Activity of 72-kDa and 92-kDa matrix metalloproteinases in placental tissues of cows with and without retained fetal membranes

J, Maj; Kankofer, Marta

doi:10.1016/s0143-4004(97)90010-2

Cited by 67 publications

(54 citation statements)

References 19 publications

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“…The results of flow cytometry show that CrTX significantly increased the cell population in the sub-G 0 and G 0 /G 1 phases, which indicates that the anti-tumor effects of CrTX were closely related to the Many studies have investigated the signaling pathways that are mediated by P38MAPK, which is one of the main signal transduction systems regulating apoptosis [9,10] . Cells transmit extracellular signals to the nucleus using P38MAPK [11] .…”

Section: Discussionmentioning

confidence: 99%

Anti-tumor activity of CrTX in human lung adenocarcinoma cell line A549

et al. 2011

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Aim: To assess the cytotoxic effect of crotoxin (CrTX), a potent neurotoxin extracted from the venom of the pit viper Crotalus durissus terrificus, in human lung adenocarcinoma A549 cells and investigated the underlying mechanisms. Methods: A549 cells were treated with gradient concentrations of CrTX, and the cell cycle and apoptosis were analyzed using a flow cytometric assay. The changes of cellular effectors p53, caspase-3 and cleaved caspase-3, total P38MAPK and pP38MAPK were investigated using Western blot assays. A549 xenograft model was used to examine the inhibition of CrTX on tumor growth in vivo. Results: Treatment of A549 cells with CrTX (25-200 μg/mL) for 48 h significantly inhibited the cell growth in a dose-dependent manner (IC 50 =78 μg/mL). Treatment with CrTX (25 μg/mL) for 24 h caused G1 arrest and induced cell apoptosis. CrTX (25 μg/mL) significantly increased the expression of wt p53, cleaved caspase-3 and phospho-P38MAPK. Pretreatment with the specific P38MAPK inhibitor SB203580 (5 μmol/L) significantly reduced CrTX-induced apoptosis and cleaved caspase-3 level, but G 1 arrest remained unchanged and highly expressed p53 sustained. Intraperitoneal injection of CrTX (10 μg/kg, twice a week for 4 weeks) significantly inhibited A549 tumor xenograft growth, and decreased MVD and VEGF levels. Conclusion: CrTX produced significant anti-tumor effects by inducing cell apoptosis probably due to activation of P38MAPK and caspase-3, and by cell cycle arrest mediated by increased wt p53 expression. In addition, CrTX displayed anti-angiogenic effects in vivo.

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Section: Discussionmentioning

confidence: 99%

Anti-tumor activity of CrTX in human lung adenocarcinoma cell line A549

et al. 2011

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“…Nevertheless, the physiological implications were yet inconclusive. 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.…”

Section: Discussionmentioning

confidence: 99%

“…About 500-mg pooled tissues were minced to ∼0.5-cm edge length and then homogenized on ice in 45-ml 0.1 M Tris-HCl buffer (pH 7.5) containing 0.1% Triton X-100 (Maj and Kankofer, 1997) with Ultra-Turrax IKA T10 (Module S10 N-10 G, IKA Corporation, Guangzhou, China) at 30 000 r.p.m. for 20 s. The homogenates were centrifuged by 200 × g for 30 min at 4°C (Kubota 5800, Kubota Corporation, Tokyo, Japan) to collect the clear supernatants and stored in aliquots under − 20°C until performing gelatin zymography within 1 week.…”

Section: Animalsmentioning

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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“…Matrix metalloproteinases (MMP) are enzymes capable of breaking down the ECM. MMP-2, MMP-9 and MMP-14 have been detected in the bovine placenta (Dilly et al, 2011;Maj and Kankofer, 1997;Walter and Boos, 2001) and are upregulated before parturition (Streyl et al, 2012). MMP's can be activated by many (inflammatory) cytokines (Hirata et al, 2003), including IL-1, IL-6 and TNF-α.…”

Section: Immune Assisted Loss Of Fetal-maternal Adherencementioning

confidence: 99%