Gelatinase (MMP-2 and -9) expression profiles during gestation in the bovine endometrium

Kizaki, Keiichiro; Ushizawa, Koichi; Takahashi, Toshio; Yamada, Osamu; Todoroki, Junichi; Sato, Takashi; Ito, Akira; Hashizume, Kazuyoshi

doi:10.1186/1477-7827-6-66

Cited by 64 publications

(56 citation statements)

References 48 publications

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“…As for NGAL-MMP-9 complex, it seemed more prevalently detected in both fluids and placenta tissues than active MMP-9. Our reports of differential gelatinase expressions on bovine placenta largely agreed with other reports on similar terms using different estimation tools (Walter and Boos, 2001;Kizaki et al 2008;Dilly et al, 2011). Nevertheless, the physiological implications were yet inconclusive.…”

Section: Discussionsupporting

confidence: 89%

“…The association of members of MMP family with the spatial regulation of ECM degradation in the bovine placenta for subsequent release of fetal membranes postpartum have been explored using different approaches, such as immunohistochemical analysis, gene expression analysis and zymography (Walter and Boos, 2001;Takagi et al, 2007;Kizaki et al, 2008;Dilly et al, 2011). In this study, we used gelatin zymography to measure the expression level of gelatinase subtypes on different topographic locations of non-retaining cow placenta.…”

Section: Discussionmentioning

confidence: 99%

“…Maj and Kankofer (1997) suggested that this high proMMP-2/low active MMP-2 in bovine placenta might adversely affect the hydrolysis of collagen, and therefore might increase the rigidity of the intravillous ECM and, consequently, result in the etiology of placental retention. On the other hand, Kizaki et al (2008) recommended proMMP-2 to be a more favorable gelatinase than MMP-9 in endometrial remodeling for prepartum cows. McNaughton and Murray (2009) included TIMP into consideration and suggested that high ratio of MMP-9/TIMP-2 expression in placentome might be associated with bovine RFM because the interaction of MMP-9 with TIMP-2 helps prevent epithelial separation within the placentome.…”

Section: Discussionmentioning

confidence: 99%

“…They have been suggested to participate in the remodeling and ECM breakdown of the uterus during estrus cycle, placentation, implantation, gestation and periparturient in different species (Walter and Boos, 2001;Uekita et al, 2004;Demir-Weusten et al, 2007;Kizaki et al, 2008;McNaughton and Murray, 2009). Multiple forms of MMP-2 and -9 are present physiologically varying in molecular size and functionality, such as the low molecular weight MMP-2 species of 68, 64 and 60 kDa, respectively (Maj and Kankofer, 1997;Kizaki et al, 2008) and the high molecular weight MMP-9 species of 125 kDa (neutrophil gelatinase-associated lipocalin-MMP-9, NGAL-MMP-9), 140 kDa (MMP-9-tissue inhibitor of metalloproteinase, MMP-9-TIMP-1) and 220 kDa (MMP-9 dimmer), respectively (Fernandez et al, 2005;Roy et al, 2008;Provatopoulou et al, 2009). NGAL or lipocalin 2 is a prominent member of the lipocalin family (Kjeldsen et al, 1993) capable of binding hydrophobic molecules.…”

Section: Introductionmentioning

confidence: 99%

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

Piamya

Tiantong

Chen

et al. 2015

Animal

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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.

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Section: Discussionsupporting

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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

Piamya

Tiantong

Chen

et al. 2015

Animal

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“…In humans and rodents, MMPs play a pivotal role in the process of trophoblast invasion throughout the implantation and placentation periods, which require the degradation and remodeling of ECM at the feto-maternal interface (Cohen et al 2006). MMPs play a similar role in bovine trophoblasts (Hirata et al 2003, Kizaki et al 2008. Thus, further investigation on the upstream signaling of the upregulation of MMP2 and MMP9 transcription and their roles during the bovine attachment processes may provide insights into trophoblast behavior in the non-invasive mode of implantation.…”

Section: Discussionmentioning

confidence: 99%

Expression of mesenchymal-related genes by the bovine trophectoderm following conceptus attachment to the endometrial epithelium

Yamakoshi¹,

Bai²,

Chaen³

et al. 2012

Reproduction

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In the course of experiments to identify and characterize the factors that function in bovine conceptuses during peri-attachment periods, various transcripts related to the epithelial-mesenchymal transition (EMT) were found. In this study, RNA was extracted from different sets of days 17, 20, and 22 (day 0Zday of estrous) bovine conceptuses and subjected to real-time PCR analysis as well as Western blotting, from which abundances of N-cadherin (CDH2), vimentin, matrix metalloproteinase 2 (gelatinase A, 72 kDa gelatinase, 72 kDa type IV collagenase) (MMP2), and matrix metallopeptidase 9 (gelatinase B, 92 kDa gelatinase, 92 kDa type IV collagenase) (MMP9) mRNAs were determined on day 22, concurrent with (CDH1) mRNA and protein downregulation. Transcription factors in EMT processes were then analyzed and changes in snail homolog 2 (Drosophila) (SNAI), zinc finger E-box binding homeobox 1 (ZEB1), zinc finger E-box binding homeobox 2 (ZEB2), twist homolog 1 (Drosophila) (TWIST1), twist homolog 2 (Drosophila) (TWIST2), and Kruppel-like factor 8 (KLF8) transcripts were found in day 22 conceptuses, while confirming SNAI2 expression by Western blotting. Immunohistochemical analysis revealed that the day 22 trophectoderm expressed the mesenchymal markers N-cadherin and vimentin as well as the epithelial marker cytokeratin. In attempts to identify the molecular mechanisms by which the trophectoderm expressed EMT-related genes, growth factor receptors associated with EMT were analyzed. Upregulation of the growth factor receptor transcripts, fibroblast growth factor receptor 1 (FGFR1), platelet-derived growth factor receptor, alpha polypeptide (PDGFRA), platelet-derived growth factor receptor, beta polypeptide (PDGFRB), and transforming growth factor, beta receptor II (70/80 kDa) (TGFBR2) mRNAs, was found on day 22. The analysis was extended to determine the integrin (ITG) transcripts and found high levels of integrin, alpha 4 (antigen CD49D, alpha 4 subunit of VLA-4 receptor) (ITGA4), integrin, alpha 8 (ITGA8), integrin, beta 3 (platelet glycoprotein IIIa, antigen CD61) (ITGB3), and integrin, beta 5 (ITGB5) mRNAs on day 22. These observations indicate that after the conceptus-endometrium attachment, EMT-related transcripts as well as the epithelial marker cytokeratin were present in the bovine trophectoderm and suggest that the implantation process for noninvasive trophoblasts requires not only extracellular matrix expression but also partial EMT.

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Dynamic in vivo changes in the activities of gelatinases, matrix metalloproteinases (MMPs), and tissue inhibitor of metalloproteinases (TIMPs) in buffalo (Bubalus bubalis) uterine luminal fluid during estrous cycle and early pregnancy

Roy

Ghosh

2010

Molecular Reproduction Devel

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In ruminants, the phenomenon of endometrial tissue remodeling during the estrous cycle and early pregnancy is not fully understood. In this report, the occurrence of tissue remodeling, if any, in buffalo endometrium was studied by detecting gelatinases, matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs); the key regulators of tissue remodeling, in uterine luminal fluids (ULF) of cycling and early pregnant (approx. 43-65 days) buffaloes. Each stage of the estrous cycle and pregnant ULF demonstrated a unique profile of gelatinase activities compared to serum/follicular fluid, with a major gelatinase band of 60 kDa with highest activity in early-luteal stage. In addition to a 32 kDa uterus-specific gelatinase band detected in both non-pregnant and pregnant ULFs, the pregnant ULF displayed three new gelatinase bands of 86, 78, and 57 kDa. Western blot technique confirmed the presence of MMP-2 (54 kDa), MMP-9 (76/73 kDa), TIMP-1 (32 kDa), TIMP-2(20 kDa), and two molecular weight forms (31 and 22 kDa) of TIMP-3 in buffalo ULF with varying band intensities. Highest MMP-2 and MMP-9 activities were observed in follicular and early-luteal stage ULFs, respectively. Highest TIMP-1 activity was observed in early-luteal ULF. Interestingly, TIMP-2 activity was only detected in mid-luteal, late-luteal, and follicular stage ULFs with significantly increasing intensities. Highest activities of 31 and 22 kDa TIMP-3 were associated with late-luteal and early-luteal stage ULFs, respectively. The varied activities of MMPs and TIMPs in buffalo ULF during the estrous cycle and early pregnancy might be a reflection of dynamic structural remodeling of the endometrium and/or developing conceptus.

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Gelatinase (MMP-2 and -9) expression profiles during gestation in the bovine endometrium

Cited by 64 publications

References 48 publications

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

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

Expression of mesenchymal-related genes by the bovine trophectoderm following conceptus attachment to the endometrial epithelium

Dynamic in vivo changes in the activities of gelatinases, matrix metalloproteinases (MMPs), and tissue inhibitor of metalloproteinases (TIMPs) in buffalo (Bubalus bubalis) uterine luminal fluid during estrous cycle and early pregnancy

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