Heparan sulfate-protein binding specificity

Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably t...

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Published inBiochemistry (Moscow) Vol. 78; no. 7; pp. 726 - 735
Main Authors Nugent, M. A., Zaia, J., Spencer, J. L.
Format Journal Article
LanguageEnglish
Published Boston Springer US 01.07.2013
Springer
Springer Nature B.V
Subjects
Animals
Antithrombin III - chemistry
Antithrombin III - metabolism
Biochemistry
Bioinformatics
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Fibroblast Growth Factors - chemistry
Fibroblast Growth Factors - metabolism
Glycoproteins
Growth factors
Health aspects
Heparan sulfate
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Humans
Leukocyte Elastase - antagonists & inhibitors
Leukocyte Elastase - metabolism
Life Sciences
Microbiology
Physiological aspects
Polysaccharides
Protein Binding
Protein folding
Proteins - chemistry
Proteins - metabolism
Review
Saccharides
Sulfates
United States
United States > US
heparin
glycosaminoglycans
proteoglycans
heparan sulfate
protein binding
bioinformatics
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Abstract Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.
AbstractList Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as coreceptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS--protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.
Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as coreceptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS--protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure. DOI: 10.1134/S0006297913070055 Key words: heparin, heparan sulfate, glycosaminoglycans, proteoglycans, protein binding, bioinformatics
Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.
Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure. [PUBLICATION ABSTRACT]
Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is characterized by a repeating disaccharide backbone that is subject to a wide range of modifications, making this class of macromolecules arguably the most information dense in all of biology. The majority of HS functions are associated with the ability to bind and regulate a wide range of proteins. Indeed, recent years have seen an explosion in the discovery of new activities for HS where it is now recognized that this class of glycans functions as co-receptors for growth factors and cytokines, modulates cellular uptake of lipoproteins, regulates protease activity, is critical to amyloid plaque formation, is used by opportunistic pathogens to enter cells, and may even participate in epigenetic regulation. This review will discuss the current state of understanding regarding the specificity of HS-protein binding and will describe the concept that protein binding to HS depends on the overall organization of domains within HS rather than fine structure.
Audience Academic
Author Nugent, M. A.
Spencer, J. L.
Zaia, J.
AuthorAffiliation 1 Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118
2 Department of Ophthalmology, Boston University School of Medicine, Boston, MA 02118
3 Department of Biomedical Engineering, Boston University, Boston, MA 02215
AuthorAffiliation_xml – name: 1 Department of Biochemistry, Boston University School of Medicine, Boston, MA 02118
– name: 3 Department of Biomedical Engineering, Boston University, Boston, MA 02215
– name: 2 Department of Ophthalmology, Boston University School of Medicine, Boston, MA 02118
Author_xml – sequence: 1
  givenname: M. A.
  surname: Nugent
  fullname: Nugent, M. A.
  email: mnugent@bu.edu
  organization: Department of Biochemistry, Boston University School of Medicine, Department of Ophthalmology, Boston University School of Medicine, Department of Biomedical Engineering, Boston University
– sequence: 2
  givenname: J.
  surname: Zaia
  fullname: Zaia, J.
  organization: Department of Biochemistry, Boston University School of Medicine
– sequence: 3
  givenname: J. L.
  surname: Spencer
  fullname: Spencer, J. L.
  organization: Department of Biochemistry, Boston University School of Medicine
BackLink https://www.ncbi.nlm.nih.gov/pubmed/24010836$$D View this record in MEDLINE/PubMed
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ContentType Journal Article
Copyright Pleiades Publishing, Ltd. 2013
COPYRIGHT 2013 Springer
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Keywords heparin
glycosaminoglycans
proteoglycans
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protein binding
bioinformatics
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Snippet Heparan sulfate (HS) represents a large class of linear polysaccharides that are required for the function of all mammalian physiological systems. HS is...
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SubjectTerms Animals
Antithrombin III - chemistry
Antithrombin III - metabolism
Biochemistry
Bioinformatics
Biomedical and Life Sciences
Biomedicine
Bioorganic Chemistry
Fibroblast Growth Factors - chemistry
Fibroblast Growth Factors - metabolism
Glycoproteins
Growth factors
Health aspects
Heparan sulfate
Heparitin Sulfate - chemistry
Heparitin Sulfate - metabolism
Humans
Leukocyte Elastase - antagonists & inhibitors
Leukocyte Elastase - metabolism
Life Sciences
Microbiology
Physiological aspects
Polysaccharides
Protein Binding
Protein folding
Proteins - chemistry
Proteins - metabolism
Review
Saccharides
Sulfates
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Title Heparan sulfate-protein binding specificity
URI https://link.springer.com/article/10.1134/S0006297913070055
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Volume 78
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