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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.
Theriogenology 2011; 75(6):1104-14T

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-maternal 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(2α) analogue, glucocorticoid, and after elective caesarean sections (each group n = 3). The expression of MMP-14, MMP-2 and of TIMP-2 was examined by real-time-PCR, immunohistochemistry, 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 stroma. 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.

Authors+Show Affiliations

Department of Anatomy, University of Veterinary Medicine Hannover, Hannover, Germany.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

21247626

Citation

Dilly, M, et al. "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, vol. 75, no. 6, 2011, pp. 1104-14.
Dilly M, Hambruch N, Shenavai S, et al. 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. 2011;75(6):1104-14.
Dilly, M., Hambruch, N., Shenavai, S., Schuler, G., Froehlich, R., Haeger, J. D., ... Pfarrer, C. (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), pp. 1104-14. doi:10.1016/j.theriogenology.2010.11.019.
Dilly M, et al. 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. 2011 Apr 1;75(6):1104-14. PubMed PMID: 21247626.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 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. AU - Dilly,M, AU - Hambruch,N, AU - Shenavai,S, AU - Schuler,G, AU - Froehlich,R, AU - Haeger,J-D, AU - Ozalp,G R, AU - Pfarrer,C, Y1 - 2011/01/17/ PY - 2010/09/15/received PY - 2010/11/09/revised PY - 2010/11/10/accepted PY - 2011/1/21/entrez PY - 2011/1/21/pubmed PY - 2011/7/1/medline SP - 1104 EP - 14 JF - Theriogenology JO - Theriogenology VL - 75 IS - 6 N2 - 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-maternal 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(2α) analogue, glucocorticoid, and after elective caesarean sections (each group n = 3). The expression of MMP-14, MMP-2 and of TIMP-2 was examined by real-time-PCR, immunohistochemistry, 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 stroma. 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. SN - 1879-3231 UR - https://www.unboundmedicine.com/medline/citation/21247626/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_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0093-691X(10)00598-4 DB - PRIME DP - Unbound Medicine ER -