High expression of the evolutionarily conserved alpha/beta hydrolase domain containing 6 (ABHD6) in Ewing tumors
Autor: | Martin S. Staege, Manuela Hesse, Ines Volkmer, Daniela Max |
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Rok vydání: | 2009 |
Předmět: |
Cancer Research
Homoserine Bone Neoplasms Sarcoma Ewing Biology Bioinformatics Serine Evolution Molecular chemistry.chemical_compound Cell Line Tumor Hydrolase medicine Humans Homology modeling Gene chemistry.chemical_classification Cancer General Medicine Lipase ABHD6 medicine.disease Prognosis Molecular biology Monoacylglycerol Lipases Enzyme Oncology chemistry Carboxylic Ester Hydrolases |
Zdroj: | Cancer science. 100(12) |
ISSN: | 1349-7006 |
Popis: | Despite improvements in the treatment of patients with Ewing family tumors (EFT), the prognosis for patients with advanced disease is still unsatisfactory. Recently, we identified lipase I as an EFT-associated gene that might be interesting for the development of new immunological or pharmacological treatment strategies. Lipase I is a member of the large protein superfamilies of α/β hydrolases and serine hydrolases. In the present paper we describe high expression of another member of these superfamilies in EFT. By DNA microarray data base mining we found exceptional high expression of α/β hydrolase domain containing 6 (ABHD6) in EFT but not in other sarcomas. Expression of ABHD6 in EFT correlated with expression of another EFT-associated gene, aristaless. Analysis of ABHD6-associated GGAA microsatellites revealed shorter microsatellites in EFT with lack of ABHD6 expression. ABHD6 homologues were found in varying chordata but not in other animal species. Based on homology modeling we predicted the 3D-structure of ABHD6, which shows high similarity with bacterial homoserine transacetylases. High expression of ABHD6 in EFT in comparison to normal tissues and other tumors suggests that ABHD6 might be an interesting new diagnostic or therapeutic target for EFT. However, knock down of ABHD6 in EFT cells did not inhibit tumor cell growth. (Cancer Sci 2009; 100: 2383–2389) |
Databáze: | OpenAIRE |
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