Proteomics

Dataset Information

80

Quantitative proteomic analysis of gallbladder cancer


ABSTRACT: We carried out an iTRAQ-based quantitative proteomic analysis of gallbladder cancer and adjacent non-tumor tissue to systematically identify differentially expressed proteins in gallbladder cancer. Ten gallbladder adenocarcinoma and ten adjacent non-tumor tissue samples were selected post pathological confirmation for the study. Samples were pooled and In-solution trypsin digestion was carried out. Post digestion, peptides were iTRAQ labeled with 114 and 115 (gallbladder adenocarcinoma) and 116 and 117 (adjacent non-tumor samples). LC-MS/MS analysis of SCX fractions was carried out using a reversed phase analytical C18 column connected to 1200 Series Nanoflow LC interfaced with LTQ-Orbitrap Velos. Data were acquired using Xcalibur 2.1. Proteome Discoverer (v 1.3) suite was used for quantitation and database searches. LC-MS/MS data were searched using Mascot and SEQUEST search algorithms against Human RefSeq 50 supplemented with frequently observed contaminants.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo sapiens  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Akhilesh Pandey  

PROVIDER: PXD000619 | Pride | 2015-06-26

REPOSITORIES: Pride

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Publications

Identification of prosaposin and transgelin as potential biomarkers for gallbladder cancer using quantitative proteomics.

Sahasrabuddhe Nandini A NA   Barbhuiya Mustafa A MA   Bhunia Shushruta S   Subbannayya Tejaswini T   Gowda Harsha H   Advani Jayshree J   Shrivastav Braj R BR   Navani Sanjay S   Leal Pamela P   Roa Juan Carlos JC   Chaerkady Raghothama R   Gupta Sanjeev S   Chatterjee Aditi A   Pandey Akhilesh A   Tiwari Pramod K PK  

Biochemical and biophysical research communications 20140320 4


Gallbladder cancer is an uncommon but lethal malignancy with particularly high incidence in Chile, India, Japan and China. There is a paucity of unbiased large-scale studies investigating molecular basis of gallbladder cancer. To systematically identify differentially regulated proteins in gallbladder cancer, iTRAQ-based quantitative proteomics of gallbladder cancer was carried out using Fourier transform high resolution mass spectrometry. Of the 2575 proteins identified, proteins upregulated in  ...[more]

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