HSD17B10

From Wikipedia, the free encyclopedia

Hydroxysteroid (17-beta) dehydrogenase 10

PDB rendering based on 1so8.

Available structures: 1so8, 1u7t, 2o23

Identifiers

Symbol(s)

HSD17B10; 17b-HSD10; ABAD; ERAB; HADH2; HCD2; MHBD; SCHAD

External IDs

OMIM: 300256 MGI: 1333871 HomoloGene: 68403

Gene ontology
Molecular Function:	• 3-hydroxyacyl-CoA dehydrogenase activity • protein binding • 7-alpha-hydroxysteroid dehydrogenase activity • oxidoreductase activity • 3-hydroxy-2-methylbutyryl-CoA dehydrogenase activity
Cellular Component:	• cytoplasm • mitochondrion • mitochondrial inner membrane • endoplasmic reticulum • plasma membrane
Biological Process:	• lipid metabolic process • metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_001037811 (mRNA)
NP_001032900 (protein)

NM_016763 (mRNA)
NP_058043 (protein)

Location

Chr X: 53.47 - 53.48 Mb

Chr X: 147.34 - 147.35 Mb

Pubmed search

[1]

[2]

Hydroxysteroid (17-beta) dehydrogenase 10, also known as HSD17B10, is a human gene.^[1]

This gene encodes 3-hydroxyacyl-CoA dehydrogenase type II, a member of the short-chain dehydrogenase/reductase superfamily. The gene product is a mitochondrial protein that catalyzes the oxidation of a wide variety of fatty acids, alcohols, and steroids. The protein has been implicated in the development of Alzheimer's disease, and mutations in the gene are the cause of 2-methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency (MHBD). Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined.^[1]

[edit] References

^ ^a ^b Entrez Gene: HSD17B10 hydroxysteroid (17-beta) dehydrogenase 10.

[edit] Further reading

Yang SY, He XY, Schulz H (2005). "3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease.". FEBS J. 272 (19): 4874–83. doi:10.1111/j.1742-4658.2005.04911.x. PMID 16176262.
Yang SY, He XY, Miller D (2007). "HSD17B10: a gene involved in cognitive function through metabolism of isoleucine and neuroactive steroids.". Mol. Genet. Metab. 92 (1-2): 36–42. doi:10.1016/j.ymgme.2007.06.001. PMID 17618155.
Vredendaal PJ, van den Berg IE, Malingré HE, et al. (1996). "Human short-chain L-3-hydroxyacyl-CoA dehydrogenase: cloning and characterization of the coding sequence.". Biochem. Biophys. Res. Commun. 223 (3): 718–23. PMID 8687463.
Furuta S, Kobayashi A, Miyazawa S, Hashimoto T (1997). "Cloning and expression of cDNA for a newly identified isozyme of bovine liver 3-hydroxyacyl-CoA dehydrogenase and its import into mitochondria.". Biochim. Biophys. Acta 1350 (3): 317–24. PMID 9061028.
Yan SD, Fu J, Soto C, et al. (1997). "An intracellular protein that binds amyloid-beta peptide and mediates neurotoxicity in Alzheimer's disease.". Nature 389 (6652): 689–95. doi:10.1038/39522. PMID 9338779.
He XY, Schulz H, Yang SY (1998). "A human brain L-3-hydroxyacyl-coenzyme A dehydrogenase is identical to an amyloid beta-peptide-binding protein involved in Alzheimer's disease.". J. Biol. Chem. 273 (17): 10741–6. PMID 9553139.
Miller AP, Willard HF (1998). "Chromosomal basis of X chromosome inactivation: identification of a multigene domain in Xp11.21-p11.22 that escapes X inactivation.". Proc. Natl. Acad. Sci. U.S.A. 95 (15): 8709–14. PMID 9671743.
Sambamurti K, Lahiri DK (1998). "ERAB contains a putative noncleavable signal peptide.". Biochem. Biophys. Res. Commun. 249 (2): 546–9. doi:10.1006/bbrc.1998.9178. PMID 9712734.
Hansis C, Jähner D, Spiess AN, et al. (1998). "The gene for the Alzheimer-associated beta-amyloid-binding protein (ERAB) is differentially expressed in the testicular Leydig cells of the azoospermic by w/w(v) mouse.". Eur. J. Biochem. 258 (1): 53–60. PMID 9851691.
Yan SD, Shi Y, Zhu A, et al. (1999). "Role of ERAB/L-3-hydroxyacyl-coenzyme A dehydrogenase type II activity in Abeta-induced cytotoxicity.". J. Biol. Chem. 274 (4): 2145–56. PMID 9890977.
He XY, Merz G, Mehta P, et al. (1999). "Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase.". J. Biol. Chem. 274 (21): 15014–9. PMID 10329704.
Oppermann UC, Salim S, Tjernberg LO, et al. (1999). "Binding of amyloid beta-peptide to mitochondrial hydroxyacyl-CoA dehydrogenase (ERAB): regulation of an SDR enzyme activity with implications for apoptosis in Alzheimer's disease.". FEBS Lett. 451 (3): 238–42. PMID 10371197.
He XY, Yang YZ, Schulz H, Yang SY (2000). "Intrinsic alcohol dehydrogenase and hydroxysteroid dehydrogenase activities of human mitochondrial short-chain L-3-hydroxyacyl-CoA dehydrogenase.". Biochem. J. 345 Pt 1: 139–43. PMID 10600649.
Yang SY, He XY (2001). "Role of type 10 17beta-hydroxysteroid dehydrogenase in the pathogenesis of Alzheimer's disease.". Adv. Exp. Med. Biol. 487: 101–10. PMID 11403151.
Frackowiak J, Mazur-Kolecka B, Kaczmarski W, Dickson D (2001). "Deposition of Alzheimer's vascular amyloid-beta is associated with decreased expression of brain L-3-hydroxyacyl-coenzyme A dehydrogenase (ERAB).". Brain Res. 907 (1-2): 44–53. PMID 11430884.
He XY, Merz G, Yang YZ, et al. (2001). "Characterization and localization of human type10 17beta-hydroxysteroid dehydrogenase.". Eur. J. Biochem. 268 (18): 4899–907. PMID 11559359.
He XY, Wen GY, Merz G, et al. (2002). "Abundant type 10 17 beta-hydroxysteroid dehydrogenase in the hippocampus of mouse Alzheimer's disease model.". Brain Res. Mol. Brain Res. 99 (1): 46–53. PMID 11869808.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.
Ofman R, Ruiter JP, Feenstra M, et al. (2003). "2-Methyl-3-hydroxybutyryl-CoA dehydrogenase deficiency is caused by mutations in the HADH2 gene.". Am. J. Hum. Genet. 72 (5): 1300–7. PMID 12696021.
Shafqat N, Marschall HU, Filling C, et al. (2003). "Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta/21-HSD.". Biochem. J. 376 (Pt 1): 49–60. doi:10.1042/BJ20030877. PMID 12917011.