Caveolin-1: a critical regulator of lung injury - PubMed (original) (raw)

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Caveolin-1: a critical regulator of lung injury

Yang Jin et al. Am J Physiol Lung Cell Mol Physiol. 2011 Feb.

Abstract

Caveolin-1 (cav-1), a 22-kDa transmembrane scaffolding protein, is the principal structural component of caveolae. Cav-1 regulates critical cell functions including proliferation, apoptosis, cell differentiation, and transcytosis via diverse signaling pathways. Abundant in almost every cell type in the lung, including type I epithelial cells, endothelial cells, smooth muscle cells, fibroblasts, macrophages, and neutrophils, cav-1 plays a crucial role in the pathogenesis of acute lung injury (ALI). ALI and its severe form, acute respiratory distress syndrome (ARDS), are responsible for significant morbidity and mortality in intensive care units, despite improvement in ventilation strategies. The pathogenesis of ARDS is still poorly understood, and therapeutic options remain limited. In this article, we summarize recent data regarding the regulation and function of cav-1 in lung biology and pathology, in particular as it relates to ALI. We further discuss the potential molecular and cellular mechanisms by which cav-1 expression contributes to ALI. Investigating the cellular functions of cav-1 may provide new insights for understanding the pathogenesis of ALI and provide novel targets for therapeutic interventions in the future.

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Figures

Fig. 1.

Fig. 1.

Structure of caveolin-1. Cav-1 contains a hydrophobic central domain with a hairpin-like conformation inserted in the inner leaflet of the plasma membrane. 14–16 Cav-1 monomers form a single cav-1 homooligomer. A simplified dimmer is illustrated here. Both the COOH and NH2 terminus of the cav-1 monomer face the cytoplasm. The caveolin scaffolding domain is located between amino acid residues 82–101 in the NH2-terminal region adjacent to the hydrophobic membrane-insertion domain. The COOH-terminal region of cav-1 contains 3 palmitoylated cysteine residues. Inset: caveolae viewed by electron microscopy (×50,000).

Fig. 2.

Fig. 2.

Scheme of proposed roles of caveolin-1 in acute lung injury.

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References

    1. Alonso MA, Millán J. The role of lipid rafts in signalling and membrane trafficking in T lymphocytes. J Cell Sci 114: 3957–3965, 2001. - PubMed
    1. Benlimame N, Le PU, Nabi IR. Localization of autocrine motility factor receptor to caveolae and clathrin-independent internalization of its ligand to smooth endoplasmic reticulum. Mol Biol Cell 9: 1773–1786, 1998. - PMC - PubMed
    1. Bento-Abreu A, Velasco A, Polo-Hernández E, Lillo C, Kozyraki R, Tabernero A, Medina JM. Albumin endocytosis via megalin in astrocytes is caveola- and Dab-1 dependent and is required for the synthesis of the neurotrophic factor oleic acid. J Neurochem 111: 49–60, 2009. - PubMed
    1. Bist A, Fielding PE, Fielding CJ. Two sterol regulatory element-like sequences mediate up-regulation of caveolin gene transcription in response to low density lipoprotein free cholesterol. Proc Natl Acad Sci USA 94: 10693–10698, 1997. - PMC - PubMed
    1. Buckley S, Barsky L, Driscoll B, Weinberg K, Anderson KD, Warburton D. Apoptosis and DNA damage in type 2 alveolar epithelial cells cultured from hyperoxic rats. Am J Physiol Lung Cell Mol Physiol 274: L714–L720, 1998. - PubMed

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