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Literature summary for 3.5.3.18 extracted from

  • Cillero-Pastor, B.; Mateos, J.; Fernandez-Lopez, C.; Oreiro, N.; Ruiz-Romero, C.; Blanco, F.J.
    Dimethylarginine dimethylaminohydrolase 2, a newly identified mitochondrial protein modulating nitric oxide synthesis in normal human chondrocytes (2012), Arthritis Rheum., 64, 204-212.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
homocysteine inhibition of the expression of DDAH-2 reduces the NO production induced by IL-1beta Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion conventional immunofluorescence and confocal microscopy reveal the presence of DDAH-2 in the mitochondria of IL-1beta-stimulated chondrocytes. Blocking the translocation to mitochondria reduces the NO production induced by IL-1beta Homo sapiens 5739
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
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Source Tissue

Source Tissue Comment Organism Textmining
cartilage DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage Homo sapiens
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chondrocyte
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Homo sapiens
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knee normal human chondrocytes are isolated from knee cartilage obtained Homo sapiens
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Synonyms

Synonyms Comment Organism
DDAH-2
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Homo sapiens
dimethylarginine dimethylaminohydrolase
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Homo sapiens

Expression

Organism Comment Expression
Homo sapiens DDAH-2 protein expression is higher in osteoarthritic cartilage than in normal cartilage up
Homo sapiens in chondrocyte mitochondria extracts, DDAH-2 expression is significantly increased after exposure to IL-1beta up