Accession Number : ADA300392

Title :   Regulation of Membrane Proteases Associated with Breast Cancer.

Descriptive Note : Annual rept. 1 Aug 94-31 Jul 95,

Corporate Author : GEORGETOWN UNIV WASHINGTON DC

Personal Author(s) : Goldstein, Leslie

PDF Url : ADA300392

Report Date : 28 AUG 1995

Pagination or Media Count : 12

Abstract : One of the fundamental aspects of malignant cells is their ability to invade the extracellular matrix. This capability is dependent on the elaboration of secreted and membrane bound proteases at the invasion front (invadopodia . Seprin is a 170 kDa integral membrane gelatinase that has been reported to be localized on invadopodia of metastatic LOX melanoma cells. We have screened a LOX cDNA library and isolated 10 seprin cDNA clones which range in size from 0.5 to 1.8 kb. Restriction endonuclease digestions of these clones indicate that 2 overlapping clones, lambda 50A2 and lambda 30B1 should encode the entire open reading frame for the 97 kDa monomeric subunit of seprin. Preliminary DNA sequence analysis indicates that seprin is homologous to the Fibroblast Activation Protein (FAP) which is repotted to be expressed on active fibroblasts in the stroma of breast carcinomas and other carcinomas. However, we detect seprinl FAP mRNA in the breast carcinoma cell line MDA - 436.

Descriptors :   *MEMBRANES(BIOLOGY), *DEOXYRIBONUCLEIC ACIDS, *CELLS(BIOLOGY), *MAMMARY GLANDS, *BREAST CANCER, CONTROL, ENZYMES, PROTEINS, NEOPLASMS, SEQUENCES, CLONES, FRAMES, FIBROBLASTS, READING, GELATINS, LIQUID OXYGEN, PEPTIDE HYDROLASES.

Subject Categories : Biology
      Biochemistry

Distribution Statement : APPROVED FOR PUBLIC RELEASE