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Fingerprinting of gelatinase subtypes for different topographic regions on non-retaining placenta of Holstein cows

Published online by Cambridge University Press:  17 October 2014

P. Piamya
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
A. Tiantong
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
S.-E. Chen
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
W.-B. Liu
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
C. Yu
Affiliation:
Department of Animal Science, National Pingtung University of Science and Technology, Pingtung 912, Taiwan, Republic of China
H. Nagahata
Affiliation:
Department of Animal Health, School of Veterinary Medicine, RakunoGakuen University, Ebetsu, Hokkaido 069-8501, Japan
C.-J. Chang*
Affiliation:
Department of Animal Science, National Chung Hsing University, Taichung 402, Taiwan, Republic of China
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Abstract

The contribution of matrix metalloproteinases (MMP) to timely discharge of the placenta from bovine uterus at parturition is yet inconclusive, partly because of the presence of multiple MMP forms in situ. In the current study, the expression of different gelatinase subtypes on non-retaining placentas of Holstein cows was fingerprinted by using gelatin zymography. Different topographic regions on the placenta were measured separately, including the placentome-like structure and the fetal and maternal sides of interplacentomal placenta, all sampled from the central and peripheral areas of the placenta, respectively. The spontaneously ruptured umbilical cords were cross-sectioned as fetus end, middle and placenta end also for separate measurement. Body fluids including blood samples from the parturient cows, their neonatal calves and umbilical cord, as well as fetal fluids and the first colostrum were measured concomitantly. Results showed multiple forms of gelatinases subtypes in the placenta tissues and body fluids, including neutrophil gelatinase-associated lipocalin (NGAL)-MMP-9 complex, both the latent and active forms of MMP-2 and MMP-9; of them, the latent forms were much more abundantly and frequently expressed than the active forms. NGAL-MMP-9 complex was more prevalently present in the body fluids than in the placenta tissues. No distinguishable pattern of the expression of any gelatinase subtype was observed among the placentome-like structure, interplacentomal placenta and umbilical cord, or between fetal and maternal sides. Nonetheless, for interplacentomal placenta, proMMP-9 expression was higher in the central than in the peripheral area. In addition, proMMP-2 expression was higher in the rupture end (fetus end) than the placenta end of the umbilical cord. In conclusion, the current validated gelatin zymography detected a gradient proMMP-9 expression on the non-retaining placenta of cows in reverse to the proximity to the umbilical insertion point, and a gradient proMMP-2 expression on a section of the umbilical cord in reverse to the proximity to the rupture site, suggesting roles played by gelatinases in normal discharge of the placenta at term.

Type
Research Article
Copyright
© The Animal Consortium 2014 

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References

Beceriklisoy, HB, Walter, I, Schafer-Somi, S, Miller, I, Kanca, H, Izgur, H and Aslan, S 2007. Matrix metalloproteinase (MMP)-2 and MMP-9 activity in the canine uterus before and during placentation. Reproduction of Domestic Animal 42, 654659.CrossRefGoogle ScholarPubMed
Bradford, M 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry 72, 248254.CrossRefGoogle ScholarPubMed
Cross, JC, Nakano, H, Natale, DR, Simmons, DG and Watson, ED 2006. Branching morphogenesis during development of placental villi. Differentiation 74, 393401.CrossRefGoogle ScholarPubMed
Demir-Weusten, AY, Seval, Y, Kaufmann, P, Demir, R, Yucel, G and Huppertz, B 2007. Matrix metalloproteinases-2, -3 and -9 in human term placenta. Acta Histochemica 109, 403412.CrossRefGoogle ScholarPubMed
Dilly, M, Hambruch, N, Shenavai, S, Schuler, G, Froehlich, R, Haeger, JD, Ozalp, GR and Pfarrer, C 2011. Expression of matrix metalloproteinase (MMP)-2, MMP-14 and tissue inhibitor of matrix metalloproteinase (TIMP)-2 during bovine placentation and at term with or without placental retention. Theriogenology 75, 11041114.CrossRefGoogle ScholarPubMed
Fernandez, CA, Yan, L, Louis, G, Yang, J, Kutok, JL and Moses, MA 2005. The matrix metalloproteinase-9/neutrophil gelatinase-associated lipocalin complex plays a role in breast tumor growth and is present in the urine of breast cancer patients. Clinical Cancer Research 11, 53905395.CrossRefGoogle Scholar
Kizaki, K, Ushizawa, K, Takahashi, T, Yamada, O, Todoroki, J, Sato, T, Ito, A and Hashizume, K 2008. Gelatinase (MMP-2 and -9) expression profiles during gestation in the bovine endometrium. Reproductive Biology and Endocrinology 6, 6676.CrossRefGoogle ScholarPubMed
Kjeldsen, L, Johnsen, AH, Sengelov, H and Borregaard, N 1993. Isolation and primary sequence of NGAL, a novel protein associated with human neutrophil gelatinase. Journal of Biological Chemistry 268, 1042510432.CrossRefGoogle ScholarPubMed
Klish, K, Hecht, W, Pfarrer, C, Schuler, G, Hoffmann, B and Leiser, B 1999. DNA content and ploidy level of bovine placentomal trophoblast giant cells. Placenta 20, 451458.CrossRefGoogle Scholar
Kolkenbrock, H, Hecker-Kia, A, Orgel, D, Kinawi, A and Ulbrich, N 1996. Progelatinase B forms from human neutrophils – complex formation of monomer/lipocalin with TIMP-1. Biological Chemistry 377, 529533.Google ScholarPubMed
Laemmli, UK 1970. Cleavage of structural proteins during assembly of the head bacteriophage T4. Nature 227, 680685.CrossRefGoogle ScholarPubMed
Maj, JG and Kankofer, M 1997. Activity of 72-kDa and 92-kDa matrix metalloproteinases in placental tissues of cows with and without retained fetal membranes. Placenta 18, 683687.CrossRefGoogle ScholarPubMed
Makowski, GS and Ramsby, ML 2003. Zymographic analysis of latent and activated forms of matrix metalloproteinase-2 and -9 in synovial fluid: correlation to polymorphonuclear leukocyte infiltration and in response to infection. Clinica Chimica Acta 329, 7781.CrossRefGoogle ScholarPubMed
McNaughton, AP and Murray, RD 2009. Structure and function of the bovine fetomaternal unit in relation to the causes of retained fetal membranes. Veterinary Record 165, 615622.CrossRefGoogle Scholar
Peter, AT 2013. Bovine placenta: a review on morphology, components, and defects from terminology and clinical perspectives. Theriogenology 80, 693705.CrossRefGoogle ScholarPubMed
Provatopoulou, X, Antonia, G, Eleni, K, Flora, Z, Ioannis, F, Evgenios, G, Afroditi, N, Ioannis, P and George, Z 2009. Circulating levels of matrix metalloproteinase-9 (MMP-9), neutrophil gelatinase-associated lipocalin (NGAL) and their complex MMP-9/NGAL in breast cancer disease. BMC Cancer 9, 390397.CrossRefGoogle ScholarPubMed
Pugin, J, Widmer, MC, Kossodo, S, Liang, CM, Preas, HHL and Suffredini, AF 1999. Human neutrophils secrete gelatinase B in vitro and in vivo in response to endotoxin and proinflammatory mediators. American Journal of Respiratory and Cell Molecular Biology 20, 458464.CrossRefGoogle ScholarPubMed
Roy, R, Louis, G, Loughlin, KR, Wiederschain, D, Kilroy, SM, Lamb, CC, Zurakowski, D and Moses, MA 2008. Tumor specific urinary matrix metalloproteinase fingerprinting: identification of high molecular weight urinary matrix metalloproteinase species. Clinical Cancer Research 14, 66106617.CrossRefGoogle ScholarPubMed
SAS Institute 2008. SAS/STAT user’s guide. Release 9.2. SAS Institute Inc., Cary, NC, USA.Google Scholar
Takagi, M, Yamamoto, D, Ohtani, M and Miyamoto, A 2007. Quantitative analysis of messenger RNA expression of matrix metalloproteinases (MMP-2 and MMP-9), tissue inhibitor-2 of matrix metalloproteinases (TIMP-2), and steroidogenic enzymes in bovine placentomes during gestation and postpartum. Molecular Reproduction and Development 74, 801807.CrossRefGoogle ScholarPubMed
Thomas, K, Thomson, AJ, Sephton, V, Cowan, C, Wood, S, Vince, G, Kingsland, CR and Lewis-Jones, DI 2002. The effect of gonadotrophic stimulation on integrin expression in the endometrium. Human Reproduction 17, 6368.CrossRefGoogle ScholarPubMed
Uekita, T, Yamanouchi, K, Sato, H, Tojo, H, Seiki, M and Tachi, C 2004. Expression and localization of matrix metalloproteinases (MT1-MMP, MMP-2) and tissue inhibitor of metalloproteinase-2 (TIMP-2) during synepitheliochorial placentation of goats (Capra hircus). Placenta 25, 810819.CrossRefGoogle ScholarPubMed
Vagnoni, KE, Zheng, J and Magness, RR 1998. Matrix metalloproteinases-2 and -9, and tissue inhibitor of metalloproteinase-1 of the sheep placenta during the last third of gestation. Placenta 19, 447455.CrossRefGoogle ScholarPubMed
Walter, I and Boos, A 2001. Matrix metalloproteinases (MMP-2 and MMP-9) and tissue inhibitor-2 of matrix metalloproteinases (TIMP-2) in the placenta and interplacental uterine wall in normal cows and in cattle with retention of fetal membrane placenta. Placenta 22, 473483.CrossRefGoogle ScholarPubMed
Wischral, A, Verreschi, ITN, Lima, SB, Hayashi, LF and Barnabe, RC 2001. Pre-parturition profile of steroids and prostaglandin in cows with or without foetal membrane retention. Animal Reproduction Science 67, 181188.CrossRefGoogle ScholarPubMed
Wooding, FB and Wathes, DC 1980. Binucleate cell migration in the bovine placentome. Journal of Reproduction and Fertility 59, 425430.CrossRefGoogle ScholarPubMed
Yan, L, Borregaard, N, Kjeldsen, L and Moses, MA 2001. The high molecular weight urinary matrix metalloproteinase (MMP) activity is a complex of gelatinase B/MMP-9 and neutrophil gelatinase-associated lipocalin (NGAL). Modulation of MMP-9 activity by NGAL. Journal of Biological Chemistry 276, 3725837265.CrossRefGoogle ScholarPubMed
Yu, TC, Chen, SE, Ho, CH, Peh, HC, Liu, WB, Tiantonga, A, Nagahata, H and Chang, CJ 2012. Involvement of TNF-α and MAPK pathway in the intramammary MMP-9 release via degranulation of cow neutrophils during acute mammary gland involution. Veterinary Immunology and Immunopathology 147, 161169.CrossRefGoogle ScholarPubMed