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

Autor: R. Froehlich, Sima Shenavai, Gerhard Schuler, Christiane Pfarrer, G.R. Özalp, J.-D. Haeger, Nina Hambruch, Marc Dilly
Přispěvatelé: Uludağ Üniversitesi/Veterinerlik Fakültesi/Kadın Hastalıkları ve Doğum Anabilim Dalı., Özalp, Gözde Rabia, AAE-3607-2019
Rok vydání: 2011
Předmět:
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
Zdroj: Theriogenology. 75:1104-1114
ISSN: 0093-691X
DOI: 10.1016/j.theriogenology.2010.11.019
Popis: 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.
Databáze: OpenAIRE
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