A number of studies have revealed histochemical changes in the trapezius muscle in people afflicted with pain. A number of these changes have been compared with the energy metabolism in the muscle cell. There is still, however, relatively little knowledge of the normal biochemical composition in the trapezius muscle. In order to investigate the trapezius muscle, a technique is used which allowed a large number of proteins to be analysed simultaneously (proteomics).
In this project, muscle biopsies from the trapezius and vastus lateralis muscles of healthy people are used. Proteins from the biopsies are separated onto gels, first by isoelectric point and then by molecular weight in accordance with 2-DIGE (Two dimensional gel electrophoresis). Before the proteins are grouped onto the same gel, each group is marked with different fluorescent colours. The intensity of each colour is measured, providing a link between the two groups. As standard, a mix of the two tests is used, which is coloured in with an additional fluorescent colour (cyanine colours). The proteins are removed from the gels and analysed with a mass spectrometer (MALDI-TOF-MS).
The results of the project reveal that a number of proteins differ from one muscle to another and this must be followed up via more in-depth studies.