ECM proteins involved in cell migration and vessel formation compromise bovine cloned placentation

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dc.contributorLab. de Toxinologia Aplicadapt_BR
dc.contributorCeTICS - Centro de Toxinas, Resposta-imune e Sinalização Celularpt_BR
dc.contributor.authorBarreto, Rodrigo da Silva Nunespt_BR
dc.contributor.authorMatias, Gustavo de Sá Schiavopt_BR
dc.contributor.authorNishiyama Junior, Milton Yutakapt_BR
dc.contributor.authorCarreira, Ana Claudia Oliveirapt_BR
dc.contributor.authorMiglino, Maria Angelicapt_BR
dc.date.accessioned2022-06-14T13:36:27Z-
dc.date.available2022-06-14T13:36:27Z-
dc.date.issued2022pt_BR
dc.identifier.citationBarreto RSN, Matias GSS, Nishiyama Junior MY, Carreira ACO, Miglino MA. ECM proteins involved in cell migration and vessel formation compromise bovine cloned placentation. Theriogenology. 2022 Aug; 188:156-162. doi:10.1016/j.theriogenology.2022.04.003.pt_BR
dc.identifier.urihttps://repositorio.butantan.gov.br/handle/butantan/4388-
dc.description.abstractAdvances in Artificial Reproductive Technologies (ARTs) in bovine embryos to produce cloned pregnancies have been developed in the last years, however high pregnancy losses rates still present. Those rates are associated to placental morphology alterations that are majorly focused on extracellular matrix (ECM) alterations and consequently placentome hyperplasia, increased trophoblast cell migration and vascular defects. Herein, we aimed to search, at protein level, pathways altered by ART that can modify the placental development harmony. For this, we used 4-month-old control (n = 3), SDS-decellularized (n = 3) and cloned (n = 3) cotyledons for proteomic analysis. Samples were grouped by condition and were washed, lysed, urea-reduced, acetone-precipitated, DTT-educed, iodoacetamide-alkylated, trypsin digested, and C-18 column purified. At the end, 3 μg protein were loaded in Orbitrap Fusion Lumos spectrometer (ThermoScientific). Generated spectra were exported to MaxQuant software (v1.6.10.43) to produce the protein list of each sample, and the LFQ intensity were statistically analyzed by Inferno software (v.1.1.6970). After this, proteins related to ECM and cellular junction ontologies were filtered and manually annotated using DAVID Bioinformatics Resources 6.8. From 2577 identified protein sequences by MaxQuant software, 165 (7.1%) were filtered by selected ontologies. We found 10 proteins (B2M, COL6A6, FERMT3, LGALS3BP, NIBAN2, PDLIM5, PON1, PRP9, RASIP1 and SPARC) upregulated in clone, when compared to control condition. The ten pathways that enriched more proteins were: focal adhesion, ECM-receptor interaction, PI3K-Akt signaling pathway, protein digestion and absorption, amoebiasis, pathways in cancer, small cell lung cancer, platelet activation, regulation of actin cytoskeleton, and proteoglycans in cancer. Functionally, detected proteins, signaling pathways and ontologies are orchestrated to permit the binucleated trophoblastic cells migration and blood vessels modelling. In conclusion, the cloned condition presents the same mechanisms as control one, however overexpression of some specific ECM proteins could be responsible to exacerbate those mechanisms and can explain all morphophysiological alterations presented in cloned pregnancies associated to high pregnancies losses rates in this condition.pt_BR
dc.description.sponsorship(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulopt_BR
dc.format.extent156-162pt_BR
dc.language.isoEnglishpt_BR
dc.relation.ispartofTheriogenologypt_BR
dc.rightsRestricted accesspt_BR
dc.titleECM proteins involved in cell migration and vessel formation compromise bovine cloned placentationpt_BR
dc.typeArticlept_BR
dc.identifier.doi10.1016/j.theriogenology.2022.04.003pt_BR
dc.identifier.urlhttps://doi.org/10.1016/j.theriogenology.2022.04.003pt_BR
dc.contributor.external(USP) Universidade de São Paulopt_BR
dc.identifier.citationvolume188pt_BR
dc.subject.keywordcloned pregnancypt_BR
dc.subject.keywordECM proteinpt_BR
dc.subject.keywordcell migrationpt_BR
dc.subject.keywordneovascularizationpt_BR
dc.relation.ispartofabbreviatedTheriogenologypt_BR
dc.identifier.citationabntv. 188, p. 156-162, ago. 2022pt_BR
dc.identifier.citationvancouver2022 Aug; 188:156-162pt_BR
dc.contributor.butantanNishiyama Junior, Milton Yutaka|:Pesquisador|:Lab. de Toxinologia Aplicada:CeTICS - Centro de Toxinas, Resposta-imune e Sinalização Celularpt_BR
dc.sponsorship.butantan(FAPESP) Fundação de Amparo à Pesquisa do Estado de São Paulo¦¦2014/50844-3pt_BR
dc.identifier.bvsccBR78.1pt_BR
dc.identifier.bvsdbIBProdpt_BR
dc.description.dbindexedYespt_BR
item.grantfulltextembargo_20990101-
item.languageiso639-1English-
item.openairetypeArticle-
item.fulltextCom Texto completo-
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