Immunolocalization of MMP-2 and MMP-9 in Placenta of Humans with Gestational Diabetes Mellitus

Year 2016, Volume: 8 Issue: 1, 12 - 19, 15.06.2016

Elif Unsal Yusuf Nergiz Ercan Ayaz Murat Akkus Mehmet Sıddık Evsen

Abstract

Background: The aim of this study was to compare of term placentas, which has gestational
diabetes mellitus and normal pregnant women in terms of immunolocalization of MMP-2 and
MMP-9.
Methods: Fifteen gestational diabetes mellitus patients and fifteen women without any systemic
disease of the placenta were collected. Fetal and maternal faces of the placentas, as well as
peripheral and central parts were examined for immunohistochemical investigation of MMP-2 and
MMP-9.Groups were evaluated through use of the SPSS 15.0 package program. P values ≤0.05
were considered statistically significant.
Results: MMP-2 reaction was weakly expressed in maternal and fetal surface, and no significant
difference between the two groups was observed. When MMP-9 expression was compared between
the groups, an increase in decidual cells of diabetic group and a decrease in syncytial nodes were
noticed. In fetal surface, a decrease in expression level was detected in chorionic villus
syncytiotrophoblasts, chorionic villus stroma, stem villus syncytiotrophoblasts, stem villous stroma
and chorionic plate.
Conclusion: Regarding our findings, MMP-9 plays a more active role than MMP-2 in gestational
diabetic placentas was concluded.

Keywords

Full-term human placenta, gestational diabetes mellitus, MMP-2

References

• 1. Jawerbaum A, Gonzalez E. Diabetic Pregnancies: The Challenge of Developing in a Pro Inflammatory Environment. Current Medicinal Chemistry 2006;2127-2138
• 2. Gerçek E, Şen H. Gestasyonel Diyabetes Mellitus Yönetimi: Öz-etkililik ve Perinatal Sonuçlar. J Cur Pediatrics 2015; 13(3):0-0
• 3. Leach L, Taylor A, Sciota F. Vascular dysfunction in the diabetic placenta: Causes and consequences. J. Anat 2009; 215, 69–76
• 4. Huppertz B, Kertschanska S, Demir A, Frank H, KaufmannP. Immunohistochemistry of matrix metalloproteinases (MMP), their substrates, and their inhibitors (TIMP) during trophoblast invasion in the human placenta. Cell Tissue Res 1998; 291, 133–148
• 5. Verma R, Mishra S, Kaul J. Cellular Changes in the Placenta in Pregnancies Jawerbaum Complicated with Diabetes. Int. J. Morphol 2010; 28, 259–64
• 6. Gheorman L, Pleşea I. E, Gheorman V. Histopathological considerations of placenta in pregnancy with diabetes. Rom. J. Morphol. Embryol 2012; 53, 329–336
• 7. Pustovrh C, Jawerbaum A . Membrane-type matrix metalloproteinase-9 activity in placental tissue from patients with pre-existing and gestational diabetes mellitus. Reprod Fertil Dev 2000; 12, 269–75.
• 8. Demir-Weusten A. Y, et al. Matrix metalloproteinases-2, -3 and -9 in human term placenta. Acta Histochem 2007;109, 403–412
• 9. Cohen M, Meisser A, Bischof P. Metalloproteinases and Human Placental Invasiveness. Placenta 2006; 27, 783–793
• 10. Pustovrh, M. C. et al. MMP/TIMP balance is modulated in vitro by 15dPGJ2 in fetuses and placentas from diabetic rats. Eur. J. Clin. Invest 2009; 39, 1082–1090
• 11. Sulik A, Chyczewski L. Immunohistochemical analysis of MMP-9, MMP-2 and TIMP-1, TIMP-2 expression in the central nervous system following infection with viral and bacterial meningitis. Folia Histochem. Cytobiol. 2008; 46, 437–442
• 12. Pathmaperuma A. N, et al. Fatty acids alter glycerolipid metabolism and induce lipid droplet formation, syncytialisation and cytokine production in human trophoblasts with minimal glucose effect or interaction. Placenta 2010; 31, 230–239
• 13. Jones CJ, Desoye G. Glycogen distribution in the capillaries of the placental villus in normal, overt and gestational diabetic pregnancy. Placenta 1993; 14, 505–517
• 14. Stojanovic N. et al. Serum levels of matrix metalloproteinases MMP-2 and MMP-9 and their inhibitors in women with glucose intolerance in pregnancy and normal controls. Gynecol Endocrinol 2010; 26, 201– 207
• 15. Sağlam A, Ünlü B, Mungan T. Matriks Metalloproteinaz-9 Ekspresyonunun Preterm Prematür Membran Rüptürü ile İ li ş kisinin İ ncelenmesi. Türkiye Klin. J. Gynecolo Obs. 2006; 16, 229–33
• 16. Vegh G L, et al. Matrix metalloproteinases and their inhibitors in gestational trophoblastic diseases and normal placenta. Gynecol. Oncol 1999; 75, 248–253
• 17. Xu P, Alfaidy N. Expression of Matrix Metalloproteinase ( MMP ) -2 and MMP-9 in Human Placenta and Fetal Membranes in Relation to Preterm and Term Labor. Clin. Endocrinol 2002; (Oxf).87, 1353– 1361
• 18. Shokry M, Omran OM, Hassan H. I, Elsedfy G O, Hussein M R A. Expression of matrix metalloproteinases 2 and 9 in human trophoblasts of normal and preeclamptic placentas: Preliminary findings. Exp. Mol. Pathol 2009; 87, 219–225.
• 19. Pustovrh M. C, et al. Increased matrix metalloproteinases 2 and 9 in placenta of diabetic rats at midgestation. Placenta 2005; 26, 339–348
• 20. Mauro A, Buscemi M, Gerbino A. Immunohistochemical and transcriptional expression of matrix metalloproteinases in full-term human umbilical cord and human umbilical vein endothelial cells. J. Mol. Histol 2010; 41, 367–377
• 21. Nissi R. et al. Circulating matrix metalloproteinase MMP-9 and MMP-2/TIMP-2 complex are associated with spontaneous early pregnancy failure. Reprod. Biol. Endocrinol 2013;11, 2
• 22. Ries, C. & Petrides, P. E. Cytokine regulation of matrix metalloproteinase activity and its regulation in disease. Biol. Chem 1995; 345–55