| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1929580 | Biochemical and Biophysical Research Communications | 2012 | 6 Pages |
The human glycine-N-acyltransferase (hGLYAT) gene and two related-genes (GLYATL1 and GLYATL2) were isolated. Human GLYAT, GLYATL1, and GLYATL2 cDNAs were isolated and shown to encode polypeptides of 295, 302, and 294 amino acids, respectively. GLYAT catalyzes glycine-N-acyltransfer reaction with benzoyl-CoA acting as a typical aralkyl transferase, while GLYATL1 catalyzed glutamine-N-acyltransfer reaction with phenylacetyl-CoA as an arylacetyl transferase. GLYAT was shown to be expressed specifically in the liver and kidney, and the cellular localization of GLYAT protein was restricted to the mitochondria. Interestingly, labeling using highly affinity purified anti-GLYAT antibody revealed that GLYAT expression was suppressed in all hepatocellular carcinomas, but not in other liver diseases. hGLYAT repression in cancerous cells in the liver was controlled at the transcriptional level. hGLYAT is a good candidate as a novel marker of hepatocellular carcinoma and may be a key molecule in the transition between differentiation and carcinogenesis of liver cells.
► We biochemically characterized three glycine-N-acyltransferase family gene products. ► We identified GLYATL1 as human glutamine-N-acyltransferase. ► Highly purified anti-GLYAT antibody was produced and used for immunohistochemistry. ► GLYAT expression was specifically depressed in HCC and not in other liver diseases.
