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Literature summary for 1.14.11.29 extracted from

  • Sun, W.; Kosyna, F.K.; Jelkmann, W.; Depping, R.
    Prolyl-4-hydroxylase 2 potentially contributes to hepatocellular carcinoma-associated erythrocytosis by maintaining hepatocyte nuclear factor-4alpha expression (2015), Cell. Physiol. Biochem., 37, 2257-2264 .
    View publication on PubMed
Search for more literature for 1.14.11.29

Application

Application Comment Organism
medicine PHD2 represents a potential contributing factor for hepatocellular carcinoma-associated erythrocytosis. Selective inhibition of PHD2 in HCC cells might be considered as a way to manage erythrocytosis in hepatocellular carcinoma (HCC) patients Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
gene EGLN1 Homo sapiens

Protein Variants

Protein Variants Comment Organism
additional information the expression of PHD2 gene is silenced via specific siRNA (siPHD2) in the erythropoietin (EPO)-producing human HCC cell line HepG2. PHD2 knockdown causes a marked reduction of erythropoietin (EPO) production. HIF seems not to be involved in this process Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2 Homo sapiens
-
 hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9GZT9
-
-

Source Tissue

Source Tissue Comment Organism Textmining
Hep-G2 cell
-
 Homo sapiens
-
hepatocellular carcinoma cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
hypoxia-inducible factor-alpha-L-proline + 2-oxoglutarate + O2
-
 Homo sapiens hypoxia-inducible factor-alpha-trans-4-hydroxy-L-proline + succinate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
EGLN1
-
 Homo sapiens
PHD2
-
 Homo sapiens
prolyl-4-hydroxylase 2
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction PHD2 knockdown causes a marked reduction of erythropoietin (EPO) production. HIF seems not to be involved in this process Homo sapiens
metabolism PDH2 regulates hypoxia-inducible factor (HIF)-independent pathways, as well as the degradation pathway of HIFalpha. HIF-2alpha does not play a major role in the regulation of erythropoietin (EPO) expression by PHD2 Homo sapiens
physiological function enzyme PHD2 is to mediate the oxygen-dependent degradation of the labile alpha-subunit of hypoxia-inducible factor (HIF). In the erythropoietin (EPO)-producing human HCC cell line HepG2, PHD2 maintains the expression of hepatocyte nuclear factor-4alpha (HNF-4alpha), an important mediator of EPO expression in hepatocytes, by inhibiting the auto-/paracrine signalling of transforming growth factor-beta1. PHD2 also regulates HIF-independent pathways by interacting with other substrates. In HepG2 cells, PHD2 suppresses the activity of TGF-beta1 pathway and consequently maintains the expression of hepatocyte nuclear factor-4alpha (HNF-4alpha), an important transcription factor promoting the erythropoietin (EPO) expression in hepatocytes. PHD2 represents a potential contributing factor for hepatocellular carcinoma-associated erythrocytosis. Erythrocytosis generally leads to elevated blood viscosity and is a significant risk factor for lung artery thromboembolism, a life-threatening condition. The ability of some HCC cells to secrete EPO, a glycoprotein hormone which promotes erythropoiesis, contributes to HCC-associated erythrocytosis Homo sapiens