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2015 ; 12
(110
): 0589
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Heparan sulfate and heparin interactions with proteins
#MMPMID26289657
Meneghetti MC
; Hughes AJ
; Rudd TR
; Nader HB
; Powell AK
; Yates EA
; Lima MA
J R Soc Interface
2015[Sep]; 12
(110
): 0589
PMID26289657
show ga
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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