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Başlık: 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
Yazarlar: Dilly, Marc
Hambruch, Nina
Shenavai, Sima
Schüler, Gerhard
Froehlich, R.
Häeger, Jan Dirk
Pfarrer, Christiane D.
Uludağ Üniversitesi/Veterinerlik Fakültesi/Kadın Hastalıkları ve Doğum Anabilim Dalı.
0000-0003-4694-6937
Özalp, Gözde Rabia
AAE-3607-2019
23985710500
Anahtar kelimeler: Reproductive biology
Veterinary sciences
Animalia
Bos
Bovinae
Bovine placenta
Matrix metalloproteinases
Retained fetal membranes
Trophoblast giant-cells
Extracellular-matrix
Glucocorticoid-receptors
Progesterone-receptors
Integrin receptors
Sheep placenta
Mammary-gland
Uterine wall
Dairy-cattle
Yayın Tarihi: 1-Nis-2011
Yayıncı: Elsevier
Atıf: Dilly, M. vd. (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(6), 1104-1114.
Özet: 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.
URI: https://doi.org/10.1016/j.theriogenology.2010.11.019
https://www.sciencedirect.com/science/article/pii/S0093691X10005984
http://hdl.handle.net/11452/23269
ISSN: 0093-691X
1879-3231
Koleksiyonlarda Görünür:Scopus
Web of Science

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