Peptide Biosynthesis: Prohormone Convertases 1/3 and 2 - Couverture souple

Hoshino, Akina; Lindberg, Iris

 
9781615043644: Peptide Biosynthesis: Prohormone Convertases 1/3 and 2
Couverture souple
ISBN 10 : 1615043640 ISBN 13 : 9781615043644
Editeur : Morgan & Claypool Life Sciences, 2012

Synopsis

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

Les informations fournies dans la section « Synopsis » peuvent faire référence à une autre édition de ce titre.

Présentation de l'éditeur

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

Les informations fournies dans la section « A propos du livre » peuvent faire référence à une autre édition de ce titre.

Éditeur
Morgan & Claypool Life Sciences
Date d'édition
2012
Langue
anglais
ISBN 10 
1615043640
ISBN 13 
9781615043644
Reliure
Broché
Nombre de pages
108
Coordonnées du fabricant
non disponible
Personne responsable
gpsr@libri.de
gpsr@libri.de

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Hamburg
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