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http://purl.uniprot.org/citations/26252542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26252542http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/26252542http://www.w3.org/2000/01/rdf-schema#comment"Reticulocalbin 3 (Rcn3) is an endoplasmic reticulum lumen protein localized to the secretory pathway. As a Ca2t-binding protein of 45 kDa (Cab45)/Rcn/ER Ca2t-binding protein of 55 kDa (ERC45)/calumenin (CREC) family member, Rcn3 is reported to function as a chaperone protein involved in protein synthesis and secretion; however, the biological role of Rcn3 is largely unknown. The results presented here, for the first time, depict an indispensable physiological role of Rcn3 in perinatal lung maturation by using an Rcn3 gene knockout mouse model. These mutant mice die immediately at birth owing to atelectasis-induced neonatal respiratory distress, although these embryos are produced with grossly normal development. This respiratory distress results from a failure of functional maturation of alveolar epithelial type II cells during alveogenesis. This immaturity of type II cells is associated with a dramatic reduction in surfactant protein A and D, a disruption in surfactant phospholipid homeostasis, and a disorder in lamellar body. In vitro studies further show that Rcn3 deficiency blunts the secretion of surfactant proteins and phospholipids from lung epithelial cells, suggesting a decrease in availability of surfactants for their surface activity. Collectively, these observations indicate an essential role of Rcn3 in perinatal lung maturation and neonatal respiratory adaptation as well as shed additional light on the mechanism of neonatal respiratory distress syndrome development."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.org/dc/terms/identifier"doi:10.1165/rcmb.2015-0036oc"xsd:string
http://purl.uniprot.org/citations/26252542http://purl.org/dc/terms/identifier"doi:10.1165/rcmb.2015-0036oc"xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Hou Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Hou Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Jin J."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Jin J."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Li Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Ren J."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Ren J."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Zhang X."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Zhang Y."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Xu R."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Xu R."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Shui G."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Shui G."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Ma R.Z."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Ma R.Z."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Man Lam S."xsd:string
http://purl.uniprot.org/citations/26252542http://purl.uniprot.org/core/author"Man Lam S."xsd:string