 Procollagen-Proline Dioxygenase
"Procollagen-Proline Dioxygenase" 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 mixed-function oxygenase that catalyzes the hydroxylation of a prolyl-glycyl containing peptide, usually in PROTOCOLLAGEN, to a hydroxyprolylglycyl-containing-peptide. The enzyme utilizes molecular OXYGEN with a concomitant oxidative decarboxylation of 2-oxoglutarate to SUCCINATE. The enzyme occurs as a tetramer of two alpha and two beta subunits. The beta subunit of procollagen-proline dioxygenase is identical to the enzyme PROTEIN DISULFIDE-ISOMERASES.
| Descriptor ID |
D011393
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| MeSH Number(s) |
D08.811.682.690.416.617.750 D08.811.682.690.708.694.750
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| Concept/Terms |
Procollagen-Proline Dioxygenase- Procollagen-Proline Dioxygenase
- Dioxygenase, Procollagen-Proline
- Procollagen Proline Dioxygenase
- Protocollagen Prolyl Hydroxylase
- Hydroxylase, Protocollagen Prolyl
- Prolyl Hydroxylase, Protocollagen
- Procollagen Prolyl 4-Hydroxylase
- 4-Hydroxylase, Procollagen Prolyl
- Procollagen Prolyl 4 Hydroxylase
- Prolyl 4-Hydroxylase, Procollagen
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Below are MeSH descriptors whose meaning is more general than "Procollagen-Proline Dioxygenase".
Below are MeSH descriptors whose meaning is more specific than "Procollagen-Proline Dioxygenase".
This graph shows the total number of publications written about "Procollagen-Proline Dioxygenase" by people in this website by year, and whether "Procollagen-Proline Dioxygenase" was a major or minor topic of these publications.
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| Year | Major Topic | Minor Topic | Total |
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| 2000 | 1 | 0 | 1 | | 2001 | 1 | 0 | 1 | | 2005 | 0 | 1 | 1 | | 2007 | 0 | 3 | 3 | | 2008 | 1 | 1 | 2 | | 2009 | 1 | 0 | 1 | | 2010 | 0 | 1 | 1 | | 2011 | 1 | 5 | 6 | | 2018 | 0 | 1 | 1 | | 2025 | 1 | 0 | 1 | | 2026 | 1 | 0 | 1 |
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Below are the most recent publications written about "Procollagen-Proline Dioxygenase" by people in Profiles.
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Staab-Weijnitz CA, Merl-Pham J, Hennen E, Onursal C, Cabeza-Boeddinghaus N, Kandhari K, Stremlau M, Behr J, Hilgendorff A, Bächinger HP, Hauck SM, Vanacore R, Hansen KC, Basak T. Prolyl-3-hydroxylase 1 is a central regulator of collagen post-translational modifications and the collagen biosynthetic network. J Biol Chem. 2026 May; 302(5):111422.
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Wu CH, Yuen KL, Molony RD, Silvers CR, Akash MMH, Messing EM, Lee YF. Protein disulfide isomerase-enriched extracellular vesicles from bladder cancer cells support tumor survival and malignant transformation in the bladder. Oncogene. 2025 Jul; 44(26):2158-2169.
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Frump AL, Selej M, Wood JA, Albrecht M, Yakubov B, Petrache I, Lahm T. Hypoxia Upregulates Estrogen Receptor ß in Pulmonary Artery Endothelial Cells in a HIF-1a-Dependent Manner. Am J Respir Cell Mol Biol. 2018 07; 59(1):114-126.
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Manalo DJ, Baek JH, Buehler PW, Struble E, Abraham B, Alayash AI. Inactivation of prolyl hydroxylase domain (PHD) protein by epigallocatechin (EGCG) stabilizes hypoxia-inducible factor (HIF-1a) and induces hepcidin (Hamp) in rat kidney. Biochem Biophys Res Commun. 2011 Dec 16; 416(3-4):421-6.
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Colgan SP, Eltzschig HK. Adenosine and hypoxia-inducible factor signaling in intestinal injury and recovery. Annu Rev Physiol. 2012; 74:153-75.
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Koeppen M, Eckle T, Eltzschig HK. The hypoxia-inflammation link and potential drug targets. Curr Opin Anaesthesiol. 2011 Aug; 24(4):363-9.
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Glover LE, Colgan SP. Hypoxia and metabolic factors that influence inflammatory bowel disease pathogenesis. Gastroenterology. 2011 May; 140(6):1748-55.
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Baek JH, Reiter CE, Manalo DJ, Buehler PW, Hider RC, Alayash AI. Induction of hypoxia inducible factor (HIF-1a) in rat kidneys by iron chelation with the hydroxypyridinone, CP94. Biochim Biophys Acta. 2011 Apr-Jun; 1809(4-6):262-8.
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van der Wel H, Johnson JM, Xu Y, Karunaratne CV, Wilson KD, Vohra Y, Boons GJ, Taylor CM, Bendiak B, West CM. Requirements for Skp1 processing by cytosolic prolyl 4(trans)-hydroxylase and a-N-acetylglucosaminyltransferase enzymes involved in O2 signaling in dictyostelium. Biochemistry. 2011 Mar 15; 50(10):1700-13.
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Glover LE, Irizarry K, Scully M, Campbell EL, Bowers BE, Aherne CM, Kominsky DJ, MacManus CF, Colgan SP. IFN-? attenuates hypoxia-inducible factor (HIF) activity in intestinal epithelial cells through transcriptional repression of HIF-1ß. J Immunol. 2011 Feb 01; 186(3):1790-8.
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