Cancer proteomics functional proteomic studies

Mass spectrometry has been applied mainly in proteome research, but also in discovery and quantitation of neuropeptides that are involved in pain mechanisms, such as nocistatin, substance P, or verification of, for example, the structure of endogenous morphine in the central nervous system. Some proteomics studies of pain are aimed at the search for pain markers in cerebrospinal fluid, as it may reflect changes in brain and spinal cord functioning. Another research area concerns proteome analysis in cancer pain using spinal cord tissue and animal models. 

Most functional proteomic studies have been performed in cancer cell lines, that is, after exposition to toxicants, RNA inhibition, differentiation agents, viral transfection, and so on. These studies covered several aspects of mutagenesis, tumor promotion, and progression. In the recent years, it has been shown that repeated analysis of the proteome at different tumor stages also deliver distinct patterns and thus a functional picture of disease progression at the molecular level. 

Reymond MA, Steinert R, Kahne T, Sagynaliev E, Allal AS, Lippert H. Expression and functional proteomics studies in colorectal cancer. Pathol Res Pract 2004 200(2) 119-127. Review. 

Hennessy BT, Lu Y, Gonzalez-Angulo AM et al (2010) A technical assessment of the utility of reverse phase protein arrays for the study of the functional proteome in non-microdis-sected hiunan breast cancers. Clin Proteomics 6 129-151... 

Different cells make different proteins, so the proteome of one cell will be different from the proteome of another. In addition, cells that are defective or damaged, such as cancer cells, have a different proteome than normal cells. Therefore, the study of proteomes is an important area of biochemistry because understanding the normal proteome of a cell helps to understand the changes that occur as a result of disease. The study of proteomes, called proteomics, seeks to understand the composition, structure, function, and interactions of all the proteins of each living cell. 

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