Heparan sulfate and heparin interactions with proteins

Heparan sulfate (HS) polysaccharides are ubiquitous components of the cell surface and extracellular matrix of all multicellular animals, whereas heparin is present within mast cells and can be viewed as a more sulfated, tissue-specific, HS variant. HS and heparin regulate biological processes throu...

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Vydáno v:Journal of the Royal Society interface Ročník 12; číslo 110; s. 0589
Hlavní autoři: Meneghetti, Maria C Z, Hughes, Ashley J, Rudd, Timothy R, Nader, Helena B, Powell, Andrew K, Yates, Edwin A, Lima, Marcelo A
Médium: Journal Article
Jazyk:angličtina
Vydáno: England 06.09.2015
Témata:
Animals
Binding Sites
Heparin - chemistry
Heparin - metabolism
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Humans
Mast Cells - chemistry
Mast Cells - metabolism
Proteins - chemistry
Proteins - metabolism
Structure-Activity Relationship
heparin
cations
heparan sulfate
redundancy
polysaccharide
protein binding
ISSN:1742-5662, 1742-5662
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Popis
Shrnutí:Heparan sulfate (HS) polysaccharides are ubiquitous components of the cell surface and extracellular matrix of all multicellular animals, whereas heparin is present within mast cells and can be viewed as a more sulfated, tissue-specific, HS variant. HS and heparin regulate biological processes through interactions with a large repertoire of proteins. Owing to these interactions and diverse effects observed during in vitro, ex vivo and in vivo experiments, manifold biological/pharmacological activities have been attributed to them. The properties that have been thought to bestow protein binding and biological activity upon HS and heparin vary from high levels of sequence specificity to a dependence on charge. In contrast to these opposing opinions, we will argue that the evidence supports both a level of redundancy and a degree of selectivity in the structure-activity relationship. The relationship between this apparent redundancy, the multi-dentate nature of heparin and HS polysaccharide chains, their involvement in protein networks and the multiple binding sites on proteins, each possessing different properties, will also be considered. Finally, the role of cations in modulating HS/heparin activity will be reviewed and some of the implications for structure-activity relationships and regulation will be discussed.
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ISSN:1742-5662
1742-5662
DOI:10.1098/rsif.2015.0589