1. 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
- Author
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R. Froehlich, Sima Shenavai, Gerhard Schuler, Christiane Pfarrer, G.R. Özalp, J.-D. Haeger, Nina Hambruch, Marc Dilly, Uludağ Üniversitesi/Veterinerlik Fakültesi/Kadın Hastalıkları ve Doğum Anabilim Dalı., Özalp, Gözde Rabia, and AAE-3607-2019
- Subjects
Veterinary sciences ,Sheep placenta ,Uterine wall ,Animal disase ,Physiology ,Placenta ,Extraembryonic Membranes ,Embryo membrane ,Matrix metalloproteinase ,Glucocorticoid-receptors ,Western blotting ,Extracellular matrix ,Food Animals ,Retained placenta ,Pregnancy ,Integrin receptors ,Tissue inhibitor of metalloproteinase 2 ,Bos ,Progesterone-receptors ,Small Animals ,Endometritis ,Retained Placenta ,Dairy Cows ,Gelatinase A ,Messenger RNA ,Reproduction ,medicine.anatomical_structure ,Bovine placenta ,Extracellular-matrix ,embryonic structures ,Matrix Metalloproteinase 2 ,Female ,medicine.medical_specialty ,Blotting, Western ,Reproductive biology ,Cattle Diseases ,Placental Retention ,Biology ,Bovinae ,Article ,Andrology ,Internal medicine ,Matrix Metalloproteinase 14 ,medicine ,Animalia ,Animals ,Zymography ,RNA, Messenger ,Dairy-cattle ,Retained fetal membranes ,Tissue Inhibitor of Metalloproteinase-2 ,Fetus ,Animal ,Equine ,Trophoblast ,Placentation ,Matrix metalloproteinases ,Metabolism ,Endocrinology ,Enzymology ,Cattle disease ,Cattle ,Animal Science and Zoology ,Mammary-gland ,Trophoblast giant-cells ,Placenta, Retained - Abstract
Matrix metalloproteinases (MMPs) and counteracting tissue inhibitors of metalloproteinases (TIMPs) are balancing extracellular matrix (ECM) formation and degradation. The latter is believed to be an important aspect for the detachment of fetal membranes postpartum when loosening the feto-matemal connection which is a prerequisite to avoid placental retention a common disease in cows leading to considerable economic loss. Membrane-type (MT) MMPs have been suggested as potential activators controlling ECM remodelling. In particular, MT1-MMP (MMP-14) is able to degrade ECM substrates and activate MMP-2 through binding TIMP-2 at the cell surface. Since the connection between the trophoblast and the maternal caruncular epithelium is supported by integrin receptors bound to ECM, we hypothesize that impaired modulation of the ECM by TIMPs/MMPs participates in the aetiology of bovine retained fetal membranes. To analyse this involvement, placentomes were collected from cows after term parturition and timely release of fetal membranes (n = 4) and cows with retained fetal membranes after various treatments for the induction of parturition using progesterone antagonist (aglepristone), PGF(2 alpha) analogue, glucocorticoid, and after elective caesarean sections (each group n = 3). The expression of MMP-14, MMP-2 and of TEMP-2 was examined by real-time-PCR, irnmunohistochemistry, Western blot and zymography. The relative mRNA expression levels of MMP-14 remained unchanged, while the expression levels of TIMP-2 and MMP-2 partly increased in animals with induced parturition and retention of fetal membranes compared to animals without placental retention. MMP-14 protein was expressed in cells of the uninucleated trophoblast, the fetal mesenchyme and maternal stoma. TIMP-2 was present exclusively in trophoblast giant cells, while MMP-2 could be detected in uninucleated trophoblast cells and the fetal mesenchyme. The presence of the activated enzyme was confirmed by zymography. In conclusion, MMP-14, MMP-2 and TIMP-2 are co-localized in the fetal compartment and therefore could influence the timely release of fetal membranes in cattle. (c) 2011 Elsevier Inc. All rights reserved.
- Published
- 2011
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