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 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.


CONCLUSIONS
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.
Wang
Pengcheng
P
Department of Physiological Sciences, Oklahoma State University, Stillwater, OK 74078, USA. pengcheng.wang@okstate.edu
Chintagari
Narendranath Reddy
NR
Narayanaperumal
Jeyaparthasarathy
J
Ayalew
Sahlu
S
Hartson
Steven
S
Liu
Lin
L
D000818:Animals; D008168:Lung / Q000648:ultrastructure*; D011506:Proteins / Q000032:analysis* / Q000502:physiology; D020543:Proteome / Q000032:analysis*; D040901:Proteomics / Q000379:methods; D011663:Pulmonary Surfactants / Q000378:metabolism; D051381:Rats; D022142:Secretory Vesicles / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D011506:Proteins; D020543:Proteome; D011663:Pulmonary Surfactants