Peptide biosynthesis: prohormone convertases 1/3 and 2
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 em...
Gespeichert in:
| Hauptverfasser: | , |
|---|---|
| Format: | Buch |
| Sprache: | English |
| Veröffentlicht: |
San Rafael, Calif.
Morgan & Claypool
2012
|
| Schriftenreihe: | Colloquium series on neuropeptides
|
| Schlagworte: | |
| Zusammenfassung: | 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 |
| Beschreibung: | Includes bibliographical references (p. 59-96) |
| Beschreibung: | IX, 97 S. Ill. |
| ISBN: | 9781615043644 |
Internformat
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| 100 | 1 | |a Hoshino, Akina |e Verfasser |4 aut | |
| 245 | 1 | 0 | |a Peptide biosynthesis |b prohormone convertases 1/3 and 2 |c Akina Hoshino ; Iris Lindberg |
| 264 | 1 | |a San Rafael, Calif. |b Morgan & Claypool |c 2012 | |
| 300 | |a IX, 97 S. |b Ill. | ||
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| 490 | 0 | |a Colloquium series on neuropeptides | |
| 500 | |a Includes bibliographical references (p. 59-96) | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Neuropeptides | |
| 650 | 4 | |a Peptide hormones | |
| 700 | 1 | |a Lindberg, Iris |e Verfasser |4 aut | |
| 999 | |a oai:aleph.bib-bvb.de:BVB01-025879570 | ||
Datensatz im Suchindex
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| author | Hoshino, Akina Lindberg, Iris |
| author_facet | Hoshino, Akina Lindberg, Iris |
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| bvnumber | BV040900070 |
| ctrlnum | (OCoLC)835651726 (DE-599)BVBBV040900070 |
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| id | DE-604.BV040900070 |
| illustrated | Illustrated |
| indexdate | 2024-07-10T00:34:55Z |
| institution | BVB |
| isbn | 9781615043644 |
| language | English |
| oai_aleph_id | oai:aleph.bib-bvb.de:BVB01-025879570 |
| oclc_num | 835651726 |
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| owner_facet | DE-20 |
| physical | IX, 97 S. Ill. |
| publishDate | 2012 |
| publishDateSearch | 2012 |
| publishDateSort | 2012 |
| publisher | Morgan & Claypool |
| record_format | marc |
| series2 | Colloquium series on neuropeptides |
| spelling | Hoshino, Akina Verfasser aut Peptide biosynthesis prohormone convertases 1/3 and 2 Akina Hoshino ; Iris Lindberg San Rafael, Calif. Morgan & Claypool 2012 IX, 97 S. Ill. txt rdacontent n rdamedia nc rdacarrier Colloquium series on neuropeptides Includes bibliographical references (p. 59-96) 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 Neuropeptides Peptide hormones Lindberg, Iris Verfasser aut |
| spellingShingle | Hoshino, Akina Lindberg, Iris Peptide biosynthesis prohormone convertases 1/3 and 2 Neuropeptides Peptide hormones |
| title | Peptide biosynthesis prohormone convertases 1/3 and 2 |
| title_auth | Peptide biosynthesis prohormone convertases 1/3 and 2 |
| title_exact_search | Peptide biosynthesis prohormone convertases 1/3 and 2 |
| title_full | Peptide biosynthesis prohormone convertases 1/3 and 2 Akina Hoshino ; Iris Lindberg |
| title_fullStr | Peptide biosynthesis prohormone convertases 1/3 and 2 Akina Hoshino ; Iris Lindberg |
| title_full_unstemmed | Peptide biosynthesis prohormone convertases 1/3 and 2 Akina Hoshino ; Iris Lindberg |
| title_short | Peptide biosynthesis |
| title_sort | peptide biosynthesis prohormone convertases 1 3 and 2 |
| title_sub | prohormone convertases 1/3 and 2 |
| topic | Neuropeptides Peptide hormones |
| topic_facet | Neuropeptides Peptide hormones |
| work_keys_str_mv | AT hoshinoakina peptidebiosynthesisprohormoneconvertases13and2 AT lindbergiris peptidebiosynthesisprohormoneconvertases13and2 |