Picture of DNA strand

Pioneering chemical biology & medicinal chemistry through Open Access research...

Strathprints makes available scholarly Open Access content by researchers in the Department of Pure & Applied Chemistry, based within the Faculty of Science.

Research here spans a wide range of topics from analytical chemistry to materials science, and from biological chemistry to theoretical chemistry. The specific work in chemical biology and medicinal chemistry, as an example, encompasses pioneering techniques in synthesis, bioinformatics, nucleic acid chemistry, amino acid chemistry, heterocyclic chemistry, biophysical chemistry and NMR spectroscopy.

Explore the Open Access research of the Department of Pure & Applied Chemistry. Or explore all of Strathclyde's Open Access research...

Enzymes involved in the metabolism of gamma-hydroxybutyrate in SH-SY5Y cells: Identification of an iron-dependent alcohol dehydrogenase ADHFe1

Lyon, Robert C. and Johnston, Stuart M. and Panopoulos, Andraes and Alzeer, Samar and McGarvie, Gail and Ellis, Elizabeth M. (2009) Enzymes involved in the metabolism of gamma-hydroxybutyrate in SH-SY5Y cells: Identification of an iron-dependent alcohol dehydrogenase ADHFe1. Chemico-Biological Interactions, 178 (1-3). pp. 283-287. ISSN 0009-2797

Full text not available in this repository.Request a copy from the Strathclyde author

Abstract

The metabolism of the endogenous metabolite γ-hydroxybutyrate (GHB) has been studied in a human neuroblastoma cell line SH-SY5Y as a model for examining neuronal metabolism. We show that GHB can be synthesized and released from these cells, indicating that pathways for GHB synthesis and secretion are present. Activities for the major enzymes that are involved in GHB metabolism are reported, and transcripts for AKR1A1, AKR7A2, ALDH5A1 and GABA-T can be detected by RT-PCR. We also demonstrate the presence of the ADHFe1 transcript, a gene that has been reported to encode a hydroxyacid-oxoacid transhydrogenase (HOT). We show that the ADHFe1 gene is related to bacterial GHB dehydrogenases and has a conserved NAD-binding site. The potential for using the SH-SY5Y cell line for investigating GHB catabolism is discussed.