Study of Splicing Factor, Proline- and Glutamine-rich by Proteomic Techniques in Human Malignant and Nonmalignant Cell Lines
2016
Splicing factor, proline- and glutamine-rich protein (SFPQ), was identified
in eight human cultivated cell lines by proteomic approaches. The cell proteins
have been separated by means of two-dimensional gel electrophoresis in two
modifications and identified by matrix-assisted laser desorption ionization mass
spectrometry with further tandem mass spectrometry. The analysis of proteins
from three human sarcomas cell lines (RD, U-2 OS and SK-UT-1B), three human
renal adenocarcinomas cell lines (A-498, 769-P and OKP-GS), and two prostate
adenocarcinomas cell lines (DU-145 and PC-3) revealed several electrophoretic
isoforms of SFPQ protein. Differences between theoretical and experimental molecular
masses and isoelectric points of SFPQ protein have been observed. Detailed
investigation of SFPQ peptides by tandem mass spectrometry has detected new phosphorylation
state of threonine residue in 168 position of SFPQ isoform in rhabdomyosarcoma cell line. Furthermore,
SFPQ has not been identified during proteomic study of several nonmalignant cell lines,
including cultured human mesenchymal stromal cells and myoblasts. However, SFPQ has been
found in all malignant cell lines in high quantity. In particular, its fractions are abundant in sarcomas
cell lines as opposed to nonmalignant mesenchymal cells. It is assumed that high quantity of SFPQ in
sarcomas cell lines may affect tumorigenesis.
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