 Carboxypeptidase H
"Carboxypeptidase H" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A ZINC-containing exopeptidase primarily found in SECRETORY VESICLES of endocrine and neuroendocrine cells. It catalyzes the cleavage of C-terminal ARGININE or LYSINE residues from polypeptides and is active in processing precursors of PEPTIDE HORMONES and other bioactive peptides.
| Descriptor ID |
D043423
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| MeSH Number(s) |
D08.811.277.656.350.245.167 D08.811.277.656.350.555.250 D08.811.277.656.675.555.250 D08.811.277.656.837.124
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| Concept/Terms |
Carboxypeptidase H- Carboxypeptidase H
- Enkephalin Convertase
- Convertase, Enkephalin
- Enkephalin-Synthesizing Carboxypeptidase
- Carboxypeptidase, Enkephalin-Synthesizing
- Enkephalin Synthesizing Carboxypeptidase
- Carboxypeptidase E
- Enkephalin-Forming Carboxypeptidase
- Carboxypeptidase, Enkephalin-Forming
- Enkephalin Forming Carboxypeptidase
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Below are MeSH descriptors whose meaning is more general than "Carboxypeptidase H".
Below are MeSH descriptors whose meaning is more specific than "Carboxypeptidase H".
This graph shows the total number of publications written about "Carboxypeptidase H" by people in this website by year, and whether "Carboxypeptidase H" was a major or minor topic of these publications.
To see the data from this visualization as text, click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1989 | 0 | 3 | 3 | | 1995 | 0 | 1 | 1 | | 1996 | 0 | 1 | 1 | | 2008 | 1 | 0 | 1 | | 2011 | 0 | 1 | 1 | | 2014 | 1 | 0 | 1 | | 2017 | 0 | 1 | 1 |
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Below are the most recent publications written about "Carboxypeptidase H" by people in Profiles.
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Blandino-Rosano M, Barbaresso R, Jimenez-Palomares M, Bozadjieva N, Werneck-de-Castro JP, Hatanaka M, Mirmira RG, Sonenberg N, Liu M, Rüegg MA, Hall MN, Bernal-Mizrachi E. Loss of mTORC1 signalling impairs ß-cell homeostasis and insulin processing. Nat Commun. 2017 07 12; 8:16014.
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Liew CW, Assmann A, Templin AT, Raum JC, Lipson KL, Rajan S, Qiang G, Hu J, Kawamori D, Lindberg I, Philipson LH, Sonenberg N, Goldfine AB, Stoffers DA, Mirmira RG, Urano F, Kulkarni RN. Insulin regulates carboxypeptidase E by modulating translation initiation scaffolding protein eIF4G1 in pancreatic ß cells. Proc Natl Acad Sci U S A. 2014 Jun 03; 111(22):E2319-28.
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Raghuraman G, Kalari A, Dhingra R, Prabhakar NR, Kumar GK. Enhanced neuropeptide Y synthesis during intermittent hypoxia in the rat adrenal medulla: role of reactive oxygen species-dependent alterations in precursor peptide processing. Antioxid Redox Signal. 2011 Apr 01; 14(7):1179-90.
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Jeffrey KD, Alejandro EU, Luciani DS, Kalynyak TB, Hu X, Li H, Lin Y, Townsend RR, Polonsky KS, Johnson JD. Carboxypeptidase E mediates palmitate-induced beta-cell ER stress and apoptosis. Proc Natl Acad Sci U S A. 2008 Jun 17; 105(24):8452-7.
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Skelly RH, Schuppin GT, Ishihara H, Oka Y, Rhodes CJ. Glucose-regulated translational control of proinsulin biosynthesis with that of the proinsulin endopeptidases PC2 and PC3 in the insulin-producing MIN6 cell line. Diabetes. 1996 Jan; 45(1):37-43.
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Alarcón C, Leahy JL, Schuppin GT, Rhodes CJ. Increased secretory demand rather than a defect in the proinsulin conversion mechanism causes hyperproinsulinemia in a glucose-infusion rat model of non-insulin-dependent diabetes mellitus. J Clin Invest. 1995 Mar; 95(3):1032-9.
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Guest PC, Pipeleers D, Rossier J, Rhodes CJ, Hutton JC. Co-secretion of carboxypeptidase H and insulin from isolated rat islets of Langerhans. Biochem J. 1989 Dec 01; 264(2):503-8.
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Guest PC, Rhodes CJ, Hutton JC. Regulation of the biosynthesis of insulin-secretory-granule proteins. Co-ordinate translational control is exerted on some, but not all, granule matrix constituents. Biochem J. 1989 Jan 15; 257(2):431-7.
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Hutton JC, Guest PC, Rhodes CJ, Fricker LD, Grimaldi KA, Siddle K, Davidson W, Bailyes EM. [Biogenesis of the insulin secretion granule]. Journ Annu Diabetol Hotel Dieu. 1989; 13-28.
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