Peptide biosynthesis : prohormone convertases 1/3 and 2 /

Bibliographic Details
Main Author: Hoshino, Akina
Other Authors: Lindberg, Iris
Format: eBook
Language:English
Published: San Rafael, Calif. (1537 Fourth Street, San Rafael, CA 94901 USA) : Morgan and Claypool, [2012]
Series:Colloquium digital library of life sciences.
Colloquium series on neuropeptides ; # 1.
Subjects:
Online Access:Connect to the full text of this electronic book
Description
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.
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.