Interaction of Glycosaminoglycans with Lipoproteinsa

Cardin, Alan D.; Jackson, Richard L.; Sparrow, Doris A.; Sparrow, James T.

doi:10.1111/j.1749-6632.1989.tb22503.x

Cited by 26 publications

(23 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Because a large number of growth factors bind to heparin with either moderate or high affinity (~10 −6 – 10 −9 M K D ), heparin-based delivery systems have proven useful for the delivery of a wide range for growth factors for different biomedical applications [21]. In the case of heparin-based systems, these interactions can also modulate the binding of growth factor to the cell surface receptor.…”

Section: Heparin Modification Of Materials For Drug Deliverymentioning

confidence: 99%

Incorporation of heparin into biomaterials

2014

View full text Add to dashboard Cite

This review provides an overview on the incorporation of heparin into biomaterials with a focus on drug delivery and the use of heparin-based biomaterials for self-assembly of polymer networks. Heparin conjugation to biomaterials was originally explored to reduce the thrombogenicity of materials in contact with blood. Many of the conjugation strategies that were developed for these applications are still popular today for other applications. More recently heparin has been conjugated to biomaterials for drug delivery applications. Many of the delivery approaches have taken advantage of the ability of heparin to bind to a wide variety of growth factors, protect them from degradation and to potentiate their interactions with cell surface receptors. More recently, the use of heparin as a base polymer for scaffold fabrication has also been explored, often utilizing non-covalent binding of heparin with peptides or proteins to promote self-assembly of hydrogel networks. This review will highlight recent advances in each of these areas.

show abstract

Section: Heparin Modification Of Materials For Drug Deliverymentioning

confidence: 99%

Incorporation of heparin into biomaterials

2014

View full text Add to dashboard Cite

show abstract

“…1857 For example, a synthetic peptide containing the consensus [-X-B-B-B-X-X-B-X-] that includes residues 3364 to 3371 of apo B-100 (T-R-K-R-G-L-K-L) binds heparin at the same ionic strength conditions as LDL 57 and corresponds to a segment of a heparin-binding CNBr fragment isolated from apo B-100. 16 Similarly, a synthetic peptide of apo E, comprising the LDL receptor binding domain 58 and having essentially the same sequence within the consensus region as the apo B-100 synthetic peptide (see Table 2), accounts for the major heparin-binding activity of apo E.…”

Section: Consensus Sequence Analyses Of Heparln-blndlng Regionsmentioning

confidence: 99%

Molecular modeling of protein-glycosaminoglycan interactions.

Cardin¹,

Weintraub²

1989

Arteriosclerosis

1,246

993

View full text Add to dashboard Cite

. Predictions were then made as to the heparln-blnding domains In endothellal cell growth factor, purpurln, and antithrombln-lll. Many of the natural sequences conforming to these consensus motifs show prominent amphlpathlc periodicities having both a-hellcal and 0-strand conformations as determined by predictive algorithms and circular dlchroism studies. The heparln-blnding domain of vttronectln was modeled and formed a hydrophlllc pocket that wrapped around and folded over a heparln octasaccharide, yielding a complementary structure. We suggest that these consensus sequence elements form potential nucleation sites for the recognition of potyanions In proteins and may provide a useful guide In identifying heparln-blnding regions In other proteins. 1112 However, the structural heterogeneity of the acidic mucopolysaccharides with respect to size, carbohydrate composition and charge, 13 and the variety of proteins that are known to bind to these molecules have complicated a detailed molecular analysis of protein-GAG interactions. The most studied system, binding of heparin to a specific domain or site on human antithrombin-lll (AT-III), involves a unique carbohydrate structure representing only a fraction of the total heparin. 14 The exact amino acid residues on AT-III or other proteins which comprise their heparin-binding domains have not been fully elucidated.To understand the molecular recognition of heparin by proteins, we recently determined the structure of the heparin-binding regions of apolipoprotein (apo) B-100, the major protein constituent of human plasma low density Received June 10, 1988; revision accepted September 14, 1988. lipoproteins (LDL). The structure of these regions was of particular interest as we hypothesized that they could mediate the interaction of LDL with acidic mucopolysaccharides of arterial tissue. We showed that LDL contains five to seven heparin-binding sites on the lipoprotein surface. 15 The heparin-binding cyanogen bromide peptides of apo B-100 were isolated, and their amino acid sequences were determined. 16 These peptides account for five domains of high positive charge density that we suggest mediate the lipoprotein's interaction with glycosaminoglycans. These same regions were also identified by Weisgraber and Rail. 17 We noticed 16 that these domains in apo B-100 have a sequence similarity to the heparinbinding regions of apo E 1819 and human vitronectin (Vn) 20 with respect to the organization of basic and hydropathic residues. The present study extends our initial observations to other proteins whose functions are modified by heparin. We show that all these proteins contain unique consensus sequences of amino acid residues that are potentially involved in heparin binding. MethodsSecondary structure predictions of Vn peptide conformations were performed by the MSEQ program 21 based on Chou-Fasman algorithms 22 and by the method of Gamier et al. 23 Both methods gave comparable predictions of predominant /3-strand and 0-tum structures, and circular dichroism studies on...

show abstract

“…Early work, based on heparin binding protein sequence comparison, led to the proposition of two binding consensus sequences, X BB X B X and X BBB XX B X , where B stands for a basic, and X is for a neutral/hydrophobic amino acid (38). This, however, does not exclude that patterns of positively charged residues comprise distant amino acids clustered by the protein folding (39).…”

Section: Resultsmentioning

confidence: 99%

“…Heparin (6 kDa) (Sigma) was biotinylated at the reducing end (Biotin-LC-hydrazide, Pierce) as described previously (38) and immobilized on a CM4 Biacore sensorchip (GE Healthcare) using an amine coupling kit. Briefly, a Biacore 3000 system (GE Healthcare) was equilibrated with running buffer HBS-EP (10 m m HEPES, 150 m m NaCl, 3 m m EDTA, 0.05% surfactant P20, pH 7.4) at 5 μl/min, and the temperature was maintained at 25 °C.…”

Section: Methodsmentioning

confidence: 99%

Transglutaminase-2 Interaction with Heparin

Lortat‐Jacob¹,

Burhan²,

Scarpellini³

et al. 2012

Journal of Biological Chemistry

View full text Add to dashboard Cite

Background: Extracellular transglutaminase-2 binds heparan sulfate and has adhesive/signaling pro-fibrotic functions.Results: Two clusters of basic residues, distal in the linear sequence of transglutaminase-2, are required for heparin binding and cell adhesion.Conclusion: Folding of the transglutaminase-2 protein brings basic residues in close proximity to form a functional heparin binding domain.Significance: Mapping the heparan sulfate binding domain will enhance design of transglutaminase-2 inhibitors.

show abstract

Interaction of Glycosaminoglycans with Lipoproteinsa

Cited by 26 publications

References 23 publications

Incorporation of heparin into biomaterials

Incorporation of heparin into biomaterials

Molecular modeling of protein-glycosaminoglycan interactions.

Transglutaminase-2 Interaction with Heparin

Contact Info

Product

Resources

About