Peptide Biosynthesis

Peptide Biosynthesis
Prohormone Convertases 1/3 and 2

Akina Hoshino, Iris Lindberg
ISBN: 9781615043644 | PDF ISBN: 9781615043651
Copyright © 2012 | 112 Pages | Publication Date: 01/01/2012

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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. In this lecture, 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. Finally, new studies have revealed an increasingly important role for PC1/3 polymorphisms and mutations in glucose homeostasis and obesity.

Table of Contents

General Introduction to the Prohormone Convertases
Prohormone Convertase 1/3
Prohormone Convertase 2
Summary and Future Directions
References
Author Biography

About the Author(s)

Akina Hoshino, University of Maryland-Baltimore
Akina Hoshino was born in Yokohama, Japan and moved to the United States to attend Vassar College where she earned her B.A. degree in Biology and Chinese. She is currently a graduate student in the Program in Neuroscience at the University of Maryland-Baltimore, working toward her Ph.D. under Dr. Iris Lindberg. Her main interests in the Lindberg lab are regulation of PC1/3 and the role of proSAAS in protein aggregation-mediated neurodegenerative diseases. She has shown that PC1/3 activity is regulated via self-association and that proSAAS can function as an anti-aggregant. In 2012, she will be heading to Seattle, Washington to research stem cell replacement therapies to treat retinal degeneration. In her spare time, she enjoys baking and doing Pilates.

Iris Lindberg, University of Maryland-Baltimore
Iris Lindberg (Ph.D. 1980 University of Wisconsin, Madison) has been working on prohormone convertases since 1991; her group, now at the University of Maryland-Baltimore, focuses on the enzymology and cell biology (and occasionally evolution) of these unusual serine proteinases and their binding proteins. Her group was the first to purify recombinant PC1/3 and PC2, and they are now working to crystallize these important enzymes. Her team also showed that 7B2 is required for proPC2 to mature to an active enzyme; 7B2 does so by blocking the spontaneous aggregation of proPC2. Recent work in the lab is centered on deriving new convertase inhibitors as well as exploring the idea that 7B2 and proSAAS represent general secretory chaperones active in neurodegenerative disease.

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