Acta histochemica 109 (2007) 403—412 Matrix metalloproteinases-2, -3 and -9 in human term placenta Ays - e Yasemin Demir-Weusten a , Yasemin Seval b , Peter Kaufmann c , Ramazan Demir b,Ã , Gultekin Yucel d , Berthold Huppertz e a Department of Clinical Biochemistry, Medical Faculty of Utrecht University, Utrecht, The Netherlands b Department of Histology and Embryology, Faculty of Medicine, Akdeniz University, 07070 Antalya, Turkey c Department of Anatomy II, University Hospital RWTH, Aachen, Germany d Department of Biochemistry, Faculty of Medicine, Akdeniz Universtiy, Antalya, Turkey e Institute of Cell Biology, Histology and Embryology, Medical University of Graz, Austria Received 24 January 2007; received in revised form 3 April 2007; accepted 4 April 2007 KEYWORDS Human term placenta; Matrix metallo- proteinases; Immuno- histochemistry; Zymography Summary Matrix metalloproteinases (MMPs) are zinc-dependent enzymes that degrade the components of the extracellular matrix (ECM) and are known to be the main mediators of human placentation and parturition. Although there are many studies on the roles and distribution of MMPs in human term placenta, so far none of the studies has investigated the distribution of MMP-2, -3 and -9 in different cells of various placental sites. In this study, we aimed to determine the distribution and enzymatic activities of MMP-2, -3 and -9 with regard to different regions of term human placenta, such as amnion, basal plate, chorionic plate, decidua, chorion laeve, Nitabuch’s stria, umbilical cord and placental villi. Eighteen normal human term placentas were obtained after vaginal deliveries. Immunohistochemistry and zymography were performed for MMP-2, -3 and -9 on placental tissue sections and protein extracts, respectively. Nearly all tissues showed immunoreactivity for MMPs. The strongest enzymatic activity for MMP-2 was seen in areas where invasive trophoblast cells invaded maternal tissues. MMP-9 had the highest enzymatic activity at the contact region of fetal and maternal parts, suggesting the importance of MMP-9 in separation of the placenta from the uterine wall during labor. MMP-3 had a similar localization to MMP-9, suggesting that besides gelatinases like MMP-2 and -9, MMP-3 (stromelysin-1) may also have important roles during labor. This study describes the site-specific distribution and activities of MMPs and therefore might help in elucidating the molecular mechanisms in pathologies such as premature rupture of membranes. & 2007 Elsevier GmbH. All rights reserved. ARTICLE IN PRESS www.elsevier.de/acthis 0065-1281/$ - see front matter & 2007 Elsevier GmbH. All rights reserved. doi:10.1016/j.acthis.2007.04.001 Ã Corresponding author. Tel./fax: +90 2422274486. E-mail address: rdemir@akdeniz.edu.tr (R. Demir).