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http://purl.uniprot.org/citations/27306493http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27306493http://www.w3.org/2000/01/rdf-schema#comment"Maternal PI3K p110δ has been implicated in smaller litter sizes in mice, but its underlying mechanism remains unclear. The placenta is an indispensable chimeric organ that supports mammalian embryonic development. Using a mouse model of genetic inactivation of PI3K p110δ (p110δ(D910A/D910A)), we show that fetuses carried by p110δ(D910A/D910A) females were growth retarded and showed increased mortality in utero mainly during placentation. The placentas in p110δ(D910A/D910A) females were anomalously anemic, exhibited thinner spongiotrophoblast layer and looser labyrinth zone, which indicate defective placental vasculogenesis. In addition, p110δ was detected in primary trophoblast giant cells (P-TGC) at early placentation. Maternal PI3K p110δ inactivation affected normal TGCs generation and expansion, impeded the branching of chorioallantoic placenta but enhanced the expression of matrix metalloproteinases (MMP-2, MMP-12). Poor vasculature support for the developing fetoplacental unit resulted in fetal death or gross growth retardation. These data, taken together, provide the first in vivo evidence that p110δ may play an important role in placental vascularization through manipulating trophoblast giant cell."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.org/dc/terms/identifier"doi:10.1038/srep28201"xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Hu X."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Li J."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Gu Q."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Zhang Q."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Wang G."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Yang X."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Zhang J."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Wang L."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Zheng L."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Ye Y."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/author"Guo S.W."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/name"Sci Rep"xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/pages"28201"xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/title"Phosphoinositide 3-Kinase (PI3K) Subunit p110delta Is Essential for Trophoblast Cell Differentiation and Placental Development in Mouse."xsd:string
http://purl.uniprot.org/citations/27306493http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/27306493http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27306493
http://purl.uniprot.org/citations/27306493http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27306493
http://purl.uniprot.org/uniprot/#_A0A0G2JGG7-mappedCitation-27306493http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27306493
http://purl.uniprot.org/uniprot/#_A0A0A6YX84-mappedCitation-27306493http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27306493
http://purl.uniprot.org/uniprot/#_D3Z783-mappedCitation-27306493http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/27306493