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

Dilly, Marc; Hambruch, Nina; Shenavai, Sima; Schuler, Gerhard; Froehlich, Rosemary J.; Haeger, J.-D.; Özalp, G. R.; Pfarrer, C.

doi:10.1016/j.theriogenology.2010.11.019

Cited by 33 publications

(28 citation statements)

References 61 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%

“…Takagi et al (2007) manually collected bovine placentomes from the uterus via the vagina postpartum. In the study by Dilly et al (2011), cow placentomes were collected through cesarean section, and high expression of MMP-2 was found in the fetal compartment,concluding a role of MMP-2 in the timely release of fetal membranes in cattle. Their ways of placentome collection were different from ours.…”

Section: Discussionmentioning

confidence: 98%

“…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%

“…They further implied that lower MMP-9 expression might be favorable for the timely release of term placenta. Dilly et al (2011) reported that placentomes collected from cows with or without RFM expressed predominantly proMMP-2 but only small amounts of active MMP-2. The balancing between MMP and TIMP is apparently an important aspect that warrants extensive exploration.…”

Section: Discussionmentioning

confidence: 99%

“…Although hormonal change and prostaglandins might play an important role, the underlying mechanisms involved in RFM are barely understood. The proteolytic enzymes specifically degrading the extracellular matrix (ECM) components of the placenta are known to participate in this process (Dilly et al, 2011).…”

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: 98%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

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 plasminogen activator system in the ovine placentome during late gestation and stage‐two of parturition

McNeel

Cushman

Vallet

2013

Molecular Reproduction Devel

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The process of placental separation is not completely understood. In domestic animals, especially cattle, it is important that expulsion of the fetal membranes takes place in a timely manner in order to achieve maximal reproductive efficiency. The activity of the matrix-metalloprotease (MMP) family of proteases is known to be reduced in placentomes from cases of retained placenta. Members of the MMP family are known to be activated by the plasminogen activator (PA) family of proteases. We hypothesized that the expression and activity of the PA family increase in the cotyledon and/or caruncle as parturition approaches, with maximal expression and activity at parturition. To test this hypothesis, we performed reverse-transcriptase quantitative PCR and plasminogen-casein zymography to detect the presence and activity of PA family members in the placentome leading up to and during parturition in spontaneous and dexamethasone-induced parturient ewes. The results from our experiments indicated that serine proteases inhibitor E1 (SERPINE1) mRNA abundance in the cotyledon was different between treatment groups (P = 0.0002). In the caruncle, gene expression for plasminogen activator urokinase-type (PLAU) was different (P = 0.0154), and there was a strong trend for differences in SERPINE1 expression (P = 0.0565). These results demonstrate that expression of the PA system in the placentome changes from late pregnancy to parturition, and the presence or activity of these enzymes may occur after fetal expulsion.

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Roles and regulation of the matrix metalloproteinase system in parturition

Geng

Huang

Jiang

2016

Molecular Reproduction Devel

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SUMMARYSignificant tissue destruction, repair, and remodeling are involved in parturition, which involves fetal membrane rupture, cervical ripening, and uterine contraction and its subsequent involution. Extracellular matrix degradation and remodeling by proteolytic enzymes, such as matrix metalloproteinases (MMPs), are required for the final steps of parturition. MMPs participate in physiological degradation and remodeling through their proteolytic activities on specific substrates, and are balanced by the action of their inhibitors. Disruption to this balance can result in pathological stress that ends with preterm or post-term birth or pre-eclampsia. In this review, we examine the roles and regulation of the MMP system in physiological and pathological labor, and propose a model that illustrates the mechanisms by which the MMP system contributes to these processes.Mol. Reprod. Dev. 83: 276À286,

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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

Cited by 33 publications

References 61 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

The plasminogen activator system in the ovine placentome during late gestation and stage‐two of parturition

Roles and regulation of the matrix metalloproteinase system in parturition

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