Facial reconstruction

Search LJMU Research Online

Browse Repository | Browse E-Theses

Heparan sulfate and heparin interactions with proteins.

Meneghetti, MC and Hughes, AJ and Rudd, TR and Nader, HB and Powell, AK and Yates, EA and Lima, MA (2015) Heparan sulfate and heparin interactions with proteins. Interface, 12. ISSN 1742-5689

[img] Text
2015 Meneghetti et al review GREEN.pdf - Accepted Version

Download (681kB)

Abstract

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, tissuespecific, 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.

Item Type: Article
Uncontrolled Keywords: MD Multidisciplinary
Subjects: Q Science > QD Chemistry
R Medicine > RS Pharmacy and materia medica
Divisions: Pharmacy & Biomolecular Sciences
Publisher: Royal Society, The
Date Deposited: 24 Aug 2015 14:35
Last Modified: 06 Sep 2017 17:49
DOI or Identification number: 10.1098/rsif.2015.0589
URI: http://researchonline.ljmu.ac.uk/id/eprint/1904

Actions (login required)

View Item View Item