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The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

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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

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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.