Chemistry: molecular biology and microbiology – Enzyme – proenzyme; compositions thereof; process for... – Hydrolase
Reexamination Certificate
1998-06-04
2001-04-10
Patterson, Jr., Charles L. (Department: 1652)
Chemistry: molecular biology and microbiology
Enzyme , proenzyme; compositions thereof; process for...
Hydrolase
Reexamination Certificate
active
06214600
ABSTRACT:
FIELD OF INVENTION
This invention relates to newly identified polynucleotides, polypeptides encoded by them and to the use of such polynucleotides and polypeptides, and to their production. More particularly, the polynucleotides and polypeptides of the present invention relate to Membrane-Type Matrix Metalloproteinase family, hereinafter referred to as HCE3P83. The invention also relates to inhibiting or activating the action of such polynucleotides and polypeptides.
BACKGROUND OF THE INVENTION
Membrane-Type Matrix Metalloproteinases (MT-MMPs) are a new family of transmembrane matrix metalloproteinases. At present, there are four MT-MMPs published in the literature (Sato, H. et al., Nature 370:61-65, 1994; Will, H. and Hinzmann, B. Eur. J. Biochem. 231:602-608, 1995; Takino, T. et al., J. Biol. Chem. 270:23013-23020; Puente, X. S. et al., Cancer Res. 56:944-949, 1996). MT-MMPs function as both a receptor and as an activator for certain MMPs and serve to localize extracellular matrix proteolysis at the pericellular region. MT-MMPs have been shown to play a role in metastasis and have been identified in numerous carcinomas. An MT-MMP has also been demonstrated to be involved in Alzheimer's Disease where it has been found in white matter microglia (Yamada, T. et al., Acta Neuropathol. 90: 421-424, 1995). MT-MMPs may also play a role in the infiltration of inflammatory cells. By Northern Array Grid Analysis, MT-MMP-5 expression was detected in cerebellum and kidney. A multiple tissue Northern blot was also probed for MT-MMP-5, which indicated the presence of MT-MMP-5 in brain, kidney and pancreas. This indicates that these Membrane-Type Matrix Metalloproteinases have an established, proven history as therapeutic targets. Clearly, there is a need for identification and characterization of further members of the Membrane-Type Matrix Metalloproteinase family which can play a role in preventing, ameliorating or correcting dysfunctions or diseases, including, but not limited to, Alzheimer's Disease, stroke, cancer, inflammation, arthritis, musculoskeletal disease, heart disease and kidney disease.
SUMMARY OF THE INVENTION
In one aspect, the invention relates to HCE3P83 polypeptides and recombinant materials and methods for their production. Another aspect of the invention relates to methods for using such HCE3P83 polypeptides and polynucleotides. Such uses include the treatment of Alzheimer's Disease, stroke, cancer, inflammation, arthritis, musculoskeletal disease, heart disease and kidney disease, among others. In still another aspect, the invention relates to methods to identify agonists and antagonists using the materials provided by the invention, and treating conditions associated with HCE3P83 imbalance with the identified compounds. Yet another aspect of the invention relates to diagnostic assays for detecting diseases associated with inappropriate HCE3P83 activity or levels.
REFERENCES:
EST #808618 (1997).
Puente, Xose S., et al. “Molecular Cloning of a Novel Membrane-type Matrix Metalloproteinase from a Human Breast Carcinoma”, Cancer Research 56, 944-949, Mar. 1, 1996.
Yamada, T., et al. “White matter microglia produce membrane-type matrix metalloprotease, an activator of gelatinase A, in human brain tissues”, Acta Neuropathol (1995) 90:421-424.
Okada, A., et al. “Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells cells of human colon, breast and head and neck carcinomas”, Proc. Natl. Acad Sci. USA, vol. 92. pp. 2730-3734, Mar. 1995, Medical Sciences.
Atkinson, Susan J., et al. “Intermolecular Autolytic Cleavage Can Contibute to the Activation of Progela Progelatinase A by Cell Membranes”, The Journal of Biological Chemistry, vol 270, No. 51, Issue of Dec. 22, pp. 30479-30485, 1995.
Cao, Jian, et al. “The C-terminal Region of Membrane Type Matrix Metalloproteinase Is a functional Transmembrane Domain Required for Pro-gelatinase A Activtion”, The Journal of Biological Chemistry Chemistry, vol. 270, No. 2, Issue of Jan. 13, pp. 801-805, (1995).
Gilles, Christine, et al. “High Level of MT-MMP Expression is Associated with Invasiveness of Cervical Cancer Cells”, Int. J. Cancer: 65, 209-213 (1996).
Imai, Kazushi, et al. “Membrane-Type Matrix Metalloproteinase 1 Is a Gelatinolytic Enzyme and Is Secreted in a Complex with Tissue Inhibitor of Metalloproteinase 21”, Cancer Research 56, 2707-2710, Jun. 15, 1996.
Nomura, Hidehiro, “Expression of Membrane-Type Matrix Metalloproteinase in Human Gastric Carcino Carcinomas”, Cancer Research 55, 3263-3266, Aug. 1, 1995.
Strongin, Alex Y., “Plasma Membrane-dependent Activation of the 72-kDa Type IV Collagenase Is Prevented by Complex Formation with TIMP-2”, The Journal of Biological Chemistry, vol. 268, No. 19 19, Issue of Jul. 5, pp. 14033-14039, (1993).
Tokuraku, Masato, et al., “Activation of the Precursor of Gelatinase A/72 kDa Type IV Collagenase/MMP-2 In Lung Carcinomas Correlates with the Expression of Membrane-Type Matrix Metalloproteinase (MT-MMP) and With Lymph Node Metastasis”, Int. J. Cancer (Pred. Oncol.): 64, 335-359 (1995).
Will, Horst, et al., “The Soluble Catalytic Domain of Membrance Type 1 Matrix Metalloproteinase Cleaves the Propetide of Progelatinase A and Initiates autoproteolytic Activation”, The Journal of Biological Chemistry, vol. 271, No. 29, Issue of Jul. 19, pp. 17119-17123, 1996.
Yamamoto, Masaaki, et al. “Differential Expression of Membrane-Type matrix Metalloproteinase and Its Correlation with Gelatinase A Activation in human Malignant Brain Tumors in Vivo and in Vitro”, Cancer Research 56, 384-392, Jan. 15, 1996.
Takino, Takahisa, et al., “Identification of the Second Membrane-type Matrix Metalloproteinase (MT-mmp-2) Gene from a Human Placenta cDNA Library”, The Journal of Biological Chemistry, vol. 270, No. 39, Issue of Sep. 29, pp. 23013-23020, (1995).
Will, Horst et al., “cDNA sequence and mRNA tissue distribution of a novel human matrix metalloprote metalloproteinase with a potential transmembrane segment”, Eur. J. Biochem. 231, 602-608 (1995).
Sato, Hiroshi, et al., “A matrix metalloproteinase expressed on the surface of invasive tumour cells”, Nature, vol. 370, Jul. 7, 1994, 61-64.
Arleth Anthony Joseph
Arnold Anne Romanic
Shabon Usman
Hecht Elizabeth J.
King William T.
Patterson Jr. Charles L.
Ratner & Prestia
SmithKline Beecham Corporation
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