Identification of a role for a mouse sperm surface aldo-keto reductase (AKR1B7) and its human analogue in the detoxification of the reactive aldehyde, acrolein

Andrologia

Volumn 45, Issue 5, 2013, Pages 326-331

  Jagoe, W N ^a   Howe, K ^a   O'Brien, S C ^a   Carroll, J ^a  

^a TRINITY COLLEGE DUBLIN   (Ireland)

Author keywords

Acrolein; AKR1B7; Aldo keto reductase; Detoxification; MVDP

Indexed keywords

ACROLEIN; AKR1B7 PROTEIN; OXIDOREDUCTASE; SPERMINE; UNCLASSIFIED DRUG; AKR1B7 PROTEIN, MOUSE; ALCOHOL DEHYDROGENASE; ALDEHYDE REDUCTASE; CARBONYL REDUCTASE;

ANIMAL TISSUE; ANTIBODY PRODUCTION; ARTICLE; CATABOLISM; CELL SURVIVAL; CONFOCAL MICROSCOPY; CYTOTOXICITY; DETOXIFICATION; ENZYME ACTIVITY; FEMALE; FEMALE GENITAL SYSTEM; HUMAN; HUMAN CELL; MALE; MALE GENITAL SYSTEM; MOUSE; NONHUMAN; PROTEIN FUNCTION; RAT; SEMINAL PLASMA; SPERM; VAS DEFERENS; ANIMAL; DRUG INACTIVATION; METABOLISM; TOXICITY;

ACROLEIN; ALCOHOL OXIDOREDUCTASES; ALDEHYDE REDUCTASE; ANIMALS; HUMANS; INACTIVATION, METABOLIC; MALE; MICE; SPERMINE;

EID: 84883367140     PISSN: 03034569     EISSN: 14390272     Source Type: Journal    
DOI: 10.1111/and.12018     Document Type: Article

References (24)

1. Aigueperse C, Martinez A, Lefrancois-Martinez AM, Veyssiere G, Jean CI (1999) Cyclic AMP regulates expression of the gene coding for a mouse vas deferens protein related to the aldo-keto reductase superfamily in human and murine adrenocortical cells. J Endocrinol 160:147-154.
2. Baumann C, Davies B, Peters M, Kaufmann-Reiche U, Lessl M, Theuring F (2007) AKR1B7 (mouse vas deferens protein) is dispensable for mouse development and reproductive success. Reproduction 134:97-109.
3. Berhane K, Widersten M, Engstrom A, Kozarich JW, Mannervik B (1994) Detoxication of base propenals and other alpha, beta-unsaturated aldehyde products of radical reactions and lipid peroxidation by human glutathione transferases. Proc Natl Acad Sci USA 91:1480-1484.
4. Bohren KM, Bullock B, Wermuth B, Gabbay KH (1989) The aldo-keto reductase superfamily. cDNAs and deduced amino acid sequences of human aldehyde and aldose reductases. J Biol Chem 264:9547-9951.
5. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254.
6. Cao D, Fan ST, Chung SS (1998) Identification and characterization of a novel human aldose reductase-like gene. J Biol Chem 273:11429-11435.
7. Fernandez C, Sharrard RM, Talbot M, Reed BD, Monks N (1995) Evaluation of the significance of polyamines and their oxidases in the aetiology of human cervical carcinoma. Br J Cancer 72:1194-1199.
8. Frenette G, Lessard C, Sullivan R (2004) Polyol pathway along the bovine epididymis. Mol Reprod Dev 69:448-456.
9. Frenette G, Thabet M, Sullivan R (2006) Polyol pathway in human epididymis and semen. J Androl 27:233-239.
10. Holtta E, Pulkkinen P, Elfving K, Janne J (1975) Oxidation of polymines by diamine oxidase from human seminal plasma. Biochem J 145:373-378.
11. Iuchi Y, Kaneko T, Matsuki S, Ishii T, Ikeda Y, Uchida K, Fujii J (2004) Carbonyl stress and detoxification ability in the male genital tract and testis of rats. Histochem Cell Biol 121:123-130.
12. Kolb NS, Hunsaker LA, Vander Jagt DL (1994) Aldose reductase-catalyzed reduction of acrolein: implications in cyclophosphamide toxicity. Mol Pharmacol 45:797-801.
13. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
14. Lee Y, Sayre LM (1998) Reaffirmation that metabolism of polyamines by bovine plasma amine oxidase occurs strictly at the primary amino termini. J Biol Chem, 273:19490-19494.
15. Lefrancois-Martinez AM, Tournaire C, Martinez A, Berger M, Daoudal S, Tritsch D, Veyssiere G, Jean C (1999) Product of side-chain cleavage of cholesterol, isocaproaldehyde, is an endogenous specific substrate of mouse vas deferens protein, an aldose reductase-like protein in adrenocortical cells. J Biol Chem 274:32875-32880.
16. Maayan R, Zukerman Z, Shohat B (1995) Oxidation of polyamines in human seminal plasma: a possible role in immunological infertility. Arch Androl 34:95-99.
17. Martinez A, Aigueperse C, Val P, Dussault M, Tournaire C, Berger M, Veyssiere G, Jean C, Lefrancois Martinez A (2001) Physiological functions and hormonal regulation of mouse vas deferens protein (AKR1B7) in steroidogenic tissues. Chem Biol Interact 130-132:903-917.
18. Paradowska A, Bohring C, Krause E, Krause W (2006) Identification of evolutionary conserved mouse sperm surface antigens by human antisperm antibodies (ASA) from infertile patients. Am J Reprod Immunol 55:321-330.
19. Rogers MS, Yim SF, Li KC, Wang CC, Arumanayagam M (2002) Cervical intraepithelial neoplasia is associated with increased polyamine oxidase and diamine oxidase concentrations in cervical mucus. Gynecol Oncol 84:383-387.
20. Spiteller P, Kern W, Reiner J, Spiteller G (2001) Aldehydic lipid peroxidation products derived from linoleic acid. Biochim Biophys Acta 1531:188-208.
21. Stevens JF, Maier CS (2008) Acrolein: sources, metabolism, and biomolecular interactions relevant to human health and disease. Mol Nutr Food Res 52:7-25.
22. Taragnat C, Berger M, Jean C (1988) Preliminary characterization, androgen-dependence and ontogeny of an abundant protein from mouse vas deferens. J Reprod Fertil 83:835-842.
23. Uchida K, Kanematsu M, Sakai K, Matsuda T, Hattori N, Mizuno Y, Suzuki D, Miyata T, Noguchi N, Niki E, Osawa T (1998) Protein-bound acrolein: potential markers for oxidative stress. Proc Natl Acad Sci USA 95:4882-4887.
24. Vallely PJ, Rees RC (1986) Seminal plasma suppression of human lymphocyte responses in vitro requires the presence of bovine serum factors. Clin Exp Immunol, 66(18):1-187.