Protease Platform
Protease Platform

Jennifer L. Harris, Ph.D.
Director of Protease Biochemistry

The regulation of protein synthesis is a complex process crucial to the survival and function of any organism. At the same time, the complementary process of protein degradation is equally critical. The more than 500 specialized “protease” enzymes that degrade proteins through the hydrolysis of peptide bonds make up one of the largest classes of enzymes encoded by the human genome. 

Historically, proteases were regarded as non-selective enzymes responsible for indiscriminately degrading dietary proteins. However, the irreversibility inherent in protease-catalyzed peptide bond hydrolysis coupled with the exquisite substrate discrimination shown by many proteases has led to a revised view, and it is now known that proteases play crucial roles in the initiation and regulation of many biological pathways. Indeed, proteases have been implicated in almost all aspects of life and death, including fertilization, development, differentiation, immunity, cell migration, cell activation, wound healing, and cell death. From a therapeutic standpoint, the modulation of proteolytic activity offers considerable promise for the treatment of a number of human diseases ranging from cardiovascular, metabolic, lung, and infectious disease to osteoporosis, cancer, stroke, neurodegeneration, and inflammation.

The complete sequencing of multiple genomes has identified the full repertoire of proteases; however, large gaps still remain in our understanding of the biological role of most proteases. Exploiting the multiple technologies developed and used at GNF, the protease group is addressing some of the major challenges in protease biology to aid in the development of protease-targeted therapeutics. Among the capabilities of the GNF protease platform are broadly enabling technologies that aid in both optimal and native substrate identification, as well as a suite of assays that assess selectivity within the protease family.

Selected Publications

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