| Description |
1 online resource (ix, 101 pages) : illustrations, digital file |
| Series |
Colloquium series on neuropeptides ; # 1 |
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Colloquium digital library of life sciences
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Colloquium series on neuropeptides ; # 1.
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| Contents |
1. General introduction to the prohormone convertases |
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2. Prohormone convertase 1/3 -- 2.1 Introduction to prohormone convertase 1/3 -- 2.1.1 Unique features -- 2.1.2 Evolution -- 2.1.3 Domain structure -- 2.1.4 PC1/3 binding protein: proSAAS -- 2.1.5 Gene location -- 2.2 Distribution -- 2.2.1 Tissue distribution -- 2.2.2 Intracellular distribution -- 2.2.3 Cell lines -- 2.2.4 Development -- 2.3 Cell biology and maturation -- 2.3.1 PC1/3 maturation and posttranslational modifications -- 2.3.2 Targeting of PC1/3 -- 2.3.3 Is PC1/3 a transmembrane protein? -- 2.4 Enzymatic characterization -- 2.4.1 General enzymatic properties -- 2.4.2 Contribution of various domains to enzymatic properties -- 2.4.3 Substrate specificity -- 2.5 Regulation of expression and activity -- 2.5.1 Transcriptional and translational control -- 2.5.2 Endogenous regulators -- 2.5.3 Regulation of PC1/3 activity by its chaperone proSAAS -- 2.5.4 Synthetic inhibitors and activators -- 2.6 Model systems, knockouts and mutants -- 2.6.1 PC1/3 knockout mice -- 2.6.2 PC1/3 Asn222Asp mutant mouse -- 2.6.3 ProSAAS transgenic mice -- 2.7 PC1/3 as a therapeutic target -- 2.7.1 Human mutations -- 2.7.2 Single nucleotide polymorphisms (SNP) -- 2.7.3 PC1/3 and other diseases -- 2.7.4 ProSAAS and disease relevance |
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3. Prohormone convertase 2 -- 3.1 Introduction to prohormone convertase 2 -- 3.1.1 Unique features -- 3.1.2 Evolution -- 3.1.3 Domain structure and functions -- 3.1.4 The PC2-binding protein 7B2 -- 3.1.5 Gene location -- 3.2 Distribution -- 3.2.1 Tissue distribution -- 3.2.2 Intracellular distribution -- 3.2.3 Cell lines -- 3.2.4 Development -- 3.3 Cell biology and maturation -- 3.3.1 ProPC2 maturation -- 3.3.2 7B2 and proPC2/PC2 targeting -- 3.4 Enzymatic characterization -- 3.4.1 General enzymatic properties -- 3.4.2 Contribution of various domains to enzymatic activity -- 3.4.3 Tissue analysis of PC2 activity -- 3.4.4 Substrate specificity -- 3.5 Regulation of expression and activity -- 3.5.1 Transcriptional and translational regulation -- 3.5.2 Endogenous inhibitors -- 3.5.3 Synthetic inhibitors and activators -- 3.5.4 Regulation of PC2 activity by its chaperone 7B2 -- 3.5.5 Regulation of 7B2 expression -- 3.6 Model systems, knockouts, and mutants -- 3.6.1 The PC2 knockout mouse -- 3.6.2 The 7B2 knockout mouse -- 3.6.3 Model systems -- 3.7 PC2 as a therapeutic target: disease relevance -- 3.7.1 Polymorphisms -- 3.7.2 Cancer |
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4. Summary and future directions -- References -- Author biography |
| Summary |
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 |
| Analysis |
prohormone convertase 1 |
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prohormone convertase 1/3 |
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prohormone convertase 2 |
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proSAAS |
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7B2 |
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neuropeptides |
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obesity |
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prohormone processing |
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posttranslational processing |
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secretory pathway |
| Notes |
Part of: Colloquium digital library of life sciences |
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Title from PDF title page (viewed Feb. 17, 2012) |
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Series from website |
| Bibliography |
Includes bibliographical references (pages 59-100) |
| Subject |
Neuropeptides.
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Peptide hormones.
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Neuropeptides
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Peptide Hormones
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MEDICAL -- Neuroscience.
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PSYCHOLOGY -- Neuropsychology.
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Neuropeptides
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Peptide hormones
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| Form |
Electronic book
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| Author |
Lindberg, Iris
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| ISBN |
9781615043651 |
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1615043659 |
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