title: Quantitation of membrane type serine protease 1 (MT-SP1) in transformed and normal cells.
abstract: Membrane type serine protease 1 (MT-SP1) is a representative member of a large family of related enzymes known as type II transmembrane serine proteases or membrane type serine proteases. MT-SP1 has been implicated in the selective proteolysis of key extracellular substrates but its physiological role is still not fully understood. MT-SP1 expression at the protein and RNA level has been previously examined by nonquantitative methods such as in situ hybridization, Northern blotting and immunohistochemistry. To establish an introductory understanding of the quantitative mRNA expression of MT-SP1 and to correlate these levels with urokinase-type plasminogen activator receptor (uPAR), a key component of extracellular proteolysis, quantitative RT-PCR was carried out. RNA expression was analyzed in 34 human cancer cell lines, 26 human tissues and 18 primary human breast cancer tissue samples. MT-SP1 mRNA is highly expressed in many breast, ovarian, prostate and colon cancer cell lines and normal human tissues of endodermal origin. At the transcript level, MT-SP1 shows a highly statistically significant correlation (Pearson's product moment correlation r = 0.784, p < 0.001) with uPAR in human breast cancer tissue. The exact role of MT-SP1 in concert with proteins such as uPAR and other members of the plasminogen activator cascade has yet to be ascertained. However, the significant correlation between MT-SP1 and uPAR transcript levels in this initial study suggests further work to establish the role of MT-SP1 as a possible prognostic, diagnostic or therapeutic target for breast cancer.
authors.affiliation: University of California at San Francisco, School of Medicine, 513 Parnassus Ave, Box 0454, San Francisco, CA 94143, USA.
authors.forename: Ami S
authors.initials: AS
authors.lastname: Bhatt
authors.forename: Toshi
authors.initials: T
authors.lastname: Takeuchi
authors.forename: Bauke
authors.initials: B
authors.lastname: Ylstra
authors.forename: David
authors.initials: D
authors.lastname: Ginzinger
authors.forename: Donna
authors.initials: D
authors.lastname: Albertson
authors.forename: Marc A
authors.initials: MA
authors.lastname: Shuman
authors.forename: Charles S
authors.initials: CS
authors.lastname: Craik
mesh_terms: D000328:Adult; D000368:Aged; D000369:Aged, 80 and over; D001943:Breast Neoplasms / Q000201:enzymology / Q000378:metabolism / Q000473:pathology; D002461:Cell Line, Transformed; D004847:Epithelial Cells / Q000166:cytology / Q000201:enzymology; D005260:Female; D006801:Humans; D008565:Membrane Proteins / Q000096:biosynthesis* / Q000235:genetics; D008875:Middle Aged; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000096:biosynthesis / Q000235:genetics; D011956:Receptors, Cell Surface / Q000096:biosynthesis / Q000378:metabolism; D055293:Receptors, Urokinase Plasminogen Activator; D020133:Reverse Transcriptase Polymerase Chain Reaction / Q000379:methods; D012697:Serine Endopeptidases / Q000096:biosynthesis* / Q000235:genetics; D014018:Tissue Distribution; D014158:Transcription, Genetic; D014407:Tumor Cells, Cultured
chemical_list: D008565:Membrane Proteins; C524898:PLAUR protein, human; D012333:RNA, Messenger; D011956:Receptors, Cell Surface; D055293:Receptors, Urokinase Plasminogen Activator; D012697:Serine Endopeptidases