Peptide biosynthesis : prohormone convertases 1/3 and 2 /
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| Other Authors: | |
| Format: | eBook |
| Language: | English |
| Published: |
San Rafael, Calif. (1537 Fourth Street, San Rafael, CA 94901 USA) :
Morgan and Claypool,
[2012]
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| Series: | Colloquium digital library of life sciences.
Colloquium series on neuropeptides ; # 1. |
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| Online Access: | Connect to the full text of this electronic book |
| Abstract: | The prohormone convertases (PC) 1/3 and 2 are calcium-activated eukaryotic subtilisins with low pH optima which accomplish the limited proteolysis of peptide hormone precursors within neurons and endocrine cells. We review the biochemistry, regulation, and roles of PC1/3 and 2 in disease, with an emphasis on the work published in the last 10 years. In the 20 years since their discovery, a great deal has been learned about their localization and cellular functions. Both PCs share the same four domains: the propeptides perform important roles in controlling activation and targeting; the catalytic domains confer specificity, with PC1/3 possessing a more restricted binding pocket than that of PC2; the P domain is required for expression and contributes to enzymatic properties; and the C-terminal tail assists in proper routing to granules. PC1/3, but not PC2, exists in full-length and C-terminally truncated forms that exhibit different biochemical properties. Both enzymes associate with binding proteins; proSAAS is thought to modulate precursor cleavage by PC1/3, while co-expression of 7B2 is obligatory for the formation of active PC2. New studies have revealed an increasingly important role for PC1/3 polymorphisms and mutations in glucose homeostasis and obesity. |
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| Item Description: | Part of: Colloquium digital library of life sciences. Series from website. Electronic resource. |
| Physical Description: | 1 online resource (ix, 101 pages) : illustrations Also available in printing. |
| Format: | Mode of access: World Wide Web. System requirements: Adobe Acrobat reader. |
| Bibliography: | Includes bibliographical references (pages 59-100). |
| ISBN: | 9781615043651 (electronic bk.) |
| Access: | Abstract freely available; full-text restricted to subscribers or individual document purchasers. |