Proteomic Approaches for the Study of Transgelins as Tumor-associated Proteins and Potential Biomarkers
Sergey S. Shishkin,
Marina A. Kovaleva,
Lidia S. Eryomina,
Ksenia V. Lisitskaya,
Leonid I. Kovalev.
Transgelins, which have been studied by proteomic methods for more than ten years as tumor-associated proteins,
are the members of calponin family, since calponin homology domains are present in their amino acid sequences
and there are other typical structural features. According to the available information there is a specific tissue distribution
of these proteins. Three closely related genes which coded transgelins are revealed in the human genome. Single nucleotide
substitutions and the expression peculiarities of these genes can be the reasons for existence of several isoforms of
three main transgelins. Different manifestations of biochemical polymorphism of transgelins are detected by now. Transgelin
(or SM22-alpha) is well known as a biomarker of smooth muscle cell differentiation. It was revealed that transgelin
acts as repressor of MMP9 gene, coding matrix metalloproteinase-9. At the same time the oppositely directed changes in
the content of transgelin proteins were found in tissue samples of malignant tumors of the respiratory, digestive and urogenital
systems, as well as in the cultivated tumor cell using proteomic technologies. Correspondingly, according to some
authors transgelins can be potential biomarkers of malignant neoplasms, but in the opinion the others – transgelins are
suppressors of tumor growth. In this review, we consider possible reasons for such differences and discuss the prospects
of solution of the existing contradictions.
Keywords: Cancer, members of calponin family, proteomic approaches, transgelins.
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