Proteolytic and Cellular Mechanisms in Prohormone and by Vivian Yuan-Hen Ho Hook

By Vivian Yuan-Hen Ho Hook

215 pages, 34 figures, 20 tables, hardcover this article is designed to supply the reader with an figuring out of present wisdom bearing on proteases all for prohormone processing, and mobile facets that needs to be thought of for correct processing, garage, and secretion of bioactive peptides. mobile facets of the concentrating on and activation of peptide hormones within the secretory pathway are mentioned within the first chapters. the following chapters (chapters 2-6) talk about the endoproteases which are taken with prohormone processing, together with the subtilisin/kexin of prohormone convertases, a singular cysteine protease referred to as prohormone thiol protease (PTP), and an aspartyl protease that has been termed POMC changing enzyme (PCE). next to the activities of endoproteases, carboxypeptidase and aminopeptidase enzymes (chapter 7) that get rid of uncomplicated amino acids from the COOH- and NH2-termini of peptide intermediates are wanted. furthermore, fresh molecular genetic reports illustrate the position of prohormone conv! ertases 1 and a pair of, in addition to the carboxypeptidase E/H, processing enzymes in weight problems and prerequisites with regards to diabetes. rules of processing proteases through the 7B2 polypeptide as a chaperone and inhibitor is gifted, in addition to a possible position for a relations of a1-antichymotrypsin protease inhibitors. next to secretion, extracellular proteolysis of neuropeptides and peptide activation of particular receptors is mentioned.

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Extra resources for Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing (Molecular Biology Intelligence Unit)

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Protein sorting among two distinct export pathways occurs from the content of maturing exocrine storage granules. J Cell Biol 1987; 105(6):2675-2684. 25. Tooze SA. Biogenesis of secretory granules. Implications arising from the immature secretory granule in the regulated pathway of secretion. FEBS Lett 1991; 285(2):220-4. 26. Arvan P, Castle D. Protein sorting and secretion granule formation in regulated secretory cells. Trends Cell Biol 1992; 2:327-331. 27. Walter P, Johnson AE. Signal sequence recognition and protein targeting to the endoplasmic reticulum membrane.

Landes Company. Fig. 1. Schematic diagram of bovine pro-opiomelanocortin (POMC). This figure illustrates the POMC domains that are delineated by dibasic cleavage sites. These sites are cleaved in a tissue specific manner to produce a variety of peptide hormones depending on the complement of processing enzymes present. ACTH and β-LPH are primarily found in the anterior pituitary while the smaller POMC derived peptides, N-POMC1-48, γ3-MSH, α-MSH and β-END, are primarily found in the intermediate lobe of the pituitary and brain.

215. Pezzati R, Bossi M, Podini P et al. High-resolution calcium mapping of the endoplasmic reticulum-Golgi-exocytic membrane system. Mol Biol Cell 1997; 8(8):1501-1512. 216. Bulenda D, Gratzl M. Matrix free Ca2+ in isolated chromaffin vesicles. Biochemistry 1985; 24:7760-7765. 217. Verkman AS, van Hoek AN, Ma T et al. Water transport across mammalian cell membranes. Am J Physiol 1996; 270(1 Pt. 1):C12-30. 26 Proteolytic and Cellular Mechanisms in Prohormone and Proprotein Processing 218. Slot JW, Geuze HJ, Gigengack S et al.

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Proteolytic and Cellular Mechanisms in Prohormone and by Vivian Yuan-Hen Ho Hook
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