BibTex RIS Cite

Malate dehydrogenase activity in human seminal plasma and spermatozoa homogenates

Year 2013, Volume: 38 Issue: 4, 648 - 658, 01.12.2013

Abstract

Purpose: Malate Dehydrogenase is an important enzyme of the Krebs cycle, most cells require this enzyme for their metabolic activity. We evaluated the Malate Dehydrogenase (NAD/NADP) activity in human seminal plasma and sperm homogenates in normozoospermic, fertile and infertile males. Also glucose and fructose concentrations were determined in the seminal plasma samples. Material and Methods: Malate Dehydrogenase (NAD/NADP) activity in human seminal plasma and sperm homogenates of normozoospermic and infertile males was determined by spectrophotometric method. Semen analysis was considered according to the WHO Criteria. Results: Malat Dehydrogenase-NAD value in seminal plasma (the mean ± SD, mU/ml) of asthenoteratospermic (40.0±25.7) and azospermic (38.0±43.6) groups were significantly lower than normozoospermic, (93.9±52.1) males. Malat Dehydrogenase-NAD value in sperm homogenates (the mean ± SD, mU/ 20x106 sperm) of teratospermic group (136.8±61.8) was significantly higher compared to the normozoospermic (87.3±26.5) males. Glucose concentration (mg/dl) in asthenoteratospermic (4.0±1.4) and azospermic (15.4±6.4) groups were significantly higher than fertile (2.0±2.1) males. Also fructose concentration (mg/dl) in asthenoteratospermic (706.6±143.3) and azospermic (338.1±228.2) groups were significantly high compared to the normozoospermic (184.7±124.8) group. Conclusion: Sperm may be some part of the source of Malat Dehydrogenase activity in semen. Malat Dehydrogenase activity in seminal plasma has an important role on energy metabolism of sperm. Intermediate substrates of Krebs cycle might have been produced under the control of Malat Dehydrogenase and these substrates may be important for sperm motility and male infertility.Key words:

References

  • Baker HWG. Male infertility. Endocrinology and metabolism clinics of North America. 1994;23:783-93.
  • Machelle MS. Infertility. USA, Prentice Hall Publishing. 1990; 1-21
  • Iammarone E, Balet R, Lower AM, Gillott C, Grudzinskas JG. Male infertility.Best Pract Res Clin Obstet Gynaecol. 2003; 17:211-29.
  • Mukai C, Okuno M. Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm. Biol Reprod. 2004; 4:540-47.
  • Christopher RG, Nicholls DJ. Malate dehydrogenase: A model for structure, evolution, and catalysis. Protein Science. 1994; 3:1883-88.
  • Wright, SK., Kish, MM., Viola RE. From Malate dehydrogenase to phenyllactate dehydrogenase. J Biol Chem.2000; 275:31689-94.
  • Yang Z, Zhang H, Hung HC, Kuo CC, Tsai LC, Yuan HS et al. Structural studies of the pigeon cytosolic NADP+-dependent malic enzyme. Protein Science. 2002; 11:332-341.
  • Bhargava G, Mui S, Pav S, Wu H, Loeber G, Tong L, Preliminary crystallographic studies of human mitochondrial NAD(P)+- dependent malic enzyme. J Struc Biol. 1999; 127:72-5.
  • Cordoba M, Pintos LN, Beconi MT. Heparin and quercitin generate differential metabolic pathways that involve aminotransferases and LDH-X dehydrogenase in cryopreserved bovine spermatozoa. Theriogenology. 2007; 67:648-54.
  • Suominen J. Seminal fructose and glucose in asthenozoospermia. Int J Androl. 2001;24:253-54.
  • Boussouar F, Benahmed M. Lactate and energy metabolism in male germ cells. Trend in Endoc Metab. 2004;15:345-50.
  • World Health Organization WHO. Laboratory Manual for the Examination of Human Semen and Semencervical Mucus Interaction, 4th ed:4-23 Cambridge UK:Cambridge University Press, 1999.
  • Worthington Enzyme Manual Malate dehydrogenase assay. Worthington Biochemical Corp.Lakewood NJ. 19 Lahnsteiner F, Berger B, Weismann T, Patzner RA. Determination of semen quality of the rainbow trout, Onchorynchus mykiss, by sperm motility, seminal plasma parameters, and spermatozoal metabolism. Aquaculture. 1998; 163: 163-81.
  • Zilli L, Schiavone R, Zonno V, Storelli C, Vilell S. Adenosine triphosphate concentration and ß-Dglucuronidase activity as indicators of sea bass semen quality. Biology of Reproduction. 2004; 70:1679–84.
  • Prasad R, Mumford D, Gordon H. Lactate and malate dehydrogenase and alpha- esterases in oligospermia. Fertil Steril. 1976; 27:832-5.
  • Cordoba M. Pintos L. Beconi T. Differential activities of malate and isocitrate NAD(P) dependent dehydrogenases are involved in the induction of capacitation and acrosome reaction in cryopreserved bovine spermatozoa. Andrologia. 2004; 37:40-6.
  • Kohsaka T, Takahara H, Tagami S, Sasada H, Masaki J. A new technique for the precise location of lactate and malate dehydrogenase in goat, boar and water buffalo spermatozoa using gel incubation film. J Reprod Fertil. 1992; 95: 201-9.
  • Matsuzawa T, Sawada H. Histochemical changes in rat sperm malate dehydrogenase activities during passage through epididymis. Endocrinol Jpn. 1987; 34:231-5.
  • Albarraccin JL, Fernandez-Novell JM, Ballester J, Rauch MC, Moreno AQ, Pena A et.al. Gluconeogenesis-Linked Glycogen Metabolism Is Important in the Achievement of In Vitro Capacitation of Dog Spermatozoa in a Medium Glucose. Biol Reprod. 2004; 71:1437-45.
  • Miki K, Qu W, Goulding EH, Willis WD, BunchDO, Strader LF et.al. Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. PNAS. 2004; 101:16501-06.
  • Fadıloğlu, M., Ulman, C., Önvural, B., Önvural A., The seminal fluid isoenzyme LDH-C4 in infertile men. Tr. J. Medical Sciences.1998; 28:609-13.
  • Yazışma Adresi / Address for Correspondence: Hülya Leventerler Faculty of Medicine, Cukurova University, Gynecology and Obstetric Department Center of Assisted Reproduction Adana, Turkey Phone: 03223386060-3831
  • E-mail: hleventerler@cu.edu.tr geliş tarihi/received :24.09.2013 kabul tarihi/accepted:07.12.2013

İnsan Seminal Plazma ve Spermatozoa Homojenatlarında Malat Dehidrogenaz Aktivitesi

Year 2013, Volume: 38 Issue: 4, 648 - 658, 01.12.2013

Abstract

Amaç: Malat Dehidrogenaz, Krebs siklusunun önemli bir enzimi olup pek çok hücre metabolik aktiviteleri için bu enzime ihtiyaç duymaktadır. Normozoospermik, fertil ve infertil erkeklerin seminal plazma ve sperm homojenatlarında Malat Dehidrogenaz (NAD/NADP) aktivitesi ölçüldü. Ayrıca seminal plazma örneklerinde glukoz ve fruktoz konsantrasyonları tesbit edildi. Materyal ve Metod: Normozoospermik, fertil ve infertil erkeklerin seminal plazma ve sperm homojenatlarında Malat Dehidrogenaz (NAD/NADP) aktivitesi spektrofotometrik yöntemle ölçüldü. Semen analizi WHO kriterlerine göre değerlendirildi. Bulgular: Seminal plazmada MDH-NAD değeri (ortalama ± SD, mU/ml), astenoteratospermik (40.0±25.7) ve azospermik (38.0±43.6) gruplarda, normozoospermik, fertil erkeklerden (93.9±52.1) anlamlı düzeyde düşük bulunmuştur. Sperm homojenatlarında MDH-NAD değeri (ortalama ± SD, mU/ 20x106 sperm) teratospermik grupta (136.8±61.8) normozoospermik, fertil erkeklerden (87.3±26.5) anlamlı düzeyde yüksek bulunmuştur. Glukoz konsantrasyonu (mg/dl), astenoteratospermik (4.0±1.4) ve azospermik (15.4±6.4) gruplarda fertil erkeklerden anlamlı düzeyde (2.0±2.1) yüksek bulunmuştur. Benzer şekilde fruktoz konsantrasyonu (mg/dl), astenoteratospermik (706.6±143.3) ve azospermik (338.1±228.2) gruplarda fertil erkeklerden anlamlı düzeyde (184.7±124.8) yüksek bulunmuştur. Sonuç: Sperm, semendeki MDH aktivite kaynağının bir bölümü olabilir. Seminal plazmadaki MDH aktivitesi spermin enerji metabolizmasında önemli bir rol oynamaktadır. Krebs siklusunun ara substratları MDH"ın kontrolünde üretilmiş olabilir ve bu substratlar sperm motilitesi ve erkek infertilitesi için önemli olabilir.Anahtar Kelimeler:

References

  • Baker HWG. Male infertility. Endocrinology and metabolism clinics of North America. 1994;23:783-93.
  • Machelle MS. Infertility. USA, Prentice Hall Publishing. 1990; 1-21
  • Iammarone E, Balet R, Lower AM, Gillott C, Grudzinskas JG. Male infertility.Best Pract Res Clin Obstet Gynaecol. 2003; 17:211-29.
  • Mukai C, Okuno M. Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm. Biol Reprod. 2004; 4:540-47.
  • Christopher RG, Nicholls DJ. Malate dehydrogenase: A model for structure, evolution, and catalysis. Protein Science. 1994; 3:1883-88.
  • Wright, SK., Kish, MM., Viola RE. From Malate dehydrogenase to phenyllactate dehydrogenase. J Biol Chem.2000; 275:31689-94.
  • Yang Z, Zhang H, Hung HC, Kuo CC, Tsai LC, Yuan HS et al. Structural studies of the pigeon cytosolic NADP+-dependent malic enzyme. Protein Science. 2002; 11:332-341.
  • Bhargava G, Mui S, Pav S, Wu H, Loeber G, Tong L, Preliminary crystallographic studies of human mitochondrial NAD(P)+- dependent malic enzyme. J Struc Biol. 1999; 127:72-5.
  • Cordoba M, Pintos LN, Beconi MT. Heparin and quercitin generate differential metabolic pathways that involve aminotransferases and LDH-X dehydrogenase in cryopreserved bovine spermatozoa. Theriogenology. 2007; 67:648-54.
  • Suominen J. Seminal fructose and glucose in asthenozoospermia. Int J Androl. 2001;24:253-54.
  • Boussouar F, Benahmed M. Lactate and energy metabolism in male germ cells. Trend in Endoc Metab. 2004;15:345-50.
  • World Health Organization WHO. Laboratory Manual for the Examination of Human Semen and Semencervical Mucus Interaction, 4th ed:4-23 Cambridge UK:Cambridge University Press, 1999.
  • Worthington Enzyme Manual Malate dehydrogenase assay. Worthington Biochemical Corp.Lakewood NJ. 19 Lahnsteiner F, Berger B, Weismann T, Patzner RA. Determination of semen quality of the rainbow trout, Onchorynchus mykiss, by sperm motility, seminal plasma parameters, and spermatozoal metabolism. Aquaculture. 1998; 163: 163-81.
  • Zilli L, Schiavone R, Zonno V, Storelli C, Vilell S. Adenosine triphosphate concentration and ß-Dglucuronidase activity as indicators of sea bass semen quality. Biology of Reproduction. 2004; 70:1679–84.
  • Prasad R, Mumford D, Gordon H. Lactate and malate dehydrogenase and alpha- esterases in oligospermia. Fertil Steril. 1976; 27:832-5.
  • Cordoba M. Pintos L. Beconi T. Differential activities of malate and isocitrate NAD(P) dependent dehydrogenases are involved in the induction of capacitation and acrosome reaction in cryopreserved bovine spermatozoa. Andrologia. 2004; 37:40-6.
  • Kohsaka T, Takahara H, Tagami S, Sasada H, Masaki J. A new technique for the precise location of lactate and malate dehydrogenase in goat, boar and water buffalo spermatozoa using gel incubation film. J Reprod Fertil. 1992; 95: 201-9.
  • Matsuzawa T, Sawada H. Histochemical changes in rat sperm malate dehydrogenase activities during passage through epididymis. Endocrinol Jpn. 1987; 34:231-5.
  • Albarraccin JL, Fernandez-Novell JM, Ballester J, Rauch MC, Moreno AQ, Pena A et.al. Gluconeogenesis-Linked Glycogen Metabolism Is Important in the Achievement of In Vitro Capacitation of Dog Spermatozoa in a Medium Glucose. Biol Reprod. 2004; 71:1437-45.
  • Miki K, Qu W, Goulding EH, Willis WD, BunchDO, Strader LF et.al. Glyceraldehyde 3-phosphate dehydrogenase-S, a sperm-specific glycolytic enzyme, is required for sperm motility and male fertility. PNAS. 2004; 101:16501-06.
  • Fadıloğlu, M., Ulman, C., Önvural, B., Önvural A., The seminal fluid isoenzyme LDH-C4 in infertile men. Tr. J. Medical Sciences.1998; 28:609-13.
  • Yazışma Adresi / Address for Correspondence: Hülya Leventerler Faculty of Medicine, Cukurova University, Gynecology and Obstetric Department Center of Assisted Reproduction Adana, Turkey Phone: 03223386060-3831
  • E-mail: hleventerler@cu.edu.tr geliş tarihi/received :24.09.2013 kabul tarihi/accepted:07.12.2013
There are 23 citations in total.

Details

Primary Language Turkish
Journal Section Research
Authors

Hulya Leventerler This is me

Safiye Taga This is me

İbrahim Ferhat Urunsak This is me

İsmail Atilla Aridogan This is me

Suna Solmaz This is me

Mehmet Turan Cetin This is me

Nurten Dikmen This is me

Publication Date December 1, 2013
Published in Issue Year 2013 Volume: 38 Issue: 4

Cite

MLA Leventerler, Hulya et al. “İnsan Seminal Plazma Ve Spermatozoa Homojenatlarında Malat Dehidrogenaz Aktivitesi”. Cukurova Medical Journal, vol. 38, no. 4, 2013, pp. 648-5.