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Titolo:
EPITOPE-MAPPED MONOCLONAL-ANTIBODIES AS TOOLS FOR FUNCTIONAL AND MORPHOLOGICAL ANALYSES OF THE HUMAN UROKINASE RECEPTOR IN TUMOR-TISSUE
Autore:
LUTHER T; MAGDOLEN V; ALBRECHT S; KASPER M; RIEMER C; KESSLER H; GRAEFF H; MULLER M; SCHMITT M;
Indirizzi:
TECH UNIV MUNICH,KLINIKUM RECHTS ISAR,FRAUENKLIN,KLIN FORSCHERGRP,DFG,ISMANINGER STR 22 D-81675 MUNICH GERMANY TECH UNIV MUNICH,INST ORGAN CHEM & BIOCHEM D-8000 MUNICH GERMANY TECH UNIV MUNICH,FRAUENKLIN D-8000 MUNICH GERMANY TECH UNIV DRESDEN,INST PATHOL D-8027 DRESDEN GERMANY
Titolo Testata:
The American journal of pathology
fascicolo: 4, volume: 150, anno: 1997,
pagine: 1231 - 1244
SICI:
0002-9440(1997)150:4<1231:EMATFF>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR RECEPTOR; LIGAND-BINDING DOMAIN; CELL-SURFACE RECEPTOR; BREAST-CANCER; IMMUNOHISTOCHEMICAL DETECTION; OVARIAN-CANCER; AMINO-ACIDS; GLYCOSYLATION; INVASION; INVASIVENESS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
49
Recensione:
Indirizzi per estratti:
Citazione:
T. Luther et al., "EPITOPE-MAPPED MONOCLONAL-ANTIBODIES AS TOOLS FOR FUNCTIONAL AND MORPHOLOGICAL ANALYSES OF THE HUMAN UROKINASE RECEPTOR IN TUMOR-TISSUE", The American journal of pathology, 150(4), 1997, pp. 1231-1244

Abstract

uPAR (CD87), the receptor for the urokinase-type plasminogen activator (uPA) facilitates tumor cell invasion and metastasis by focusing uPAproteolytic activity to the cell surface. As uPAR exists in various molecular forms, it is desirable to use well defined antibodies for analyses of uPAR antigen expression in human malignant tumors by immunological methods. Therefore, twelve monoclonal antibodies (MAbs) directedagainst uPAR were generated by using nonglycosylated, recombinant human uPAR (spanning amino acids 1 to 284), expressed in Escherichia coli, as the immunogen. The reaction pattern of these MAbs with the immunogen and a series of carboxyl-terminally truncated versions of uPAR demonstrated that at least six different epitopes of uPAR are recognized. All MAbs reacted under reducing conditions ill immunoblot analyses with E. coli-expressed uPAR and also with highly, glycosylated, functionally intact, recombinant human uPAR expressed in Chinese hamster ovary(CHO) cells. Seven of the MAbs recognized CHO uPAR under nonreducing conditions as well By flow cytofluorometric analyses, three of these MAbs were shown to bind to native human uPAR present on the cell surface of monocytoid U937 cells with MAb IIIF10 being the best. Saturation of uPAR with uPA on U937 cells completely blocked interaction of MAb IIIF10 with uPAR (mapped epitope, amino acids 52 to 60 of domain I of uPAR). In turn, preincubation of U937 cells with MAb IIIF10 efficientlyreduced binding of uPA to uPAR, indicating that the epitope detected by MAb IIIF10 is located within or closely to the uPA-binding site of uPAR, and thus, this site may be a target to influence uPA/uPAR-mediated proteolysis in tumors. Binding of MAbs IID7 or IIIB11 (mapped epitope, amino acids 125 to 132 of domain II of uPAR) to uPAR is not affected when uPAR is occupied by uPA. As these MAbs reacted strongly with cellular uPAR antigen in formalin-fixed paraffin-embedded tumor sections, the domain-II-specific antibodies IID7 and IIIB11 may be useful forimmunohistochemical studies of uPAR expression in tissue remodeling processes In tumor invasion. In conclusion, we have devised well defined and epitope-mapped MAbs to uPAR that are highly specific tools for detection and targeting of uPAR in tumor tissue.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/07/20 alle ore 05:29:51