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Rat Amnion Type IV Collagen Composition and Metabolism: Implications for Membrane Breakdown¹

^a Center for Research on Reproduction and Women's Health and Departments of Obstetrics and Gynecology and ^b Pathology and Laboratory Medicine, University of Pennsylvania Medical Center, Philadelphia, Pennsylvania 19104 ^c Department of Medicine, Beth Israel Hospital and Harvard Medical School, Boston, Massachusetts 02215 ^d Bristol Heart Institute, Bristol Royal Infirmary, Bristol BS2 8HW, United Kingdom

We report here that rat amnion type IV collagens are composed primarily of 1(IV) and 2(IV) chains. Amnion basement membrane collagens were more sensitive to degradation by collagenases than were adult rat kidney basement membrane collagens, which are enriched in 3(IV), 4(IV), and 6(IV) chains. Amnion type IV collagen content per unit of protein was markedly reduced by Day 21 of pregnancy, the day of delivery. Increased amnion levels of matrix metalloproteinase (MMP)-2 and MMP-9, gelatinases that degrade type IV collagen, were found by Day 21, suggesting that collagen breakdown was responsible, in part, for the decline in amnion type IV collagen. Infection of organ cultures of Day 18 rat amnions with a recombinant adenovirus expressing MMP-9 (AdMMP-9) caused release of collagen fragments detected as hydroxyproline in the culture fluid, amnion cell detachment, and apoptosis. The AdMMP-9-induced apoptosis was prevented by the MMP inhibitor batimastat. These findings suggest that MMPs are implicated in anoikis and apoptotic death of amnion cells, and may be part of a complex program of fetal membrane remodeling that occurs before delivery.

¹ These studies were supported by NIH grant HD34612 (J.F.S.) and grants from the March of Dimes National Foundation (J.F.S.) and Medical Research Council of Great Britain (A.H.).

² Correspondence: Jerome F. Strauss, III, 778 Clinical Research Building, 415 Curie Boulevard, Philadelphia, PA 19104. FAX: 215 573 5408; jfs3{at}mail.med.upenn.edu

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