Protocol detail

Membrane Proteome Profiling of Lung Cancer Metastasis

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Each membrane protein fraction isolated from the indicated lung cancer cell lines by the membrane protein enrichment kit was separated by SDS-PAGE and then subjected to in-gel enzymatic digestion. The tryptic peptides were identified by the linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer (LTQ-FTICR MS, Thermo Electron) independently in duplicate 15 (link). Identification of protein and label-free quantitative analysis were performed using MaxQuant 16 (link) and MaxLFQ 17 (link) software, respectively. A total of 233 proteins that exhibited at least a 2-fold increase in brain-metastatic cancer cells (Bm7 vs. F4) were identified.

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Lin C.C., Huang Y.K., Cho C.F., Lin Y.S., Lo C.C., Kuo T.T., Tseng G.C., Cheng W.C., Chang W.C., Hsiao T.H., Lai L.C., Shih J.Y., Liu Y.H., Chao K.S., Hsu J.L., Lee P.C., Sun X., Hung M.C, & Sher Y.P. (2020). Targeting positive feedback between BASP1 and EGFR as a therapeutic strategy for lung cancer progression. Theranostics, 10(24), 10925-10939.

Publication 2020

LTQ-FTICR MS

A proteins Brain metastatic cancer Cell lines Cells Cyclotron Digestion Electron Enzymatic Lung cancer Membrane protein Peptides Protein Resonance Sds page Tryptic

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Variable analysis

independent variables

Lung cancer cell lines (Bm7 and F4)

dependent variables

Proteins that exhibited at least a 2-fold increase in brain-metastatic cancer cells (Bm7) compared to the non-brain-metastatic cancer cells (F4)

control variables

Membrane protein fractions isolated from the indicated lung cancer cell lines by the membrane protein enrichment kit
SDS-PAGE separation of the membrane protein fractions
In-gel enzymatic digestion of the tryptic peptides
Identification of the tryptic peptides by the linear ion trap-Fourier transform ion cyclotron resonance mass spectrometer (LTQ-FTICR MS, Thermo Electron)

controls

No positive or negative controls were explicitly mentioned in the provided information.

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