The role of syndecan-2 in amyloid plaque formation

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The role of syndecan-2 in amyloid plaque formation. / Leonova, E. I.; Galzitskaya, O. V.

In: Molecular Biology, Vol. 49, No. 1, 01.01.2015, p. 77-85.

Research output: Contribution to journal › Review article › peer-review

Author

Leonova, E. I. ; Galzitskaya, O. V. / The role of syndecan-2 in amyloid plaque formation. In: Molecular Biology. 2015 ; Vol. 49, No. 1. pp. 77-85.

BibTeX

@article{4c6b2e7b868948708464eec501a47efd,

title = "The role of syndecan-2 in amyloid plaque formation",

abstract = "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.",

keywords = "Alzheimer{\textquoteright}s disease, disordered regions, extracellular matrix, heparan sulfate proteoglycan, syndecan",

author = "Leonova, {E. I.} and Galzitskaya, {O. V.}",

year = "2015",

month = jan,

day = "1",

doi = "10.1134/S0026893315010082",

language = "English",

volume = "49",

pages = "77--85",

journal = "Molecular Biology",

issn = "0026-8933",

publisher = "Pleiades Publishing",

number = "1",

}

RIS

TY - JOUR

T1 - The role of syndecan-2 in amyloid plaque formation

AU - Leonova, E. I.

AU - Galzitskaya, O. V.

PY - 2015/1/1

Y1 - 2015/1/1

N2 - 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.

AB - 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.

KW - Alzheimer’s disease

KW - disordered regions

KW - extracellular matrix

KW - heparan sulfate proteoglycan

KW - syndecan

UR - http://www.scopus.com/inward/record.url?scp=84923031756&partnerID=8YFLogxK

U2 - 10.1134/S0026893315010082

DO - 10.1134/S0026893315010082

M3 - Review article

C2 - 25916113

AN - SCOPUS:84929940206

VL - 49

SP - 77

EP - 85

JO - Molecular Biology

JF - Molecular Biology

SN - 0026-8933

IS - 1

ER -

ID: 45419897