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Effect of nitric oxide on Sertoli cell microtubule of piglets

Published online by Cambridge University Press:  29 January 2010

Yang Li ,
Wang Xian-zhong ,
Yang Meng-bo  and
Zhang Jia-hua
Yang Li
Affiliation:
Chongqing Key Laboratory of Forage & Herbivore, College of Animal Science and Technology, Southwest University, Chongqing 400716, China
Wang Xian-zhong
Affiliation:
Chongqing Key Laboratory of Forage & Herbivore, College of Animal Science and Technology, Southwest University, Chongqing 400716, China
Yang Meng-bo
Affiliation:
Chongqing Key Laboratory of Forage & Herbivore, College of Animal Science and Technology, Southwest University, Chongqing 400716, China
Zhang Jia-hua*
Affiliation:
Chongqing Key Laboratory of Forage & Herbivore, College of Animal Science and Technology, Southwest University, Chongqing 400716, China
*
* Corresponding author. E-mail: [email protected]
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Abstract

To illustrate the effect of nitric oxide (NO) on the microtubules of Sertoli cells (SC), SCs of piglets were treated with sodium nitroprusside (SNP). Changes in cell viability, anti-oxidant activity, enzyme activity and p38 mutagen-activated protein kinase (p38MAPK) activation were detected. The results were as follows. A low concentration of NO can keep SC microtubule and cell viability normal, and a high concentration of NO could increase p38MAPK activation, decrease anti-oxidant activity and transferrin secretion, and destroy the structure and distribution of the microtubules. The results suggest that SNP treatment results in an increase in NO in SCs and decreased cell anti-oxidant activity. The high concentration of NO destroys cell microtubules by activating p38MAPK.

Keywords

Sertoli cellsnitric oxidemicrotubule
Type
Research Papers
Information
Chinese Journal of Agricultural Biotechnology , Volume 6 , Issue 3 , December 2009 , pp. 257 - 263
Copyright
Copyright © China Agricultural University 2009

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References

Bauche, F, Fouchard, MH and Jegou, B (1994) Antioxidant system in rat testicular cells. FEBS Letters 349: 392–396.CrossRefGoogle ScholarPubMed
Carini, R, de Grazia, C, Splendore, R, et al. (2003) Signal pathway responsible for hepatocyte preconditioning by nitric oxide. Free Radical Biology and Medicine 34: 1047–1055.Google Scholar
Davis, KL, Martin, E, Turko, IV and Murad, F (2001) Novel effects of nitric oxide. Annual Review of Pharmacology and Toxicology 41: 203–236.CrossRefGoogle ScholarPubMed
Endo, S and Launey, T (2003) Nitric oxide activates extracellular signal-regulated kinase 1/2 and enhances declustering of ionotropic glutamate receptor subunit 2/3 in rat cerebellar Purkinje cells. Neuroscience Letters 350: 122–126.Google Scholar
Hanafy, KA, Krumenacker, JS and Murad, F (2001) NO, nitrotyrosine, and cyclic GMP in signal transduction. Medical Science Monitor 7: 801–819.Google Scholar
He, LP, Tian, Y, Li, MX, Liao, Y and Zhu, SY (2002) Effect of nitric oxide pathway on sperm autogenesis in rats. Basic and Clinical Medicine 22: 88–91 (in Chinese with English abstract).Google Scholar
Hogg, N, Singh, RJ and Kalyanaraman, B (1996) The role of glutathione in the transport and catabolism of nitric oxide. FEBS Letters 382: 223–228.CrossRefGoogle ScholarPubMed
Kang, YM, Zhang, J, Li, J and Duan, XL (2002) Research advance in nitric oxide and nitric oxide synthase in testis. Bulletin of the Academy of Military Medical Sciences 26: 301–304 (in Chinese with English abstract).Google Scholar
Landino, LM, Hasan, R, McGaw, A, et al. (2002) Peroxynitrite oxidation of tubulin sulfhydryls inhibits microtubule polymerization. Archives of Biochemistry and Biophysics 398: 213–220.Google Scholar
Landino, LM, Koumas, MT, Mason, CE and Alston, JA (2007) Modification of tubulin cysteines by nitric oxide and nitroxyl donors alters tubulin polymerization activity. Chemical Research in Toxicology 20: 1693–1700.CrossRefGoogle ScholarPubMed
Lee, NP and Cheng, CY (2004a) Adaptors, junction dynamics and spermatogenesis. Biology of Reproduction 71: 392–404.CrossRefGoogle ScholarPubMed
Lee, NP and Cheng, CY (2004b) Nitric oxide/nitric oxide synthase, spermatogenesis and tight junction dynamics. Biology of Reproduction 70: 267–276.Google Scholar
Maccarrone, M, Cecconi, S, Rossi, G, Battista, N, Pauselli, R and Finazzi-Agro, A (2003) Anandamide activity and degradation are regulated by early postnatal aging and follicle-stimulating hormone in mouse Sertoli cells. Endocrinology 144: 20–28.CrossRefGoogle ScholarPubMed
Tepperman, BL, Abrahamson, TD and Soper, BD (1998) The role of cyclic guanylate monophosphate in nitric oxide-induced injury to rat small intestinal epithelial cells. The Journal of Pharmacology and Experimental Therapeutics 284: 929–933.Google Scholar
Tukey, JW (1965) Data analysis and the frontiers of geophysics: more can be learned from data by wise use of spectrum analysis, choice of expression and straggling values. Science 148: 1283–1289.Google Scholar
Vaananen, AJ, Kankuri, E and Rauhala, P (2005) Nitric oxide-related species-induced protein oxidation: reversible, irreversible and protective effects on enzyme function of papain. Free Radical Biology and Medicine 38: 1102–1111.CrossRefGoogle ScholarPubMed
Wang, XZ, Sun, Y, Pan, HM, Wu, JY and Zhang, JH (2006) Regulating the expression of StAR through ERK1/2 pathway activation. Veterinaria et Zootechnica Sinica 37: 1154–1159 (in Chinese with English abstract).Google Scholar
Yamamoto, T, Yuyama, K and Yamamoto, H (2006) Low concentrations of nitric oxide (NO) induced cell death in PC12 cells through activation of p38 mitogen-activated protein kinase (p38MAPK) but not via extracellular signal-regulated kinases (ERK1/2) or c-Jun N-terminal protein kinase (JNK). Neuroscience Letters 392: 170–173.Google Scholar
Yang, MG, Hao, XK, Yang, Y, et al. (2004) Relation of nitric oxide with transferrin content in human semen. Journal of the Fourth Military Medical University 25: 725–727 (in Chinese with English abstract).Google Scholar
Zhu, Q, Emanuele, NV and Van, TD (2004) Calponin is expressed by Sertoli cells within rat testes and is associated with actin-enriched cytoskeleton. Cell and Tissue Research 316: 243–253.Google Scholar