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Titolo:
MONOCLONAL-ANTIBODIES DIFFERENTIALLY REACTIVE WITH NATIVE AND REDUCTIVELY MODIFIED BOWMAN-BIRK PROTEASE INHIBITOR
Autore:
WAN XS; KOCH CJ; LORD EM; MANZONE H; BILLINGS PC; DONAHUE JJ; ODELL CS; MILLER JH; SCHMIDT NA; KENNEDY AR;
Indirizzi:
UNIV PENN,SCH MED,DEPT RADIAT ONCOL,530 CLIN RES BLDG,415 CURIE BLVD PHILADELPHIA PA 19104 UNIV ROCHESTER,CTR CANC ROCHESTER NY 14642
Titolo Testata:
Journal of immunological methods
fascicolo: 1, volume: 180, anno: 1995,
pagine: 117 - 130
SICI:
0022-1759(1995)180:1<117:MDRWNA>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
NF-KAPPA-B; TRANSFORMATION INVITRO; C3H-10T1/2 CELLS; TRANSCRIPTION; ACTIVATION; SOYBEANS; PROTEINS; BINDING; H2O2;
Keywords:
BOWMAN-BIRK PROTEASE INHIBITOR; MONOCLONAL ANTIBODY; BOWMAN-BIRK PROTEASE INHIBITOR REDUCTION; CHEMOPREVENTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
30
Recensione:
Indirizzi per estratti:
Citazione:
X.S. Wan et al., "MONOCLONAL-ANTIBODIES DIFFERENTIALLY REACTIVE WITH NATIVE AND REDUCTIVELY MODIFIED BOWMAN-BIRK PROTEASE INHIBITOR", Journal of immunological methods, 180(1), 1995, pp. 117-130

Abstract

Bowman-Birk protease inhibitor (BBI) is a potent anticarcinogen that suppresses malignant transformation at nanomolar concentrations. Smallamounts of BBI in its native form can be measured by immunoassay using specific monoclonal antibodies (MAbs); however, the MAbs currently available are not capable of detecting BBI metabolites in human body fluids. To develop new reagents for the study of BBI exposure and pharmocokinetics, we produced four MAbs, designated 3B6, 3E3, 4H8 and 5G2, from hybridomas derived from a mouse immunized with reductively modified BBI. The epitopes recognized by the four MAbs were characterized using BBI in its native form or modified by different methods. MAb 3B6 reacted with native BBI. Partial reduction of BBI with 720 Gy of gamma radiation in an oxygen-free solution of 100 mM formate increased the reactivity of BBI with 3B6; however, extensive reduction of BBI with 100mM DL-dithiothreitol (DTT) completely abolished this antigenic reactivity. In contrast, the other three MAbs reacted with BBI molecules that had been reduced either with 720 Gy of radiation in formate solutionor with DTT. Alkylation of the radiochemically reduced BBI with N-ethylmaleimide further increased the reactivity of BBI with 3E3, 4H8 and 5G2, possibly by preventing the formation of new disulfide bonds within the BBI molecules. The binding of 4H8 and 5G2 to BBI antigen was inhibited by the binding of 3E3, and vice versa. Thus, the epitopes recognized by 3E3, 4H8 and 5G2 are probably located close to one another onthe reduced BBI molecules. These three MAbs were able to react with BBI metabolites in urine samples collected from volunteers after oral administration of BBI. The ability of these MAbs to detect BBI metabolites indicates that BBI may be reductively modified in vivo and these MAbs may be useful reagents for monitoring the uptake of BBI into humantissues in cancer chemoprevention studies with BBI.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/10/20 alle ore 06:28:43