Proteomic analysis of lamellar bodies isolated from rat lungs

BACKGROUND: Lamellar bodies are lysosome-related secretory granules and store lung surfactant in alveolar type II cells. To better understand the mechanisms of surfactant secretion, we carried out proteomic analyses of lamellar bodies isolated from rat lungs. RESULTS: With peptide mass fingerprintin...

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Detalles Bibliográficos
Autores principales: Wang, Pengcheng, Chintagari, Narendranath Reddy, Narayanaperumal, Jeyaparthasarathy, Ayalew, Sahlu, Hartson, Steven, Liu, Lin
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2008
Materias:
Research Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2459160/
https://www.ncbi.nlm.nih.gov/pubmed/18577212
http://dx.doi.org/10.1186/1471-2121-9-34
Descripción
Sumario:BACKGROUND: Lamellar bodies are lysosome-related secretory granules and store lung surfactant in alveolar type II cells. To better understand the mechanisms of surfactant secretion, we carried out proteomic analyses of lamellar bodies isolated from rat lungs. RESULTS: With peptide mass fingerprinting by Matrix Assisted Laser Desorption/Ionization – Time of Flight mass spectrometry, 44 proteins were identified with high confidence. These proteins fell into diverse functional categories: surfactant-related, membrane trafficking, calcium binding, signal transduction, cell structure, ion channels, protein processing and miscellaneous. Selected proteins were verified by Western blot and immunohistochemistry. CONCLUSION: This proteomic profiling of lamellar bodies provides a basis for further investigations of functional roles of the identified proteins in lamellar body biogenesis and surfactant secretion.

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