Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry

Zanivan, S. , Gnad, F., Wickstrom, S. A., Geiger, T., Macek, B., Cox, J., Fassler, R. and Mann, M. (2008) Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry. Journal of Proteome Research, 7(12), pp. 5314-5326. (doi:10.1021/pr800599n) (PMID:19367708)

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Abstract

Kinases play a prominent role in tumor development, pointing to the presence of specific phosphorylation patterns in tumor tissues. Here, we investigate whether recently developed high resolution mass spectrometric (MS) methods for proteome and phosphoproteome analysis can also be applied to solid tumors. As tumor model, we used TG3 mutant mice carrying skin melanomas. At total of 100 μg of solid tumor lysate yielded a melanoma proteome of 4443 identified proteins, including at least 88 putative melanoma markers previously found by cDNA microarray technology. Analysis of 2 mg of lysate from dissected melanoma with titansphere chromatography and 8 mg with strong cation exchange together resulted in the identification of more than 5600 phosphorylation sites on 2250 proteins. The phosphoproteome included many hits from pathways important in melanoma. One-month storage at −80 °C did not significantly decrease the number of identified phosphorylation sites. Thus, solid tumor can be analyzed by MS-based proteomics with similar efficiency as cell culture models and in amounts compatible with biopsies.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Zanivan, Dr Sara Rossana
Authors: Zanivan, S., Gnad, F., Wickstrom, S. A., Geiger, T., Macek, B., Cox, J., Fassler, R., and Mann, M.
College/School:College of Medical Veterinary and Life Sciences > Institute of Cancer Sciences
Journal Name:Journal of Proteome Research
Publisher:American Chemical Society
ISSN:1535-3893
ISSN (Online):1535-3907
Published Online:31 October 2008

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