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Am J Physiol Endocrinol Metab 295: E987, 2008; doi:10.1152/ajpendo.90521.2008
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LETTERS TO THE EDITOR

Re: Hadh2 and 3-hydroxyacyl-CoA dehydrogenase

Song-Yu Yang and Xue-Ying He

Department of Neurochemistry, New York State Institute for Basic Research in Developmental Disabilities, Staten Island, New York

TO THE EDITOR: To investigate the impact of maternal diabetes on oocyte metabolism and meiotic maturation, Ratchford et al. (10) reported changes in 3-hydroxyacyl-CoA dehydrogenase II (Hadh2) activity in oocytes after treatment with 5-aminoimidazole-4-carboxamide-1-β-D-ribofuranoside or after administration of human chorionic gonadotropin, respectively (as shown in Figs. 3A and 4A of Ref. 10). These data were obtained by performing β-hydroxyacyl-CoA dehydrogenase (BOAC) assays (6), in which acetoacetyl-CoA served as the substrate. Using this substrate, these authors actually measured the combined activities of Hadh2 and 3-hydroxyacyl-CoA dehydrogenase in the oocytes, since the reduction of acetoacetyl-CoA by NADH could be effectively catalyzed by both of these distinct dehydrogenases (3, 4, 12).

The term BOAC, an abbreviation favored by some groups in the past (6, 8), has been updated to 3-hydroxyacyl-CoA dehydrogenase (HADH) (OMIM1 601609 [OMIM] ). According to the conventional usage, Hadh2 is an abbreviation for 3-hydroxyacyl-CoA dehydrogenase II (4, 14, 15). Moreover, the terms HADH2 and 3-hydroxyacyl-CoA dehydrogenase II have recently been replaced by HSD17B10 and hydroxysteroid (17β) dehydrogenase 10 (HSD10), respectively, as approved designations for the gene and gene product (OMIM 300256 [OMIM] ) (5).

HSD10, a multifunctional enzyme (1, 13, 14), is a member of the short-chain dehydrogenase/reductase family (1, 3) but not the 3-hydroxyacyl-CoA dehydrogenase family, which consists of 3-hydroxyacyl-CoA dehydrogenases and long-chain 3-hydroxyacyl-CoA dehydrogenase (OMIM609016) (11, 14).

The report (10) stated that "a lack of Hadh2 activity may impart early developmental problems, leading to embryo lethality," and further concluded that, in oocytes from diabetic mice, "activities of Hadh2 and Gpt2, two enzymes activated by AMPK, were significantly less in these oocytes." The identity of this Hadh2 activity is ambiguous. For scientific accuracy, the distinction between Hadh2 and 3-hydroxyacyl-CoA dehydrogenase is essential.

For the purpose of specifically measuring intracellular Hadh2 activities, branched-chain acyl-CoA thioesters, instead of acetoacetyl-CoA, should be used as the substrate in either the forward (7) or reverse reaction (9). In contrast to 3-hydroxyacyl-CoA dehydrogenase catalyzing the third reaction of straight-chain fatty acid oxidation spiral (2, 12), HSD10 (formerly Hadh2) functions in isoleucine and steroid metabolism (1, 13, 15). In our opinion, it is most likely that, in addition to the 3-hydroxyacyl-CoA dehydrogenase activity, the HSD10 (formerly Hadh2) activity is also relevant to the metabolism and meiotic maturation of oocytes.

GRANTS

Our work is supported in part by the New York State Office of Mental Retardation and Developmental Disabilities.

FOOTNOTES


Address for reprint requests and other correspondence: S.-Y. Yang, NYS Institute for Basic Research in Developmental Disabilities, 1050 Forest Hill Road, Staten Island, NY 10314 (e-mail: syang{at}mail.csi.cuny.edu)

1 OMIM, Online Mandelian Inheritance in Man, a database of the National Center for Biotechnology Information, US National Library of Medicine. Back

REFERENCES

  1. He XY, Yang SY. Roles of type 10 17beta-hydroxysteroid dehydrogenase in intracrinology and metabolism of isoleucine and fatty acids. Endoc Metab Immune Disord Drug Targets 6: 95–102, 2006.
  2. He XY, Yang SY. 3-Hydroxyacyl-CoA dehydrogenase (HAD) deficiency replaces short-chain hydroxyacyl-CoA dehydrogenase (SCHAD) deficiency as well as medium- and short-chain hydroxyacyl-CoA dehydrogenase (M/SCHAD) deficiency as the consensus name of this fatty acid oxidation disorder. Mol Genet Metab 91: 205–206, 2007.[CrossRef][Web of Science][Medline]
  3. He XY, Schulz H, Yang SY. A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical with an amyloid β-peptide binding protein involved in Alzheimer's disease. J Biol Chem 273: 10741–10746, 1998.[Abstract/Free Full Text]
  4. Kobayashi A, Jiang LL, Hashimoto T. Two mitochondrial 3-hydroxyacyl-CoA dehydrogenase 5 in bovine liver. J Biochem (Tokyo) 119: 775–782, 1996.[Abstract/Free Full Text]
  5. Korman SH, Yang SY. HSD17B10 replaces HADH2 as the approved designation for the gene mutated in 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency. Mol Genet Metab 91: 115, 2007.[CrossRef][Web of Science][Medline]
  6. Lowry OH, Berger SJ, Carter JG, Chi MM, Manchester JK, Knor J, Pusateri ME. Diversity of metabolic patterns in human tumors: enzymes of energy metabolism and related metabolites and cofactors. J Neurochem 41: 994–1010, 1983.[CrossRef][Web of Science][Medline]
  7. Luo MJ, Mao LF, Schulz H. Short-chain 3-hydroxy-2-methylacyl-CoA dehydrogenase from rat liver: purification and characterization of a novel enzyme of isoleucine metabolism. Arch Biochem Biophys 321: 214–220, 1995.[CrossRef][Web of Science][Medline]
  8. Michel RN, Cowper G, Chi MM, Manchester JK, Falter H, Lowry OH. Effects of tetrodotoxin-induced neural inactivation on single muscle fiber metabolic enzymes. Am J Physiol Cell Physiol 267: C55–C66, 1994.[Abstract/Free Full Text]
  9. Ofman R, Ruiter JP, Feenstra M, Duran M, Poll-The BT, Zschocke J, Ensenauer R, Lehnert W, Sass JO, Sperl W, Wanders RJ. 2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene. Am J Hum Genet 72: 1300–1307, 2003.[CrossRef][Web of Science][Medline]
  10. Ratchford AM, Chang AS, Chi MM, Sheridan R, Moley KH. Maternal diabetes adversely affects AMP-activated protein kinase activity and cellular metabolism in murine oocytes. Am J Physiol Endocrinol Metab 293: E1198–E1206, 2007.[Abstract/Free Full Text]
  11. Yang SY. The large subunit of the pig heart mitochondrial membrane-bound β-oxidation complex is a long-chain enoyl-CoA hydratase:3-hydroxyacyl-CoA dehydrogenase bifunctional enzyme. Comp Biochem Physiol B Biochem Mol Biol 109: 557–566, 1994.[CrossRef][Medline]
  12. Yang SY, He XY. Molecular mechanism of fatty acid β-oxidation enzyme catalysis. In: Current Views of Fatty Acid Oxidation and Ketogenesis: From Organelles to Point Mutations, edited by Quant P and Eaton S. New York: Kluwer Academic/Plenum, 1999, p. 133–143.
  13. Yang SY, He XY, Miller D. HSD17B10: a gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids. Mol Genet Metab 92: 36–42, 2007.[CrossRef][Web of Science][Medline]
  14. Yang SY, He XY, Schulz H. 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease. FEBS J 272: 4874–4883, 2005.[CrossRef][Medline]
  15. Yang SY, He XY, Schulz H. Multiple functions of type 10 17beta-hydroxysteroid dehydrogenase. Trends Endocrinol Metab 16: 167–175, 2005.[CrossRef][Web of Science][Medline]



This article has been cited by other articles:


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 Proc. Natl. Acad. Sci. USAHome page
S.-Y. Yang, X.-Y. He, S. E. Olpin, V. R. Sutton, J. McMenamin, M. Philipp, R. B. Denman, and M. Malik
Mental retardation linked to mutations in the HSD17B10 gene interfering with neurosteroid and isoleucine metabolism
PNAS, September 1, 2009; 106(35): 14820 - 14824.
[Abstract] [Full Text] [PDF]

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