Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/123735
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Type: Journal article
Title: Changes in matrix metalloproteinase (MMP)-2 and MMP-9 in the fetal amnion and chorion during gestation and at term and preterm labor
Author: Yonemoto, H.
Young, C.
Ross, J.
Guilbert, L.
Fairclough, R.
Olson, D.
Citation: Placenta, 2006; 27(6-7):669-677
Publisher: Elsevier
Issue Date: 2006
ISSN: 0143-4004
1532-3102
Statement of
Responsibility: 
H. Yonemotoa,b, C. B. Youngb,c, J. T. Rossb,c, L. L. Guilbertb,d, R. J. Faircloughe and D. M. Olson
Abstract: 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.
Keywords: Matrix metalloproteinases; MMP-2; MMP-9; Amnion; Chorion; Gestation; Preterm labor; Term labor
Rights: © 2005 Elsevier Ltd. All rights reserved.
RMID: 0030081849
DOI: 10.1016/j.placenta.2005.05.014
Appears in Collections:Public Health publications

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