Current Proteomics

Bernd Rehm  
Institute of Molecular BioSciences Massey University
Private Bag 11222
Palmerston North
New Zealand

Back

Proteomic Approaches for the Study of Transgelins as Tumor-associated Proteins and Potential Biomarkers

Author(s): Sergey S. Shishkin, Marina A. Kovaleva, Lidia S. Eryomina, Ksenia V. Lisitskaya, Leonid I. Kovalev.

Abstract:

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.

Order Reprints Order Eprints Rights & PermissionsPrintExport

Article Details

VOLUME: 10
ISSUE: 2
Year: 2013
Page: [165 - 178]
Pages: 14
DOI: 10.2174/1570164611310020008
Price: $58