Quantitation of Membrane Type Serine Protease 1 (MT-SP1) in Transformed and Normal Cells
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A.S. Bhatt
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. MTSP1 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 urokinasetype 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 (Pearsons 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.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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Articles in the same Issue
- Obituary
- Thrombin Signaling in the Brain: The Role of Protease-Activated Receptors
- Transcriptional Repression of the Human p53 Gene by Hepatitis B Viral Core Protein (HBc) in Human Liver Cells
- Identification of Cytosolic Leucyl Aminopeptidase (EC 3.4.11.1) as the Major Cysteinylglycine-Hydrolysing Activity in Rat Liver
- A Novel Influenza A Virus Activating Enzyme from Porcine Lung: Purification and Characterization
- Binding of Urokinase Plasminogen Activator to gp130 via a Putative Urokinase-Binding Consensus Sequence
- Modifications of Glyceraldehyde-3-Phosphate Dehydrogenase Induced by Increasing Concentrations of Peroxynitrite: Early Recognition by 20S Proteasome
- Different Isoforms of the Non-Integrin Laminin Receptor Are Present in Mouse Brain and Bind PrP
- Cell-Type Specific Targeting and Gene Expression Using a Variant of Polyoma VP1 Virus-Like Particles
- Quantitation of Membrane Type Serine Protease 1 (MT-SP1) in Transformed and Normal Cells
- Interaction of Heat Shock Protein 70 Peptide with NK Cells Involves the NK Receptor CD94
- Cystatins C, E/M and F in Human Pleural Fluids of Patients with Neoplastic and Inflammatory Lung Disorders
- A Homodimeric Sporamin-Type Trypsin Inhibitor with Antiproliferative, HIV Reverse Transcriptase-Inhibitory and Antifungal Activities from Wampee (Clausena lansium) Seeds
- Primary Structure and Reactive Site of a Novel Wheat Proteinase Inhibitor of Subtilisin and Chymotrypsin
- Diverse Enzymatic Specificities of Digestive Proteases, 'Intestains', Enable Colorado Potato Beetle Larvae to Counteract the Potato Defence Mechanism
- Protease Inhibitors Prevent Plasminogen-Mediated, But Not Pemphigus Vulgaris-Induced, Acantholysis in Human Epidermis
- Purification and Primary Structure Determination of Human Lysosomal Dipeptidase
- A Bioinformatic Approach to the Identification of Candidate Genes for the Development of New Cancer Diagnostics
