhibition. The enhanced adhesion observed even in the face of combined antibody inhibition was consistent with such complexes possessing correspondingly slower dissociation rates. Thus, suggesting that peptomers may function in a like manner to multimeric peptide MHC complexes (tetramers) binding more than one cell receptor on a specific cell. These findings evoke both peptidomimics of native ligands and their peptomers as potential reagents by which to target tumor cells for chemotherapy, imaging, or retargeting viral vectors for gene therapy.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 30/03/20 alle ore 19:15:49