Premium
Status of MMP 9 and TIMP 1 in Pregnant women with Preeclampsia in Indian Population
Author(s) -
ARORA PALLAVI,
MOCHAN SANKAT,
GUPTA SUNIL KUMAR,
SAXENA SHOBHIT,
RANI NEERJA,
PALLAVI SK,
SHARMA ARUNDHATI,
LUTHRA KALPANA,
DWIVEDI SADANAND,
BHATLA NEERJA,
DHINGRA RENU
Publication year - 2019
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2019.33.1_supplement.774.28
Subject(s) - preeclampsia , matrix metalloproteinase , western blot , andrology , immunohistochemistry , medicine , zymography , timp1 , population , spiral artery , placenta , messenger rna , metalloproteinase , endocrinology , biology , gene expression , pregnancy , fetus , gene , biochemistry , genetics , environmental health
Matrix metalloproteinases (MMPs) specifically MMP 9 is a key regulator of vascular and uterine spiral artery remodelling and its activity is controlled at multiple levels, including gene transcription, activation of its latent forms and endogenous inhibition by tissue inhibitors of metalloproteinases [TIMPs (specifically TIMP 1)]. Alteration in MMP 9 and TIMP 1 expression may contribute to uterine and vascular dysfunction leading to adverse pregnancy outcomes such as Preeclampsia (PE) and FGR. Therefore, in the present study, we sought to analyse the levels of this enzyme (MMP 9) and its regulator (TIMP 1) in the patients of PE. Methods The blood samples from the enrolled pregnant women [Total: 60, Preeclamptic: 30, Normotensive, Non‐proteinuric (Controls): 30)] were used for determining the mRNA expression of MMP 9 and TIMP 1 using qRT‐PCR. The sera of the above subjects were used for measuring MMP 9 and TIMP 1 protein levels using commercially available ELISA kits (R and D system). However, 30 caesarean delivered placentae (15 PE and 15 normotensive) were used to analyse the mRNA expression of MMP 9 and TIMP 1 using qRT‐PCR. Also, the MMP 9 and TIMP1 protein expression was seen by immunohistochemistry (IHC) and immunofluorescence (IF) staining. Zymography was performed for MMP 9 characterization and TIMP 1 expression was evaluated using western blot in these placentae. Results MMP 9 mRNA expression reduced in both plasma (2.66 folds) and placentae (6.66 folds) of PE patients as compared to controls. However, TIMP 1 mRNA expression was elevated in both plasma (2.23 folds) and placentae (8.32 folds) of PE patients as compared to controls. ELISA results demonstrated decrease in MMP 9 (p=0.0526; Wilcoxon matched‐pairs signed rank test) and increase in TIMP 1 (p=0.9133; Wilcoxon matched‐pairs signed rank test) protein levels in PE patients as compared to healthy controls. Immunolocalisation revealed stronger expression of MMP 9 in placental syncytiotrophoblasts and stroma in control placentae as compared to PE placentae. However, TIMP 1 intensity reduced in placental villi and decidual cells in the placentae from normotensive non‐proteinuric pregnant women. MMP 9 activity (zymography) was also found to be less and TIMP‐1 (western blot) upregulated in PE placentae as compared to control placentae. Conclusion Understanding the role of MMP 9 and TIMP 1 in uteroplacental and vascular remodelling and function could help design new approaches for prediction and management of preeclampsia. Ethical Clearance: Ref. No. IECPG‐101/21.03.2018 Support or Funding Information F.No.IR‐516/2018/RS This abstract is from the Experimental Biology 2019 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .