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Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing

Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing by Vivian Yuan-Wen Ho Hook
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This text is designed to provide the reader with an understanding of current knowledge concerning proteases involved in prohormone processing, and cellular aspects that must be considered for proper processing, storage, and secretion of bioactive peptides. Cellular aspects of the targeting and activation of peptide hormones in the secretory pathway are discussed in the first two chapters. The next chapters (chapters 2-6) discuss the endoproteases that are involved in prohormone processing, including the subtilisin/kexin of prohormone convertases, a novel cysteine protease known as Ôprohormone thiol proteaseÕ (PTP), and an aspartyl protease that has been termed ÒPOMC converting enzymeÓ (PCE). Subsequent to the actions of endoproteases, carboxypeptidase and aminopeptidase enzymes (chapter 7) that remove basic amino acids from the COOH- and NH2-termini of peptide intermediates are needed. Moreover, recent molecular genetic studies illustrate the role of prohormone convertases 1 and 2, as well as the carboxypeptidase E/H, processing enzymes in obesity and conditions related to diabetes. Regulation of processing proteases by the 7B2 polypeptide as a chaperone and inhibitor is presented, as well as a potential role for a family of a1-antichymotrypsin protease inhibitors. Subsequent to secretion, extracellular proteolysis of neuropeptides and peptide activation of specific receptors is discussed.
Landes Bioscience; October 1998
233 pages; ISBN 9781587064173
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Title: Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing
Author: Vivian Yuan-Wen Ho Hook