DNA encoding the human serine protease C-E

Abstract

Here we describe the molecular identification of a cDNA encoding a novel serine protease we have termed protease C-E. The deduced amino acid sequence, and it alignment with other well-characterized serine proteases indicates that it is a member of the S1 serine protease family. We have found that the protease C-E mRNA is expressed in pancreas, placenta, prostate, small intestine, stomach, spleen, fibroblasts and epidermis, as well as in certain regions of the brain i.e., cerebellum, cerebral cortex, pituitary and hippocampus. Enzymatically active protease C-E, as produced using the methodologies described herein, is amenable to further biochemical analyses for the identification of physiological substrates and specific modulators.

Description

BACKGROUND OF THE INVENTION [0001] The members of the trypsin / chymotrypsin-like (S1) serine protease family are gaining recognition due to the increased awareness that these enzymes play pivotal roles in a multitude of diverse physiological processes. In addition to the classical functions the proteases trypsin and chymotrypsin perform during the digestive process, serine proteases also participate in regulating key amplification cascades through the proteolytic activation of inactive zymogen precursors. Thus, in many instances the protease substrates within these cascades are themselves the inactive form, or zymogen, of a “downstream” serine protease. Well-known examples of this serine protease-mediated regulation include blood coagulation, (Davie et al. (1991). Biochemistry 30:10363-70), kinin formation (Proud and Kaplan (1988). Annu. Rev. Immunol. 6:49-83) and the complement system (Reid and Porter (1981). Annual Review of Biochemistry 50:433-464). Although these proteolytic path...

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Benefits of technology

[0004] Enzymatically active protease C-E is amenable to further biochemical analyses for the identification of physiological substrates and specific modulators. Modulators identified in the chromogenic assay disclosed herein are potentially useful as therapeutic agents in the treatment of diseases associated with certain regions of the brain, but not limited to neurodegeneration. In addition, expression of protease C-E in fibroblasts and epidermis suggests that modulators of protease C-E function could be used to treat disorders effecting skin as well. Since th

Problems solved by technology

Unfortunately use of some proteases is limited by their potential to cause allergic reactions in sensitive individuals or by reduced efficiency when used in a non-natural environment.

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