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Proteomics analysis of autophagic cells under starvation
Author(s) -
Kang Jeong Han,
Ding WenXing,
Liao Yong,
Yin XiaoMing
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.858.2
Subject(s) - autophagy , proteomics , proteome , organelle , microbiology and biotechnology , cytosol , gel electrophoresis , biology , two dimensional gel electrophoresis , cytoplasm , chemistry , lysosome , biochemistry , enzyme , apoptosis , gene
Autophagy is involved in the bulk degradation of long‐lived cytosolic proteins and subcellular organelles, and is important for the survival of cells during starvation and stress. The underlying mechanisms are still unclear. A comparative proteomics approach, combining two‐dimensional gel‐electrophoresis with matrix‐assisted laser desorption/ionization time‐of flight mass spectrometry, was used to identify proteins whose expression is changed under amino acid starvation‐induced autophagy cells. We anticipated that this study might provide clues on protein regulations that may be important for autophagy process. In total, the expression levels of 58 protein spots changed significantly between the starved cells and control cells. The large differences in protein expressions were observed for enzymes involved in intermediate metabolism, structure proteins and proteins associated with subcellular organelles. The expression of some proteins was validated by RT‐PCR, Immunoblotting, immunofluorescent microscopy and functional activity assays. The data described here will contribute to establishing a functional profile of proteome in autophagy‐induced cells. Furthermore, the proteins identified in this study may be attractive candidates as biomarkers for any pathogenesis processes involving autophagy.