Accession Number : ADA318157
Title : Regulation of Membrane Protease Associated with Breast Cancer.
Descriptive Note : Annual rept. 1 Aug 95-31 Jul 96,
Corporate Author : GEORGETOWN UNIV WASHINGTON DC
Personal Author(s) : Goldstein, Leslie
PDF Url : ADA318157
Report Date : AUG 1996
Pagination or Media Count : 15
Abstract : We initially proposed to determine the role of mp 170 seprase in the metastasis of breast cancer. The mp170 seprase exhibits its highest identity (94%) with the integral membrane protein Fibroblast Activation Protein Alpha (FAP)that is expressed in vivo in carcinomas and sarcomas but whose function is unknown. The in vitro breast carcinoma line MDA-MB-436 which is known to express mp170 seprase would appear to be a good candidate for transfection experiments with sense and antisense cDNA constructs of mp170 seprase. Using the in vitro extracellular matrix (ECM) invasion/degradation assay we could monitor the effects of the overexpression and underexpression of this gelatinase on the invasive phenotype of MDA-MB-436 as well as other cell lines (MDA-MB-231 etc.) at various stages of neoplastic development. The deduced amino acid sequence predicts a type II integral membrane protein of 760 amino acids. And its carboxyl terminus contains a putative catalytic region which is homologous to the nonclassical serine protease subfamily represented by the ectopeptidase Dipeptidyl Peptidase IV (DPPIV). Therefore, our first priority is to isolate a cDNA clone that encodes the entire open reading frame(ORF) of mp170 seprase.
Descriptors : *MEMBRANES(BIOLOGY), *BREAST CANCER, DEGRADATION, ENZYMES, PROTEINS, ISOLATION, NEOPLASMS, DEOXYRIBONUCLEIC ACIDS, IN VITRO ANALYSIS, CATALYSIS, IN VIVO ANALYSIS, ASSAYING, AMINO ACIDS, PEPTIDE HYDROLASES, SERINE, CARBOXYL RADICALS, METASTASIS.
Subject Categories : Biochemistry
Anatomy and Physiology
Medicine and Medical Research
Distribution Statement : APPROVED FOR PUBLIC RELEASE