Comparative studies of gelatinase activity in cattle and buffalo bull seminal plasma through gelatin zymography

T C BALAMURUGAN; R PRAKASH KRUPAKARAN; S ARUNKUMAR; GURU D V PANDIYAN; P PERUMAL

doi:10.56093/ijans.v85i5.48544

Authors

T C BALAMURUGAN Assistant Professor, Veterinary College and Research Institute (TANUVAS), Orathanadu, Tamil Nadu 614 625 India
R PRAKASH KRUPAKARAN Associate Professor, Department of Veterinary Physiology and Biochemistry, TANUVAS- Veterinary College and Research Institute, Orathanadu, Tamil Nadu 614 625 India
S ARUNKUMAR Associate Professor, Department of Veterinary Parasitology, TANUVAS- Veterinary College and Research Institute, Orathanadu, Tamil Nadu 614 625 India
GURU D V PANDIYAN Assistant Professor, Veterinary College and Research Institute (TANUVAS), Orathanadu, Tamil Nadu 614 625 India
P PERUMAL Scientist, Animal Reproduction Division, ICAR-NRC on Mithun, Jharapani, Nagaland

https://doi.org/10.56093/ijans.v85i5.48544

Keywords:

Buffaloes, Gelatin zymography, Gelatinase, MMP, Seminal plasma

Abstract

A comparative study was undertaken to study the gelatinase activity in seminal plasma of Murrah buffalo and Jersey crossbred cattle bull through gelatin zymography. In gelatin zymography, the presence of 3 prominent bands at 220 KDa, 92 KDa and 72 KDa for both buffalo and cattle seminal plasma were observed. All these 3 forms are proteolytically active, degraded the gelatin in gelatin zymography. The 220 KDa homodimer of MMP-9 was very prominent in buffaloes semen compared to cattle semen. On the contrary, 135 KDa heterodimer of MMP -9 was observed only in cattle seminal plasma. The 72 KDa band was very feeble in both the cases. The level of expression of 220 KDa and 92 KDa bands was constant compared to that of 72 KDa. The relative amount of 92 KDa band to that of 72 KDa band was at least 3-5 times higher. The difference between buffalo and cattle seminal plasma was very obvious by the presence of 135 KDa band. On gelatin zymography, the distinguished feature of cattle seminal plasma was the presence of 135 KDa heterodimer of MMP. It is concluded that the 135 KDa band was observed
only in cattle seminal plasma. Further, more upregulation of MMP-9 mediated through MMP-2 activity was observed in buffalo seminal plasma.

Downloads

Download data is not yet available.

References

Baumgart E, Lenk V, Loening S A and Jung K. 2002. Tissue inhibitors of metalloproteinases 1 and 2 in human seminal plasma and their association with spermatozoa. International Journal of Andrology 25: 369–71. DOI: https://doi.org/10.1046/j.1365-2605.2002.00383.x

Bhakat C. 1994. ‘Effect of preputial washing and antibacterial treatment and preservability of bovine semen. ’ M. Sc. Thesis, NDRI Deemed University, Karnal, Haryana, India.

Bhakat M, Mohanty T K, Raina S, Gupta V S and Khan H M. 2011. Frozen semen production performance of Murrah buffalo bulls. Buffalo Bulletin 30 (2): 157–62.

Fiaz M, Usmani R H, Abdullah M and Ahmad T. 2010. Evaluation of semen quality of Holstein Friesian and Jersey bulls maintained under subtropical environment. Pakistan Veterinary Journal 30 (2): 75–78.

Fowlkes J L and Winkler M K. 2002. Exploring the interface between metallo-proteinase activity and growth factor and cytokine bioavailability. Cytokine and Growth Factor Reviews 13: 277–87. DOI: https://doi.org/10.1016/S1359-6101(02)00005-9

Gokhale S B, Mushtaque M, Phadke N L, Dinodkar R and Ambhore G S. 2003. Studies on the effect of hydrogen ion concentration of extender on semen characters of Murrah buffalo bulls. Indian Journal of Animal Reproduction 24 (2): 158–60.

Gurupriya V S, Divyashree B C and Roy S C. 2014. Cryogenic changes in proteases and antiprotease activities of buffalo (Bubalus bubalis) and cattle (Bos taurus) semen. Theriogenology 81: 396–402. DOI: https://doi.org/10.1016/j.theriogenology.2013.10.010

Heussen C and Dowdle E B. 1980. Electrophoretic analysis of plasminogen activators in polyacrylamide gels containing sodium dodecyl sulfate and copolymerized substrates. Analytical Biochemistry 102 (1): 196–202. DOI: https://doi.org/10.1016/0003-2697(80)90338-3

Hulboy D L, Rudolph L A and Matrisian L M. 1997. Matrix metalloproteinases as mediators of reproductive function. Molecular Human Reproduction 3: 27–45. DOI: https://doi.org/10.1093/molehr/3.1.27

Kanchan B and Singh N. 2005. Semen characteristics, semen discard rate and fertility in Murrah buffalo bulls. Indian Journal of Animal Reproduction 26 (2): 120–22.

Koivisto M B, Costa M T, Perri S H and Vicente W R. 2009. The effect of season on semen characteristics and freezability in Bos indicus and Bos taurus bulls in the south-eastern region of Brazil. Reproduction in Domestic Animals 44: 587–92. DOI: https://doi.org/10.1111/j.1439-0531.2008.01023.x

Kottowska M, Kot³owskaa R, Kowalskib J, Glogowskib J, Jankowskic A and Ciereszko 2005. Gelatinases and serine proteinase inhibitors of seminal plasma and the reproductive tract of turkey (Meleagris gallopavo). Theriogenology 63: 1667–81. DOI: https://doi.org/10.1016/j.theriogenology.2004.07.020

Kumar S, Sahni K L and Bistha G S. 1993. Cytomorphological characteristics of motile and static semen of buffalo bulls. Buffalo Journal 9 (2): 117–27.

Laemmli U K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680 – 85. DOI: https://doi.org/10.1038/227680a0

Makowski G S and Ramsby M L. 1996. Calibrating gelatin zymograms with human gelatinase standards. Analytical Biochemistry 236 (2): 353–56. DOI: https://doi.org/10.1006/abio.1996.0179

Mondal D K, Nagpaul P K and Gupta A K. 2000. Seasonal variation in seminal attributes and sexual behaviour of Murrah buffalo bulls. Indian Journal of Dairy Science 53: 278–83.

Nagase H and Woessner J F. 1999. Matrix metallo-proteinases. Journal of Biological Chemistry 274:21491–99. DOI: https://doi.org/10.1074/jbc.274.31.21491

Nagase H. 1996. Matrix metallo-proteinases. Ainc Metalloproteases in Health and Disease. pp- 153–204. (Ed.) Hooper N M. Taylor and Francis, London.

Nath R. 1988. ‘Cryopreservation of buffalo semen.’ M.V.Sc. Thesis GB University of Agricultural and Technology, Pantnagar, India.

Patel K V, Dhami A J, Chauhan M K, Dave A S, Vadodaria V P and Dugwekar Y G. 2000. Freezability, enzyme leakage and fertility of bovine spermatozoa. Indian Journal of Dairy Science 53 (4): 284–90.

Pipan M Z, Kosec M, Mrkun J and Zrimsek P. 2010. Gelatinases in boar seminal plasma and their relation to semen indicators. Acta Veterinary Brno 79: 491–96. DOI: https://doi.org/10.2754/avb201079030491

Ravimurugan T, Kanagaraj P and Thangaraju P. 2008. Frozen semen production potential of Murrah bulls. Tamilnadu Journal of Veterinary and Animal Sciences 25: 165–73.

Saengsoia W, Shiaa W Y, Shyua C L, Wub J T, Warinraka C, Wei-Ming Leea W M and Feng-Pang Cheng F P. 2011. Detection of matrix metalloproteinase MMP-2 and MMP-9 in canine seminal plasma. Animal Reproduction Science 127: 114–19. DOI: https://doi.org/10.1016/j.anireprosci.2011.07.004

Saxena V B and Tripathi S S. 1978. Studies on the physicochemical attributes and freezability of semen of crossbred bulls. Indian Journal of Animal Sciences 48: 865–69.

Singh S P, Pandit R K and Bhadoriya H B S. 2000. Sexual behaviour and seminal characteristics in Jersey, Sahiwal and half-bred bulls. Indian Journal of Animal Sciences 70 (3): 279– 80.

Sori H, Prasad S and Zewdie E. 2006. Seminal characterization of some elite Ethiopian indigenous breeds of bull. Indian Journal of Animal Reproduction 27 (2): 54–60.

Tentes I, Asimakopoulos B, Mourvati E, Diedrich K, Al-Hasani S and Nikolettos N. 2007. Matrix metalloproteinase (MMP)- 2 and MMP-9 in seminal plasma. Journal of Assisted Reproduction and Genetics 24: 278–81. DOI: https://doi.org/10.1007/s10815-007-9129-6

Tomar S S and Singh S P. 1996. Studies on reaction time and some of the seminal attributes and their inter-relationship in Murrah buffalo bulls. Indian Journal of Animal Research 30 (1): 49–54.

Woessner (Jr) J F. 1994. The family of matrix metalloproteinases. Annals of the New York Academy of Sciences 732: 11–21. DOI: https://doi.org/10.1111/j.1749-6632.1994.tb24720.x

Woessner J F. 1991. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB Journal 5: 2145–54. DOI: https://doi.org/10.1096/fasebj.5.8.1850705

Yin H Z, Vogel M M, Schneider M, Ercole C, Zhang G and Sinha A A. 1990. Gelatinolytic proteinase activities in human seminal plasma. Journal of Reproduction and Fertility 88: 491–501. DOI: https://doi.org/10.1530/jrf.0.0880491