Characterization of VAMP-2 in the lung: implication in lung surfactant secretion.

Cell Biology International
Pengcheng WangLin Liu

Abstract

Lung surfactant is crucial for reducing the surface tension of alveolar space, thus preventing the alveoli from collapse. Lung surfactant is synthesized in alveolar epithelial type II cells and stored in lamellar bodies before being released via the fusion of lamellar bodies with the apical plasma membrane. SNAREs (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptors) play an essential role in membrane fusion. We have previously demonstrated the requirement of t-SNARE (target SNARE) proteins, syntaxin 2 and SNAP-23 (N-ethylmaleimide-sensitive factor-attachment protein 23), in regulated surfactant secretion. Here, we characterized the distribution of VAMPs (vesicle-associated membrane proteins) in rat lung and alveolar type II cells. VAMP-2, -3 and -8 are shown in type II cells at both mRNA and protein levels. VAMP-2 and -8 were enriched in LB (lamellar body) fraction. Immunochemistry studies indicated that VAMP-2 was co-localized with the LB marker protein, LB-180. Functionally, the cytoplasmic domain of VAMP-2, but not VAMP-8 inhibited surfactant secretion in type II cells. We suggest that VAMP-2 is the v-SNARE (vesicle SNARE) involved in regulated surfactant secretion.

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Citations

Dec 8, 2014·FEBS Letters·Honghao ZhangLin Liu
Jan 14, 2016·Bioarchitecture·Riddhi Atul JaniSubba Rao Gangi Setty
Oct 30, 2016·Annals of Anatomy = Anatomischer Anzeiger : Official Organ of the Anatomische Gesellschaft·Bárbara OlmedaJesus Pérez-Gil
Jan 14, 2018·Developmental Dynamics : an Official Publication of the American Association of Anatomists·Maiko IkezawaHiroshi Yorifuji
Sep 13, 2019·Nature Communications·Alexandria N Hughes, Bruce Appel

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