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Mutations of rat surfactant protein A have distinct effects on its glycosylation, secretion, aggregation and degradation.

Life sciences - 11 Nov 2014

Yang Wenbing, Shen Haitao, Fang Guodong, Li Hui, Li Lan, Deng Fang, Gu Wei, Li Kangsheng, Ma Lian, Gu Jiang, Wang Yongyu

Abstract excerpt

AIMS: Surfactant protein A (SP-A) plays critical roles in the innate immune system and surfactant homeostasis of the lung. Mutations in SP-A2 of the carbohydrate recognition domain (CRD) impair its glycosylation and are associated with pulmonary fibrosis in humans. We aim to examine how mutations in SP-A that impair its glycosylation affect its biological properties and lead to disease. MAIN METHODS: We generated...

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PMID: 25242514
DOI: 10.1016/j.lfs.2014.09.006

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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