What is the role of matrix metalloproteinase-2 in placenta percreta?

Aim This study compared the placental expression of the matrix metalloproteinase‐2 (MMP‐2) enzyme, which is thought to play a key role in the penetration of trophoblastic cells, in third‐trimester placenta percreta (PP) patients with that of women with normal pregnancies. Methods Twenty‐five pregnan...

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Veröffentlicht in:The journal of obstetrics and gynaecology research 2015-07, Vol.41 (7), p.1018-1022
Hauptverfasser: Kocarslan, Sezen, Incebıyık, Adnan, Guldur, Muhammet Emin, Ekinci, Turan, Ozardali, Hasan Ilyas
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container_issue 7
container_start_page 1018
container_title The journal of obstetrics and gynaecology research
container_volume 41
creator Kocarslan, Sezen
Incebıyık, Adnan
Guldur, Muhammet Emin
Ekinci, Turan
Ozardali, Hasan Ilyas
description Aim This study compared the placental expression of the matrix metalloproteinase‐2 (MMP‐2) enzyme, which is thought to play a key role in the penetration of trophoblastic cells, in third‐trimester placenta percreta (PP) patients with that of women with normal pregnancies. Methods Twenty‐five pregnant subjects who underwent cesarean section due to PP and 25 term pregnant subjects who underwent cesarean section for obstetric reasons were included in the study. Demographic data, pathology reports, and histopathological samples were examined. Blocks containing samples of placenta underwent immunohistochemical analysis using the MMP‐2 antibody. Immunohistochemical expression of placental samples obtained from both groups was examined and compared. Results There were no statistically significant differences in the demographic data (P > 0.05). With regard to immunohistochemistry, cytoplasmic staining of trophoblastic cells was considered immunohistochemically positive. In the PP tissue samples, positive MMP‐2 staining was detected as follows: 0 immunoreactivity, one patient (4%); 1(+), six patients (24%); 2(+), seven patients (28%); and 3(+), 11 patients (44%). In the term pregnant placental tissue samples, positive MMP‐2 staining was detected in five patients (20%) at 0 immunoreactivity, 12 (48%) at 1(+) immunoreactivity, five (20%) at 2(+) immunoreactivity, and three patients (12%) at 3(+) immunoreactivity. Immunohistochemical expression was significantly different between the PP and normal term pregnancy placental tissues (P = 0.02). Conclusion The stronger expression of the MMP‐2 enzyme in the PP as compared to the normal placental tissue suggests that this enzyme may be an effective mediator in the pathogenesis of PP.
doi_str_mv 10.1111/jog.12667
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Methods Twenty‐five pregnant subjects who underwent cesarean section due to PP and 25 term pregnant subjects who underwent cesarean section for obstetric reasons were included in the study. Demographic data, pathology reports, and histopathological samples were examined. Blocks containing samples of placenta underwent immunohistochemical analysis using the MMP‐2 antibody. Immunohistochemical expression of placental samples obtained from both groups was examined and compared. Results There were no statistically significant differences in the demographic data (P &gt; 0.05). With regard to immunohistochemistry, cytoplasmic staining of trophoblastic cells was considered immunohistochemically positive. In the PP tissue samples, positive MMP‐2 staining was detected as follows: 0 immunoreactivity, one patient (4%); 1(+), six patients (24%); 2(+), seven patients (28%); and 3(+), 11 patients (44%). In the term pregnant placental tissue samples, positive MMP‐2 staining was detected in five patients (20%) at 0 immunoreactivity, 12 (48%) at 1(+) immunoreactivity, five (20%) at 2(+) immunoreactivity, and three patients (12%) at 3(+) immunoreactivity. Immunohistochemical expression was significantly different between the PP and normal term pregnancy placental tissues (P = 0.02). Conclusion The stronger expression of the MMP‐2 enzyme in the PP as compared to the normal placental tissue suggests that this enzyme may be an effective mediator in the pathogenesis of PP.</description><identifier>ISSN: 1341-8076</identifier><identifier>EISSN: 1447-0756</identifier><identifier>DOI: 10.1111/jog.12667</identifier><identifier>PMID: 25656855</identifier><language>eng</language><publisher>Australia: Blackwell Publishing Ltd</publisher><subject>Adult ; Cesarean Section ; Cross-Sectional Studies ; Female ; Hospitals, University ; Humans ; Immunohistochemistry ; Matrix Metalloproteinase 2 - metabolism ; matrix metalloproteinase-2 ; Placenta - enzymology ; Placenta - metabolism ; Placenta - pathology ; Placenta Accreta - enzymology ; Placenta Accreta - pathology ; Placenta Accreta - surgery ; placenta percreta ; Pregnancy ; Pregnancy Trimester, Third ; term placenta ; Turkey ; Up-Regulation</subject><ispartof>The journal of obstetrics and gynaecology research, 2015-07, Vol.41 (7), p.1018-1022</ispartof><rights>2015 The Authors. Journal of Obstetrics and Gynaecology Research © 2015 Japan Society of Obstetrics and Gynecology</rights><rights>2015 The Authors. Journal of Obstetrics and Gynaecology Research © 2015 Japan Society of Obstetrics and Gynecology.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5237-c317b621271dedbd54b4b209513f1c1e5d13b63938455ae4f488963e7502714b3</citedby><cites>FETCH-LOGICAL-c5237-c317b621271dedbd54b4b209513f1c1e5d13b63938455ae4f488963e7502714b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fjog.12667$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fjog.12667$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1416,27922,27923,45572,45573</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/25656855$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kocarslan, Sezen</creatorcontrib><creatorcontrib>Incebıyık, Adnan</creatorcontrib><creatorcontrib>Guldur, Muhammet Emin</creatorcontrib><creatorcontrib>Ekinci, Turan</creatorcontrib><creatorcontrib>Ozardali, Hasan Ilyas</creatorcontrib><title>What is the role of matrix metalloproteinase-2 in placenta percreta?</title><title>The journal of obstetrics and gynaecology research</title><addtitle>J Obstet Gynaecol Res</addtitle><description>Aim This study compared the placental expression of the matrix metalloproteinase‐2 (MMP‐2) enzyme, which is thought to play a key role in the penetration of trophoblastic cells, in third‐trimester placenta percreta (PP) patients with that of women with normal pregnancies. Methods Twenty‐five pregnant subjects who underwent cesarean section due to PP and 25 term pregnant subjects who underwent cesarean section for obstetric reasons were included in the study. Demographic data, pathology reports, and histopathological samples were examined. Blocks containing samples of placenta underwent immunohistochemical analysis using the MMP‐2 antibody. Immunohistochemical expression of placental samples obtained from both groups was examined and compared. Results There were no statistically significant differences in the demographic data (P &gt; 0.05). With regard to immunohistochemistry, cytoplasmic staining of trophoblastic cells was considered immunohistochemically positive. In the PP tissue samples, positive MMP‐2 staining was detected as follows: 0 immunoreactivity, one patient (4%); 1(+), six patients (24%); 2(+), seven patients (28%); and 3(+), 11 patients (44%). In the term pregnant placental tissue samples, positive MMP‐2 staining was detected in five patients (20%) at 0 immunoreactivity, 12 (48%) at 1(+) immunoreactivity, five (20%) at 2(+) immunoreactivity, and three patients (12%) at 3(+) immunoreactivity. Immunohistochemical expression was significantly different between the PP and normal term pregnancy placental tissues (P = 0.02). Conclusion The stronger expression of the MMP‐2 enzyme in the PP as compared to the normal placental tissue suggests that this enzyme may be an effective mediator in the pathogenesis of PP.</description><subject>Adult</subject><subject>Cesarean Section</subject><subject>Cross-Sectional Studies</subject><subject>Female</subject><subject>Hospitals, University</subject><subject>Humans</subject><subject>Immunohistochemistry</subject><subject>Matrix Metalloproteinase 2 - metabolism</subject><subject>matrix metalloproteinase-2</subject><subject>Placenta - enzymology</subject><subject>Placenta - metabolism</subject><subject>Placenta - pathology</subject><subject>Placenta Accreta - enzymology</subject><subject>Placenta Accreta - pathology</subject><subject>Placenta Accreta - surgery</subject><subject>placenta percreta</subject><subject>Pregnancy</subject><subject>Pregnancy Trimester, Third</subject><subject>term placenta</subject><subject>Turkey</subject><subject>Up-Regulation</subject><issn>1341-8076</issn><issn>1447-0756</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2015</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kMtOwzAQRS0EglJY8APIS1ik9dvJCiEeLVBRFqBKbCwnmdCUpCl2KsrfYyjtjtl4JJ97NLoInVDSo2H6s-atR5lSegd1qBA6Ilqq3bBzQaOYaHWADr2fEUJ1QuN9dMCkkiqWsoOuJ1Pb4tLjdgrYNRXgpsC1bV25wjW0tqqahWtaKOfWQ8RwOceLymYwby1egMtcYC6O0F5hKw_Hf28XvdzePF8No9F4cHd1OYoyybiOMk51qhhlmuaQp7kUqUgZSSTlBc0oyJzyVPGEx0JKC6IQcZwoDlqSEBEp76KztTec9LEE35q69BlUlZ1Ds_SGqkQHvWAyoOdrNHON9w4Ks3Blbd2XocT8lGZCaea3tMCe_mmXaQ35lty0FID-GvgsK_j632Tux4ONMlonSt_Capuw7t2EXy3N5HFghow8DJLRk3nl381rgzs</recordid><startdate>201507</startdate><enddate>201507</enddate><creator>Kocarslan, Sezen</creator><creator>Incebıyık, Adnan</creator><creator>Guldur, Muhammet Emin</creator><creator>Ekinci, Turan</creator><creator>Ozardali, Hasan Ilyas</creator><general>Blackwell Publishing Ltd</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>201507</creationdate><title>What is the role of matrix metalloproteinase-2 in placenta percreta?</title><author>Kocarslan, Sezen ; Incebıyık, Adnan ; Guldur, Muhammet Emin ; Ekinci, Turan ; Ozardali, Hasan Ilyas</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5237-c317b621271dedbd54b4b209513f1c1e5d13b63938455ae4f488963e7502714b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2015</creationdate><topic>Adult</topic><topic>Cesarean Section</topic><topic>Cross-Sectional Studies</topic><topic>Female</topic><topic>Hospitals, University</topic><topic>Humans</topic><topic>Immunohistochemistry</topic><topic>Matrix Metalloproteinase 2 - metabolism</topic><topic>matrix metalloproteinase-2</topic><topic>Placenta - enzymology</topic><topic>Placenta - metabolism</topic><topic>Placenta - pathology</topic><topic>Placenta Accreta - enzymology</topic><topic>Placenta Accreta - pathology</topic><topic>Placenta Accreta - surgery</topic><topic>placenta percreta</topic><topic>Pregnancy</topic><topic>Pregnancy Trimester, Third</topic><topic>term placenta</topic><topic>Turkey</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kocarslan, Sezen</creatorcontrib><creatorcontrib>Incebıyık, Adnan</creatorcontrib><creatorcontrib>Guldur, Muhammet Emin</creatorcontrib><creatorcontrib>Ekinci, Turan</creatorcontrib><creatorcontrib>Ozardali, Hasan Ilyas</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>The journal of obstetrics and gynaecology research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kocarslan, Sezen</au><au>Incebıyık, Adnan</au><au>Guldur, Muhammet Emin</au><au>Ekinci, Turan</au><au>Ozardali, Hasan Ilyas</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>What is the role of matrix metalloproteinase-2 in placenta percreta?</atitle><jtitle>The journal of obstetrics and gynaecology research</jtitle><addtitle>J Obstet Gynaecol Res</addtitle><date>2015-07</date><risdate>2015</risdate><volume>41</volume><issue>7</issue><spage>1018</spage><epage>1022</epage><pages>1018-1022</pages><issn>1341-8076</issn><eissn>1447-0756</eissn><abstract>Aim This study compared the placental expression of the matrix metalloproteinase‐2 (MMP‐2) enzyme, which is thought to play a key role in the penetration of trophoblastic cells, in third‐trimester placenta percreta (PP) patients with that of women with normal pregnancies. Methods Twenty‐five pregnant subjects who underwent cesarean section due to PP and 25 term pregnant subjects who underwent cesarean section for obstetric reasons were included in the study. Demographic data, pathology reports, and histopathological samples were examined. Blocks containing samples of placenta underwent immunohistochemical analysis using the MMP‐2 antibody. Immunohistochemical expression of placental samples obtained from both groups was examined and compared. Results There were no statistically significant differences in the demographic data (P &gt; 0.05). With regard to immunohistochemistry, cytoplasmic staining of trophoblastic cells was considered immunohistochemically positive. In the PP tissue samples, positive MMP‐2 staining was detected as follows: 0 immunoreactivity, one patient (4%); 1(+), six patients (24%); 2(+), seven patients (28%); and 3(+), 11 patients (44%). In the term pregnant placental tissue samples, positive MMP‐2 staining was detected in five patients (20%) at 0 immunoreactivity, 12 (48%) at 1(+) immunoreactivity, five (20%) at 2(+) immunoreactivity, and three patients (12%) at 3(+) immunoreactivity. Immunohistochemical expression was significantly different between the PP and normal term pregnancy placental tissues (P = 0.02). Conclusion The stronger expression of the MMP‐2 enzyme in the PP as compared to the normal placental tissue suggests that this enzyme may be an effective mediator in the pathogenesis of PP.</abstract><cop>Australia</cop><pub>Blackwell Publishing Ltd</pub><pmid>25656855</pmid><doi>10.1111/jog.12667</doi><tpages>5</tpages></addata></record>
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source MEDLINE; Wiley Online Library Journals Frontfile Complete
subjects Adult
Cesarean Section
Cross-Sectional Studies
Female
Hospitals, University
Humans
Immunohistochemistry
Matrix Metalloproteinase 2 - metabolism
matrix metalloproteinase-2
Placenta - enzymology
Placenta - metabolism
Placenta - pathology
Placenta Accreta - enzymology
Placenta Accreta - pathology
Placenta Accreta - surgery
placenta percreta
Pregnancy
Pregnancy Trimester, Third
term placenta
Turkey
Up-Regulation
title What is the role of matrix metalloproteinase-2 in placenta percreta?
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