KaydedilenlerDerginizi ekleyin

Dergiler / International Archives of Medical Research / 2026 / Volume: 8 Issue: 1

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

Elif Unsal
Yusuf Nergiz
Ercan Ayaz
Murat Akkus
Mehmet Sıddık Evsen
Sayfa
—
Yayın Tarihi
2016-06-15
DOI
—
🏛️Bu makalenin bibliyografik verileri ve tam metin bağlantısı DergiPark üzerinden sağlanmıştır.
DergiPark Kaydı ↗
✨

Yapay Zeka Hızlı Bakış & Çıkarımlar

AI Insight
⚡ TL;DR(1 Cümlede Hızlı Çıkarım)

Conclusion: Regarding our findings, MMP-9 plays a more active role than MMP-2 in gestational diabetic placentas was concluded.

📌 3 Maddede Bu Makale

🎯
Amaç & Hipotez: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.
📊
Temel Bulgular & Veri: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.
💡
Sonuç & Katkı:Conclusion: Regarding our findings, MMP-9 plays a more active role than MMP-2 in gestational diabetic placentas was concluded.
🔬Tür:Research Article
📍Kapsam:Genişletilmiş Akademik Örneklem
⚙️Değişkenler:Full-term human placenta · gestational diabetes mellitus · MMP-2

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.

🔖

Bu Makaleye Atıf Yap

Unsal, E., Nergiz, Y., Ayaz, E., Akkus, M., Evsen, M. S. (2016). Immunolocalization of MMP-2 and MMP-9 in Placenta of Humans with Gestational Diabetes Mellitus. International Archives of Medical Research, Volume: 8 Issue: 1. https://ajindex.com/articles/1493227

📄 Tam Metin PDF Okuyucu

📄

PDF görüntüleyici hazırlanıyor...

Kaynakça (23)

  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
  23. 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.