Vol 49(2015) N 1 p. 77-85; DOI 10.1134/S0026893315010082
E.I. Leonova1,2, O.V. Galzitskaya1*
The role of syndecan-2 in amyloid plaque formation
1Institute of Protein Research, Russian Academy of Sciences, Pushchino, 142290 Russia
Friedrich Engels once defined life as 'the mode of existence of protein bodies.' This notion has become widely acknowledged; however, upon closer inspection, not only is the mere existence of protein bodies important, but also their changes over time. What are the characteristics of aging? Apparently, the characteristics include changes in the functioning of protein molecules, in particular uncontrolled protein aggregation, which may occur in any organ and may involve any protein. Although their clinical presentations are different, diseases associated with pathological accumulation of aggregated proteins are considered as a general group termed amyloidosis. Depending on the protein aggregation site, amyloidosis may present as a variety of pathologic conditions ranging from neurodegenerative disorders and malignant tumors to arthritis and tuberculosis. There is no doubt that the understanding of the mechanisms that underlie the transformation of absolutely normal functioning proteins into pathological aggregated forms will help to develop novel medications that could prevent protein aggregation and, thus, contribute to the prolongation of life. This review discusses the functions of syndecan-2, its structural organization, and its role in the formation of amyloid plaques.
syndecan, heparan sulfate proteoglycan, disordered regions, extracellular matrix, Alzheimer's disease