nach oben

Journal of Assisted Reproduction and Genetics

Erschienen in:

01.04.2013 | Gamete Biology

Characterization of 3-hydroxyisobutyrate dehydrogenase, HIBADH, as a sperm-motility marker

verfasst von: Yung-Chieh Tasi, Hsin-Chih Albert Chao, Chia-Ling Chung, Xiu-Ying Liu, Ying-Ming Lin, Pao-Chi Liao, Hsien-An Pan, Han-Sun Chiang, Pao-Lin Kuo, Ying-Hung Lin

Erschienen in: Journal of Assisted Reproduction and Genetics | Ausgabe 4/2013

Einloggen, um Zugang zu erhalten

Abstract

Purpose

Asthenozoospermia is a major cause of male infertility. However, the molecular mechanisms underlying sperm-motility defects remain largely unknown in the majority of cases. In our previous study, we applied a proteomic approach to identify unknown proteins that were downregulated in spermatozoa with low motility compared to spermatozoa with good motility. Several sperm motility- related proteins have been identified. In this study, 3-hydroxyisobutyrate dehydrogenase (HIBADH), one of the proteins identified using the proteomic tools, is further characterized.

Methods

Reverse-transcription polymerase chain reactions (RT-PCR), western blotting, and immunofluorescence assays (IFA) were preformed to investigate the expression pattern. The enzymatic activity of HIBADH was evaluated in sperm with good (>50 %), moderate (< 50 %) and lower motility (< 20 %).

Results

Using RT-PCR, we found that transcripts of HIBADH are enriched in the cerebellum, heart, skeletal muscle, uterus, placenta, and testes of male humans. In western blotting, it is expressed in the placenta, testes, and spermatozoa. During spermiogenesis, HIBADH is located at the mid-piece (a specialized development from the mitochondria) of elongating, elongated, and mature sperm. The enzymatic activity of HIBADH in sperm with moderate and lower motility were significantly reduced compared with good motility (P < 0.0001 and P < 0.05, respectively).

Conclusions

Our study indicated that HIBADH is involved in the mitochondrial function of spermatozoa, and maintains sperm motility. It may serve as a sperm-motility marker.

Nur mit Berechtigung zugänglich

Hughes V. Geneticists crack the code of infertility. Nat Med. 2008;14:1174.PubMedCrossRef

Boivin J, Bunting L, Collins JA, Nygren KG. International estimates of infertility prevalence and treatment-seeking: potential need and demand for infertility medical care. Hum Reprod. 2007;22:1506–12.PubMedCrossRef

Carlsen E, Giwercman A, Keiding N, Skakkebaek NE. Evidence for decreasing quality of semen during past 50 years. BMJ. 1992;305:609–13.PubMedCrossRef

Mukhopadhyay D, Varghese AC, Pal M, Banerjee SK, Bhattacharyya AK, Sharma RK, et al. Semen quality and age-specific changes: a study between two decades on 3,729 male partners of couples with normal sperm count and attending an andrology laboratory for infertility-related problems in an Indian city. Fertil Steril. 2010;93:2247–54.PubMedCrossRef

WHO. World Health Organization Laboratory manual for the examination of human semen and sperm-cervical mucus interaction. 1999.

Boyle CA, Khoury MJ, Katz DF, Annest JL, Kresnow MJ, DeStefano F, et al. The relation of computer-based measures of sperm morphology and motility to male infertility. Epidemiology. 1992;3:239–46.PubMedCrossRef

Curi SM, Ariagno JI, Chenlo PH, Mendeluk GR, Pugliese MN, Sardi Segovia LM, et al. Asthenozoospermia: analysis of a large population. Arch Androl. 2003;49:343–9.PubMedCrossRef

Ryder TA, Mobberley MA, Hughes L, Hendry WF. A survey of the ultrastructural defects associated with absent or impaired human sperm motility. Fertil Steril. 1990;53:556–60.PubMed

Comhaire FH, Mahmoud AM, Depuydt CE, Zalata AA, Christophe AB. Mechanisms and effects of male genital tract infection on sperm quality and fertilizing potential: the andrologist’s viewpoint. Hum Reprod Updat. 1999;5:393–8.CrossRef

10.

Infante JP, Huszagh VA. Synthesis of highly unsaturated phosphatidylcholines in the development of sperm motility: a role for epididymal glycerol-3-phosphorylcholine. Mol Cell Biochem. 1985;69:3–6.PubMedCrossRef

11.

Visconti PE, Johnson LR, Oyaski M, Fornes M, Moss SB, Gerton GL, et al. Regulation, localization, and anchoring of protein kinase A subunits during mouse sperm capacitation. Dev Biol. 1997;192:351–63.PubMedCrossRef

12.

Nolan MA, Babcock DF, Wennemuth G, Brown W, Burton KA, McKnight GS. Sperm-specific protein kinase A catalytic subunit Calpha2 orchestrates cAMP signaling for male fertility. Proc Natl Acad Sci U S A. 2004;101:13483–8.PubMedCrossRef

13.

White DR, Aitken RJ. Relationship between calcium, cyclic AMP, ATP, and intracellular pH and the capacity of hamster spermatozoa to express hyperactivated motility. Gamete Res. 1989;22:163–77.PubMedCrossRef

14.

Ho HC, Granish KA, Suarez SS. Hyperactivated motility of bull sperm is triggered at the axoneme by Ca2+ and not cAMP. Dev Biol. 2002;250:208–17.PubMedCrossRef

15.

Ren D, Navarro B, Perez G, Jackson AC, Hsu S, Shi Q, et al. A sperm ion channel required for sperm motility and male fertility. Nature. 2001;413:603–9.PubMedCrossRef

16.

Sakata Y, Saegusa H, Zong S, Osanai M, Murakoshi T, Shimizu Y, et al. Ca(v)2.3 (alpha1E) Ca2+ channel participates in the control of sperm function. FEBS Lett. 2002;516:229–33.PubMedCrossRef

17.

Makler A, David R, Blumenfeld Z, Better OS. Factors affecting sperm motility. VII. Sperm viability as affected by change of pH and osmolarity of semen and urine specimens. Fertil Steril. 1981;36:507–11.PubMed

18.

Martinez-Heredia J, Estanyol JM, Ballesca JL, Oliva R. Proteomic identification of human sperm proteins. Proteomics. 2006;6:4356–69.PubMedCrossRef

19.

Guo X, Shen J, Xia Z, Zhang R, Zhang P, Zhao C, et al. Proteomic analysis of proteins involved in spermiogenesis in mouse. J Proteome Res. 2010;9:1246–56.PubMedCrossRef

20.

Baker MA. The ’omics revolution and our understanding of sperm cell biology. Asian J Androl. 2011;13:6–10.PubMedCrossRef

21.

Shetty J, Diekman AB, Jayes FC, Sherman NE, Naaby-Hansen S, Flickinger CJ, et al. Differential extraction and enrichment of human sperm surface proteins in a proteome: identification of immunocontraceptive candidates. Electrophoresis. 2001;22:3053–66.PubMedCrossRef

22.

Shetty J, Naaby-Hansen S, Shibahara H, Bronson R, Flickinger CJ, Herr JC. Human sperm proteome: immunodominant sperm surface antigens identified with sera from infertile men and women. Biol Reprod. 1999;61:61–9.PubMedCrossRef

23.

Shibahara H, Sato I, Shetty J, Naaby-Hansen S, Herr JC, Wakimoto E, et al. Two-dimensional electrophoretic analysis of sperm antigens recognized by sperm immobilizing antibodies detected in infertile women. J Reprod Immunol. 2002;53:1–12.PubMedCrossRef

24.

Naaby-Hansen S, Mandal A, Wolkowicz MJ, Sen B, Westbrook VA, Shetty J, et al. CABYR, a novel calcium-binding tyrosine phosphorylation-regulated fibrous sheath protein involved in capacitation. Dev Biol. 2002;242:236–54.PubMedCrossRef

25.

Ficarro S, Chertihin O, Westbrook VA, White F, Jayes F, Kalab P, et al. Phosphoproteome analysis of capacitated human sperm. Evidence of tyrosine phosphorylation of a kinase-anchoring protein 3 and valosin-containing protein/p97 during capacitation. J Biol Chem. 2003;278:11579–89.PubMedCrossRef

26.

Baker MA, Witherdin R, Hetherington L, Cunningham-Smith K, Aitken RJ. Identification of post-translational modifications that occur during sperm maturation using difference in two-dimensional gel electrophoresis. Proteomics. 2005;5:1003–12.PubMedCrossRef

27.

Zhao C, Huo R, Wang FQ, Lin M, Zhou ZM, Sha JH. Identification of several proteins involved in regulation of sperm motility by proteomic analysis. Fertil Steril. 2007;87:436–8.PubMedCrossRef

28.

Martinez-Heredia J, de Mateo S, Vidal-Taboada JM, Ballesca JL, Oliva R. Identification of proteomic differences in asthenozoospermic sperm samples. Hum Reprod. 2008;23:783–91.PubMedCrossRef

29.

Chan CC, Shui HA, Wu CH, Wang CY, Sun GH, Chen HM, et al. Motility and protein phosphorylation in healthy and asthenozoospermic sperm. J Proteome Res. 2009;8:5382–6.PubMedCrossRef

30.

Siva AB, Kameshwari DB, Singh V, Pavani K, Sundaram CS, Rangaraj N, et al. Proteomics-based study on asthenozoospermia: differential expression of proteasome alpha complex. Mol Hum Reprod. 2010;16:452–62.PubMedCrossRef

31.

Parte PP, Rao P, Redij S, Lobo V, D’Souza SJ, Gajbhiye R, Kulkarni V. Sperm phosphoproteome profiling by ultra performance liquid chromatography followed by data independent analysis (LC-MS(E)) reveals altered proteomic signatures in asthenozoospermia. J Proteomics 2012.

32.

Chao HC, Chung CL, Pan HA, Liao PC, Kuo PL, Hsu CC. Protein tyrosine phosphatase non-receptor type 14 is a novel sperm-motility biomarker. J Assist Reprod Genet. 2011;28:851–61.PubMedCrossRef

33.

Rougraff PM, Paxton R, Kuntz MJ, Crabb DW, Harris RA. Purification and characterization of 3-hydroxyisobutyrate dehydrogenase from rabbit liver. J Biol Chem. 1988;263:327–31.PubMed

34.

Rougraff PM, Zhang B, Kuntz MJ, Harris RA, Crabb DW. Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases. J Biol Chem. 1989;264:5899–903.PubMed

35.

Marshall VD, Sokatch JR. Regulation of valine catabolism in Pseudomonas putida. J Bacteriol. 1972;110:1073–81.PubMed

36.

Koyama S, Hata S, Witt CC, Ono Y, Lerche S, Ojima K, et al. Muscle RING-finger protein-1 (MuRF1) as a connector of muscle energy metabolism and protein synthesis. J Mol Biol. 2008;376:1224–36.PubMedCrossRef

37.

Lin YH, Lin YM, Teng YN, Hsieh TY, Lin YS, Kuo PL. Identification of ten novel genes involved in human spermatogenesis by microarray analysis of testicular tissue. Fertil Steril. 2006;86:1650–8.PubMedCrossRef

38.

Cheng YS, Kuo PL, Teng YN, Kuo TY, Chung CL, Lin YH, et al. Association of spermatogenic failure with decreased CDC25A expression in infertile men. Hum Reprod. 2006;21:2346–52.PubMedCrossRef

39.

Yeh YC, Yang VC, Huang SC, Lo NW. Stage-dependent expression of extra-embryonic tissue-spermatogenesis-homeobox gene 1 (ESX1) protein, a candidate marker for X chromosome-bearing sperm. Reprod Fertil Dev. 2005;17:447–55.PubMedCrossRef

40.

Hawes JW, Crabb DW, Chan RM, Rougraff PM, Harris RA. Chemical modification and site-directed mutagenesis studies of rat 3-hydroxyisobutyrate dehydrogenase. Biochemistry. 1995;34:4231–7.PubMedCrossRef

41.

Murin R, Schaer A, Kowtharapu BS, Verleysdonk S, Hamprecht B. Expression of 3-hydroxyisobutyrate dehydrogenase in cultured neural cells. J Neurochem. 2008;105:1176–86.PubMedCrossRef

42.

Kidd SA, Eskenazi B, Wyrobek AJ. Effects of male age on semen quality and fertility: a review of the literature. Fertil Steril. 2001;75:237–48.PubMedCrossRef

43.

Olds-Clarke P. How does poor motility alter sperm fertilizing ability? J Androl. 1996;17:183–6.PubMed

44.

Mukai C, Okuno M. Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm flagellar movement. Biol Reprod. 2004;71:540–7.PubMedCrossRef

45.

Burgos C, Maldonado C. Gerez de Burgos NM, Aoki A, Blanco A. Intracellular localization of the testicular and sperm-specific lactate dehydrogenase isozyme C4 in mice. Biol Reprod. 1995;53:84–92.PubMedCrossRef

46.

Travis AJ, Foster JA, Rosenbaum NA, Visconti PE, Gerton GL, Kopf GS, et al. Targeting of a germ cell-specific type 1 hexokinase lacking a porin-binding domain to the mitochondria as well as to the head and fibrous sheath of murine spermatozoa. Mol Biol Cell. 1998;9:263–76.PubMed

47.

Worrall EB, Gassain S, Cox DJ, Sugden MC, Palmer TN. 3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase. Biochem J. 1987;241:297–300.PubMed

48.

Mathews CK vHKaAK. Biochemistry. San Francisco,USA: Addison Wesley Longman Press; 2000.

49.

Albarracin JL, Mogas T, Palomo MJ, Pena A, Rigau T, Rodriguez-Gil JE. In vitro capacitation and acrosome reaction of dog spermatozoa can be feasibly attained in a defined medium without glucose. Reprod Domest Anim. 2004;39:129–35.PubMedCrossRef

50.

Ballester J, Fernandez-Novell JM, Rutllant J, Garcia-Rocha M, Jesus Palomo M, Mogas T, et al. Evidence for a functional glycogen metabolism in mature mammalian spermatozoa. Mol Reprod Dev. 2000;56:207–19.PubMedCrossRef

51.

Williams AC, Ford WC. The role of glucose in supporting motility and capacitation in human spermatozoa. J Androl. 2001;22:680–95.PubMed

52.

Galantino-Homer HL, Florman HM, Storey BT, Dobrinski I, Kopf GS. Bovine sperm capacitation: assessment of phosphodiesterase activity and intracellular alkalinization on capacitation-associated protein tyrosine phosphorylation. Mol Reprod Dev. 2004;67:487–500.PubMedCrossRef

Titel: Characterization of 3-hydroxyisobutyrate dehydrogenase, HIBADH, as a sperm-motility marker
verfasst von: Yung-Chieh Tasi
Hsin-Chih Albert Chao
Chia-Ling Chung
Xiu-Ying Liu
Ying-Ming Lin
Pao-Chi Liao
Hsien-An Pan
Han-Sun Chiang
Pao-Lin Kuo
Ying-Hung Lin
Publikationsdatum: 01.04.2013
Verlag: Springer US
Erschienen in: Journal of Assisted Reproduction and Genetics / Ausgabe 4/2013
Print ISSN: 1058-0468
Elektronische ISSN: 1573-7330
DOI: https://doi.org/10.1007/s10815-013-9954-8

Update Gynäkologie

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert – ganz bequem per eMail.

Newsletter bestellen

Springer Medizin

Characterization of 3-hydroxyisobutyrate dehydrogenase, HIBADH, as a sperm-motility marker