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Heparan sulfate and heparin interactions with proteins
Maria C Z Meneghetti1, Ashley J Hughes2, Timothy R Rudd3
1Departamento de Bioquímica, Universidade Federal de São Paulo (UNIFESP), Rua Três de Maio, São Paulo 40440-020, Brazil.
Journal of the Royal Society, Interface
|August 21, 2015
Summary
Heparan sulfate (HS) and heparin are crucial for biological regulation via protein interactions. Their structure-activity relationship involves both selectivity and redundancy, influenced by cations.
Area of Science:
- Biochemistry
- Glycobiology
- Molecular Biology
Background:
- Heparan sulfate (HS) and heparin are vital polysaccharides in animal cells and extracellular matrices.
- They regulate biological processes through extensive protein interactions.
- HS and heparin exhibit diverse biological and pharmacological activities.
Purpose of the Study:
- To explore the structure-activity relationship of HS and heparin.
- To reconcile opposing views on HS/heparin binding specificity versus charge dependence.
- To investigate the role of cations in modulating HS/heparin activity.
Main Methods:
- Review of in vitro, ex vivo, and in vivo experimental evidence.
- Analysis of protein-binding properties of HS and heparin.
- Consideration of polysaccharide chain structure and protein binding sites.
Main Results:
- Evidence supports a dualistic structure-activity relationship for HS and heparin, involving both redundancy and selectivity.
- The multi-dentate nature of HS/heparin chains and protein networks contribute to this relationship.
- Cations play a significant role in modulating HS/heparin activity.
Conclusions:
- The structure-activity relationship of HS and heparin is complex, balancing specificity and redundancy.
- Understanding these interactions is key to elucidating their regulatory roles.
- Further research into cation modulation can reveal new therapeutic strategies.
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