Detergent addition to tryptic digests and ion mobility separation prior to MS/MS improves peptide yield and protein identification for in situ proteomic investigation of frozen and formalin‐fixed paraffin‐embedded adenocarcinoma tissue sections

• Published in: Proteomics (Weinheim) Vol. 9; no. 10; pp. 2750 - 2763
• Main Authors: Djidja, Marie‐Claude, Francese, Simona, Loadman, Paul M., Sutton, Chris W., Scriven, Peter, Claude, Emmanuelle, Snel, Marten F., Franck, Julien, Salzet, Michel, Clench, Malcolm R.
• Format: Journal Article
• Language: English
• Published: Weinheim WILEY‐VCH Verlag 01.05.2009; Wiley-VCH; Wiley-VCH Verlag
• Subjects: Adenocarcinoma - chemistry; Analytical, structural and metabolic biochemistry; Animals; Biological and medical sciences; Breast Neoplasms - chemistry; Cell Line, Tumor; Detergents; Disease Models, Animal; Female; Formalin fixed paraffin embedded; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation, Neoplastic; Humans; Imaging; Life Sciences; MALDI; MCF7; Mice; Mice, Inbred BALB C; Miscellaneous; Neoplasm Proteins - analysis; Neoplasm Proteins - chemistry; Neoplasm Transplantation; Paraffin Embedding; Proteins; Proteomics - methods; Sensitivity and Specificity; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; Stress proteins; Trypsin - metabolism; Adenocarcinoma; MCF7; Peptides; In situ; Formalin fixed paraffin embedded; MALDI; Identification; Malignant tumor; Protein; Stress; Imaging; Proteomics; Yield; Stress proteins; Cancer

The identification of proteins involved in tumour progression or which permit enhanced or novel therapeutic targeting is essential for cancer research. Direct MALDI analysis of tissue sections is rapidly demonstrating its potential for protein imaging and profiling in the investigation of a range of...