Changes in Matrix Metalloproteinase (MMP)-2 and MMP-9 in the Fetal Amnion and Chorion During Gestation and at Term and Preterm Labor
Yonemoto, H and Young, C. B and Ross, J. T and Guilbert, L. L and Fairclough, R. J and Olson, D. M (2006) Changes in Matrix Metalloproteinase (MMP)-2 and MMP-9 in the Fetal Amnion and Chorion During Gestation and at Term and Preterm Labor. Placenta, 27 (6-7). pp. 669-677. ISSN 0143-4004Full text for this resource is not available from the Research Repository.
Increased matrix metalloproteinase (MMP)-9 proteolytic activity is associated with term birth, preterm birth and premature rupture of membranes. However, most studies show no changes with MMP-2, which binds tightly to cell and matrix proteins. We hypothesized better protein extraction would reveal new MMP patterns. Human amnion and chorion were collected from 25 patients at preterm or term, extracted with 2% SDS (a high concentration), and the MMP protein levels and pro-enzyme activities were determined by Western immunoblotting and zymography. MMP-2 protein and MMP-2 and -9 pro-enzyme activities in the amnion increased significantly (p<0.05) with labor at term, and were higher than at preterm labor (p<0.05), when extracted with high SDS concentration. There were no changes in chorion MMPs under any condition. These associations suggest MMP-2 may be another regulator of membrane rupture and other labor-associated mechanisms at term parturition, and its role(s) should be examined further.
|Uncontrolled Keywords:||ResPubID19281, matrix metalloproteinases, MMP-2; MMP-9, amnion, chorion, gestation, preterm labor, term labor|
|Subjects:||FOR Classification > 1114 Paediatrics and Reproductive Medicine
FOR Classification > 1101 Medical Biochemistry and Metabolomics
Faculty/School/Research Centre/Department > School of Biomedical and Health Sciences
|Date Deposited:||03 May 2012 05:20|
|Last Modified:||12 Dec 2014 02:55|
|ePrint Statistics:||View download statistics for this item|
|Citations in Scopus:||24 - View on Scopus|
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