Serum amyloid A in the placenta and its role in trophoblast invasion
The serum amyloid A (SAA) protein is known to function in the acute phase response and immunoregulation. Recently, SAA has been shown to be involved in cell proliferation, differentiation and migratory behavior in different cell types. Here, we evaluated whether exogenous SAA could influence trophob...
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creator | Sandri, Silvana Urban Borbely, Alexandre Fernandes, Isabella de Oliveira, Edson Mendes Knebel, Franciele Hinterholz Ruano, Rodrigo Zugaib, Marcelo Filippin-Monteiro, Fabiola Bevilacqua, Estela Campa, Ana |
description | The serum amyloid A (SAA) protein is known to function in the acute phase response and immunoregulation. Recently, SAA has been shown to be involved in cell proliferation, differentiation and migratory behavior in different cell types. Here, we evaluated whether exogenous SAA could influence trophoblast invasion and differentiation using both the trophoblast-like BeWo cell line and fully differentiated human extravillous trophoblast cells (EVT) isolated from term placentae. SAA stimulated BeWo cell invasion, as measured in Matrigel invasion assays, and induced metalloprotease mRNA expression and activity. Given that BeWo cells express Toll-like receptor 4 (TLR4), a known receptor for SAA, we examined the role of TLR4 in SAA-induced invasion using a TLR4 neutralizing antibody. We also tested whether SAA could affect markers of trophoblast syncytialization in BeWo cells. We observed that SAA decreased βhCG secretion and did not influence trophoblast syncytialization. Using EVT cells isolated from human term basal plates, we confirmed that SAA at 1 and 10 µg/mL doubled EVT invasion in a TLR4-dependent manner, but at 20 µg/mL inhibited EVT cells invasiveness. In addition, we observed that SAA was expressed in both BeWo cells and human term placentae, specifically in the syncytiotrophoblast, decidual cells and EVT. In conclusion, SAA was identified as a molecule that functions in the placental microenvironment to regulate metalloprotease activity and trophoblast invasion, which are key processes in placentation and placental homeostasis. |
doi_str_mv | 10.1371/journal.pone.0090881 |
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Recently, SAA has been shown to be involved in cell proliferation, differentiation and migratory behavior in different cell types. Here, we evaluated whether exogenous SAA could influence trophoblast invasion and differentiation using both the trophoblast-like BeWo cell line and fully differentiated human extravillous trophoblast cells (EVT) isolated from term placentae. SAA stimulated BeWo cell invasion, as measured in Matrigel invasion assays, and induced metalloprotease mRNA expression and activity. Given that BeWo cells express Toll-like receptor 4 (TLR4), a known receptor for SAA, we examined the role of TLR4 in SAA-induced invasion using a TLR4 neutralizing antibody. We also tested whether SAA could affect markers of trophoblast syncytialization in BeWo cells. We observed that SAA decreased βhCG secretion and did not influence trophoblast syncytialization. Using EVT cells isolated from human term basal plates, we confirmed that SAA at 1 and 10 µg/mL doubled EVT invasion in a TLR4-dependent manner, but at 20 µg/mL inhibited EVT cells invasiveness. In addition, we observed that SAA was expressed in both BeWo cells and human term placentae, specifically in the syncytiotrophoblast, decidual cells and EVT. In conclusion, SAA was identified as a molecule that functions in the placental microenvironment to regulate metalloprotease activity and trophoblast invasion, which are key processes in placentation and placental homeostasis.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0090881</identifier><identifier>PMID: 24614130</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Adipocytes ; Angiogenesis ; Antibodies ; Biology ; Breast cancer ; Cell Line ; Cell Movement ; Chorionic gonadotropins ; Endocrinology ; Extracellular matrix ; Female ; Giant Cells - cytology ; Giant Cells - metabolism ; Humans ; Immunology ; Medicine ; Metabolism ; Penicillin ; Placenta ; Placenta - metabolism ; Pregnancy ; Rheumatoid arthritis ; RNA ; Rodents ; Serum Amyloid A Protein - metabolism ; Toll-like receptors ; Trophoblasts - cytology ; Trophoblasts - metabolism</subject><ispartof>PloS one, 2014-03, Vol.9 (3), p.e90881-e90881</ispartof><rights>COPYRIGHT 2014 Public Library of Science</rights><rights>2014 Sandri et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>2014 Sandri et al 2014 Sandri et al</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c758t-bb4fb3b1fc9c8fc9433f1072bb3629fa892f9422fe87befe520f0c35821bf3f23</citedby><cites>FETCH-LOGICAL-c758t-bb4fb3b1fc9c8fc9433f1072bb3629fa892f9422fe87befe520f0c35821bf3f23</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948705/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3948705/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2102,2928,23866,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24614130$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Oudejans, Cees</contributor><creatorcontrib>Sandri, Silvana</creatorcontrib><creatorcontrib>Urban Borbely, Alexandre</creatorcontrib><creatorcontrib>Fernandes, Isabella</creatorcontrib><creatorcontrib>de Oliveira, Edson Mendes</creatorcontrib><creatorcontrib>Knebel, Franciele Hinterholz</creatorcontrib><creatorcontrib>Ruano, Rodrigo</creatorcontrib><creatorcontrib>Zugaib, Marcelo</creatorcontrib><creatorcontrib>Filippin-Monteiro, Fabiola</creatorcontrib><creatorcontrib>Bevilacqua, Estela</creatorcontrib><creatorcontrib>Campa, Ana</creatorcontrib><title>Serum amyloid A in the placenta and its role in trophoblast invasion</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The serum amyloid A (SAA) protein is known to function in the acute phase response and immunoregulation. Recently, SAA has been shown to be involved in cell proliferation, differentiation and migratory behavior in different cell types. Here, we evaluated whether exogenous SAA could influence trophoblast invasion and differentiation using both the trophoblast-like BeWo cell line and fully differentiated human extravillous trophoblast cells (EVT) isolated from term placentae. SAA stimulated BeWo cell invasion, as measured in Matrigel invasion assays, and induced metalloprotease mRNA expression and activity. Given that BeWo cells express Toll-like receptor 4 (TLR4), a known receptor for SAA, we examined the role of TLR4 in SAA-induced invasion using a TLR4 neutralizing antibody. We also tested whether SAA could affect markers of trophoblast syncytialization in BeWo cells. We observed that SAA decreased βhCG secretion and did not influence trophoblast syncytialization. Using EVT cells isolated from human term basal plates, we confirmed that SAA at 1 and 10 µg/mL doubled EVT invasion in a TLR4-dependent manner, but at 20 µg/mL inhibited EVT cells invasiveness. In addition, we observed that SAA was expressed in both BeWo cells and human term placentae, specifically in the syncytiotrophoblast, decidual cells and EVT. In conclusion, SAA was identified as a molecule that functions in the placental microenvironment to regulate metalloprotease activity and trophoblast invasion, which are key processes in placentation and placental homeostasis.</description><subject>Adipocytes</subject><subject>Angiogenesis</subject><subject>Antibodies</subject><subject>Biology</subject><subject>Breast cancer</subject><subject>Cell Line</subject><subject>Cell Movement</subject><subject>Chorionic gonadotropins</subject><subject>Endocrinology</subject><subject>Extracellular matrix</subject><subject>Female</subject><subject>Giant Cells - cytology</subject><subject>Giant Cells - metabolism</subject><subject>Humans</subject><subject>Immunology</subject><subject>Medicine</subject><subject>Metabolism</subject><subject>Penicillin</subject><subject>Placenta</subject><subject>Placenta - metabolism</subject><subject>Pregnancy</subject><subject>Rheumatoid arthritis</subject><subject>RNA</subject><subject>Rodents</subject><subject>Serum Amyloid A Protein - 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Recently, SAA has been shown to be involved in cell proliferation, differentiation and migratory behavior in different cell types. Here, we evaluated whether exogenous SAA could influence trophoblast invasion and differentiation using both the trophoblast-like BeWo cell line and fully differentiated human extravillous trophoblast cells (EVT) isolated from term placentae. SAA stimulated BeWo cell invasion, as measured in Matrigel invasion assays, and induced metalloprotease mRNA expression and activity. Given that BeWo cells express Toll-like receptor 4 (TLR4), a known receptor for SAA, we examined the role of TLR4 in SAA-induced invasion using a TLR4 neutralizing antibody. We also tested whether SAA could affect markers of trophoblast syncytialization in BeWo cells. We observed that SAA decreased βhCG secretion and did not influence trophoblast syncytialization. Using EVT cells isolated from human term basal plates, we confirmed that SAA at 1 and 10 µg/mL doubled EVT invasion in a TLR4-dependent manner, but at 20 µg/mL inhibited EVT cells invasiveness. In addition, we observed that SAA was expressed in both BeWo cells and human term placentae, specifically in the syncytiotrophoblast, decidual cells and EVT. In conclusion, SAA was identified as a molecule that functions in the placental microenvironment to regulate metalloprotease activity and trophoblast invasion, which are key processes in placentation and placental homeostasis.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>24614130</pmid><doi>10.1371/journal.pone.0090881</doi><tpages>e90881</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adipocytes Angiogenesis Antibodies Biology Breast cancer Cell Line Cell Movement Chorionic gonadotropins Endocrinology Extracellular matrix Female Giant Cells - cytology Giant Cells - metabolism Humans Immunology Medicine Metabolism Penicillin Placenta Placenta - metabolism Pregnancy Rheumatoid arthritis RNA Rodents Serum Amyloid A Protein - metabolism Toll-like receptors Trophoblasts - cytology Trophoblasts - metabolism |
title | Serum amyloid A in the placenta and its role in trophoblast invasion |
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