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Literature summary for 3.3.2.6 extracted from

  • Oi, N.; Yamamoto, H.; Langfald, A.; Bai, R.; Lee, M.H.; Bode, A.M.; Dong, Z.
    LTA4H regulates cell cycle and skin carcinogenesis (2017), Carcinogenesis, 38, 728-737 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Homo sapiens P09960
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Source Tissue

Source Tissue Comment Organism Textmining
A-431 cell
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Homo sapiens
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carcinoma cell the enzyme is overexpressed in several human cancers Homo sapiens
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HaCaT cell
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Homo sapiens
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keratinocyte
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Homo sapiens
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SCC-13 cell
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Homo sapiens
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skin
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Homo sapiens
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skin cancer cell LTA4H is overexpressed in human skin cancer tissues Homo sapiens
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skin squamous cell carcinoma cell facial Homo sapiens
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UM-SCC-12 cell
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Homo sapiens
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Synonyms

Synonyms Comment Organism
leukotriene A4 hydrolase
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Homo sapiens
LTA4H
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Homo sapiens

General Information

General Information Comment Organism
malfunction knocking out LTA4H significantly reduces skin cancer development in the 7,12-dimethylbenz(a)anthracene (DMBA)-initiated/12-O-tetradecanoylphorbol-13-acetate (TPA)-promoted two-stage skin cancer mouse model. LTA4H depletion dramatically decreases anchorage-dependent and -independent skin cancer cell growth by inducing cell cycle arrest at the G0/G1 phase. Depletion of LTA4H enhances p27 protein stability, which is associated with decreased phosphorylation of CDK2 at Thr160 and inhibition of the CDK2/cyclin E complex, resulting in down-regulated p27 ubiquitination. Cell phenotypes, overview Homo sapiens
physiological function leukotriene A4 hydrolase (LTA4H) is a bifunctional zinc metalloenzyme overexpressed in several human cancers. LTA4H regulates cell cycle and skin carcinogenesis. LTA4H is a key modulator of cell cycle through its negative effect on p27 expression. LTA4H mediates the G0/G1 cell cycle phase through p27 proteasome degradation and is is implicated in cell growth, cell cycle distribution. LTA4H mediates p27 stability through LTB4/BLT1 pathway. LTA4H and BLT1 influence the formation of the CDK2/cyclin E complex and the phosphorylation of CDK2 at Thr160 Homo sapiens