Matrix Metalloproteinase-1 and -9 in Human Placenta during Spontaneous Vaginal Delivery and Caesarean Sectioning in Preterm Pregnancy

Sundrani, Deepali; Chavan‐Gautam, Preeti; Pisal, Hemlata; Mehendale, Savita; Joshi, Sadhana

doi:10.1371/journal.pone.0029855

Cited by 42 publications

(34 citation statements)

References 39 publications

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“…This is consistent with our earlier study where we have reported a negative association between placental MMP9 levels and DHA levels in the whole cohort (Sundrani et al 2012). It is suggested that reduced omega 3 fatty acids may up regulate two-series prostaglandin release thereby increasing the levels of MMPs.…”

Section: Discussionsupporting

confidence: 93%

“…Considering both mode of deliveries, there were 68 women in term labor and 66 women in preterm labor. The inclusion and exclusion criteria were the same as reported in our earlier study (Sundrani et al 2012).…”

Section: Subjectsmentioning

confidence: 99%

“…Fresh placental tissues were obtained from normal and preterm pregnancies, immediately after delivery, processed, and stored until assayed as described by us earlier (Sundrani et al 2012).…”

Section: Tissue Collection and Processingmentioning

confidence: 99%

“…Placental tissue lysates were prepared as described by us earlier (Sundrani et al 2012). MMP2, MMP3, TIMP1, and TIMP2 levels were measured from placental tissue lysates using commercial ELISA kits (Abnova, Taipei, Taiwan for MMP2, MMP3, and TIMP2; Abcam, Inc., Cambridge, MA, USA for TIMP1).…”

Section: Mmp and Timp Levels From Placental Tissue Lysatesmentioning

confidence: 99%

“…We have recently reported increased placental levels of MMP1 (collagenase) and MMP9 (gelatinase) in women delivering preterm (Sundrani et al 2012). The activity of MMPs is reported to be regulated by homocysteine, oxidative stress, and long-chain polyunsaturated fatty acids (LCPUFA; Guo et al 2006, Kundu et al 2009, Solakivi et al 2009, Zainal et al 2009, Zeydanli & Turan 2009, Ke et al 2010.…”

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinases-2, -3 and tissue inhibitors of metalloproteinases-1, -2 in placentas from preterm pregnancies and their association with one-carbon metabolites

Sundrani¹,

Chavan‐Gautam²,

Pisal³

et al. 2013

Reproduction

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Maternal nutrition is an important determinant of one-carbon metabolism and defects in the one-carbon metabolism may lead to poor obstetric outcomes. This study was designed to test the hypothesis that altered intake/metabolism of micronutrients (folic acid and vitamin B 12 ) and docosahexaenoic acid (DHA) contributes to increased homocysteine and oxidative stress leading to altered levels of matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) in women delivering preterm. We have earlier reported increased vitamin B 12 , homocysteine, and oxidative stress along with reduced placental DHA in women delivering preterm. In this study, we further examine the placental levels of MMP2, MMP3, TIMP1, and TIMP2 in 75 women delivering at term and 73 women delivering preterm. Placental levels of MMPs and TIMPs were determined by ELISA. Placental MMP2 and MMP3 levels were higher (P!0.01) in women delivering preterm as compared with term. There was no difference in the placental TIMP1 and TIMP2 levels in women delivering preterm and at term. Further placental MMP2 and MMP3 levels were higher (P!0.01) in women with preterm labor as compared with those in labor at term, suggesting that MMPs may favor degradation of extracellular matrix in the placenta during preterm labor. Our study for the first time suggests a crucial role of micronutrients and MMPs in preterm birth. Future studies need to examine if epigenetic modifications through the one-carbon cycle contribute to increased levels of MMPs leading to preterm deliveries.

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Section: Discussionsupporting

confidence: 93%

Section: Subjectsmentioning

confidence: 99%

Section: Tissue Collection and Processingmentioning

confidence: 99%

Section: Mmp and Timp Levels From Placental Tissue Lysatesmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Matrix metalloproteinases-2, -3 and tissue inhibitors of metalloproteinases-1, -2 in placentas from preterm pregnancies and their association with one-carbon metabolites

Sundrani¹,

Chavan‐Gautam²,

Pisal³

et al. 2013

Reproduction

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Genesis of placental sequestration in malaria and possible targets for drugs for placental malaria

Clark

2019

Birth Defects Research

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Malaria during pregnancy results in intrauterine growth restriction, fetal anemia, and infant mortality. Women are more susceptible to malaria during pregnancy due to malaria-induced inflammation and the sequestration of infected red blood cells in the placenta, which bind to the chondroitin sulfate portion of syndecan-1 on the syncytiotrophoblast and in the intervillous space. Syndecan-1 is a dimeric proteoglycan with an extracellular ectodomain that is cleaved from the transmembrane domain (referred to as "shedding") by matrix metalloproteinases (MMPs), likely the secreted MMP-9. The ectodomain includes four binding sites for chondroitin sulfate, which are proximal to the transmembrane domain, and six distal binding sites primarily for heparan sulfate. This "shedding" of syndecan-1 is inhibited by the presence of the heparan sulfate chains, which can be removed by heparanase. The intervillous space contains fibrin strands and syndecan-1 ectodomains free of heparan sulfate. The following is proposed as the sequence of events that leads to and is primarily responsible for sequestration in the intervillous space of the placenta. Inflammation associated with malaria triggers increased heparanase activity that degrades the heparan sulfate on the membrane-bound syndecan-1. Inflammation also upregulates MMP-9 and the removal of heparan sulfate gives MMP-9 access to cleave syndecan-1, thereby releasing dimeric syndecan-1 ectodomains with at least four chondroitin sulfate chains attached. These multivalent ectodomains bind infected RBCs together leading to their aggregation and entrapment in intervillous fibrin. This mechanism suggests possible new targets for anti-placental malaria drugs such as the inhibition of MMP-9. Doxycycline is an antimalarial drug which inhibits MMP-9. K E Y W O R D Sfibrin, heparanase, malaria, metalloproteinase, placenta, sequestration, syndecan-1

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Investigating the expression of MMPs and TIMPs in preterm placenta and role of CpG methylation in regulating MMP‐9 expression

Sundrani

Narang

Mehendale³

et al. 2017

IUBMB Life

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Matrix metalloproteinases (MMPs) and tissue inhibitors of MMPs (TIMPs) are crucial to the processes of normal labor and parturition. We have previously reported aberrant protein levels of MMPs in placenta of women delivering preterm as compared to term. In this study, we examine the mRNA levels of MMPs (MMP-1, MMP-2, and MMP-9) and TIMPs (TIMP-1, TIMP-2) in the placenta from women delivering preterm as compared with term and further study the promoter DNA methylation of the MMP-9 gene in a sub-sample of term and preterm placentae. A total of 110 women were included in the study; 56 delivered term and 54 delivered preterm. MMP and TIMP mRNA levels were determined by Taqman-based qPCR. Promoter CpG methylation of MMP-9 gene was studied on a subset of 10 term and 8 preterm placenta using Epitect Methyl-II PCR assay kit. The mRNA levels of MMP-1,-2 were higher and those of TIMP-1,-2 were lower in the placentae of women delivering preterm. MMP-9 levels were comparable between the two groups. Among women undergoing spontaneous vaginal deliveries, higher mRNA levels of MMP-1, -2 and -9 were seen in the placentae of those delivering preterm as compared to term. Similar results were seen in women undergoing preterm labor as compared to term. MMP-9 gene promoter was hypomethylated in preterm placenta as compared to term placenta, while the mRNA levels were comparable between the two groups. The observed imbalance between MMP and TIMP expression may have prematurely triggered the signaling cascade leading to preterm birth. © 2017 IUBMB Life, 69(12):985-993, 2017.

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Matrix Metalloproteinase-1 and -9 in Human Placenta during Spontaneous Vaginal Delivery and Caesarean Sectioning in Preterm Pregnancy

Cited by 42 publications

References 39 publications

Matrix metalloproteinases-2, -3 and tissue inhibitors of metalloproteinases-1, -2 in placentas from preterm pregnancies and their association with one-carbon metabolites

Matrix metalloproteinases-2, -3 and tissue inhibitors of metalloproteinases-1, -2 in placentas from preterm pregnancies and their association with one-carbon metabolites

Genesis of placental sequestration in malaria and possible targets for drugs for placental malaria

Investigating the expression of MMPs and TIMPs in preterm placenta and role of CpG methylation in regulating MMP‐9 expression

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