Proteomic analysis of lamellar bodies isolated from rat lungs
1 Department of Physiological Sciences, Oklahoma State University, Stillwater, OK 74078, USA
2 Department of Pathobiology, Oklahoma State University, Stillwater, OK 74078, USA
3 Department of Biochemistry & Molecular Biology, Oklahoma State University, Stillwater, OK 74078, USA
Citation and License
BMC Cell Biology 2008, 9:34 doi:10.1186/1471-2121-9-34Published: 24 June 2008
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.
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.
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.