In October 1905, Phoebus Aaron Levene published an article titled “The Cleavage Products of Proteoses” in the very first issue of the Journal of Biological Chemistry. This set the stage for more than 100 years of protease-related research in the journal.
It is perhaps fitting that proteases appeared in the JBC so early on, as proteases are themselves likely one of the earliest enzymes to appear in protein evolution, catabolizing other proteins to generate the amino acids necessary for primitive organisms.
Of course, as a century of research appearing in the JBC and other journals has shown, proteases are more than mere random protein destroyers. These ancient enzymes, which are found in all organisms, from viruses to humans, catalyze a wide range of highly specific reactions that are responsible for modulating protein-protein interactions, creating new bioactive molecules, processing cellular information and regulating molecular signals. As a result of their multiple roles, proteases are involved in almost every physiological process including DNA replication, cell proliferation, tissue morphogenesis, fertilization, wound repair and inflammation.
That’s why, in spite of their long history, proteases remain at the cutting edge of biological research today. And that’s also why the JBC decided to run a comprehensive minireview series covering these diverse, complex and, ultimately, invaluable proteins.
For more information
The JBC minireview series “Proteolytic Enzymes” can be found online, where it is also available for print purchase.
Started in the journal in May 2009, the thematic series “Proteolytic Enzymes,” coordinated by JBC Associate Editor Judith S. Bond, brings together 10 minireview articles that encompass a broad range of topics and many familiar names in the protease community.
Together, these minireviews, and an introductory article written by Bond and Carlos López-Ótin, provide insight into the world of proteases, including the details of their structure, enzymatic activity and regulation. The articles also provide a look back at the molecular evolution of proteases and a look forward at the frontiers of protease research, including studies into the proteolytic regulation of transcription factor activity and protein ectodomain shedding.
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Among the minireviews included in the series are a detailed overview of the 26S proteasome by Ami Navon and Aaron Ciechanover; a review of our current knowledge of human caspases written by Cristina Pop and Guy S. Salvesen; a look at the exosite requirements of serpin specificity by Peter G. W. Gettins and Steven T. Olson; a review of the structural and mechanistic features of intramembrane-cleaving proteases by Michael S. Wolfe and a discussion of the proteolytic regulation of epithelial sodium channels by Thomas R. Kleyman and colleagues.
The thematic minireview series provides a valuable overview of the family of protein sculptors known as proteases that decisively influence the rhythms of cell life and death in all living organisms.
Nick Zagorski (email@example.com) is a science writer at ASBMB.