Interaction of heparin with annexin V

Capila, Ishan; VanderNoot, Victoria A.; Mealy, Tanya R.; Seaton, Barbara A.; Linhardt, Robert J.

doi:10.1016/s0014-5793(99)00245-8

Cited by 51 publications

(45 citation statements)

References 26 publications

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“…It has also been shown that Ca 2þ is an essential activator of a heparin degrading enzyme, heparinase I, in which the heparin-Ca 2þ complex is the true enzyme substrate, whereas Ca 2þ -free heparin is a competitive inhibitor [147]. Annexin V, an abundant anticoagulant and phospholipid binding protein binds HS in a calcium ion-dependent manner, binding via two binding sites on opposite faces of the protein [148,149]. The phospholipid binding and calcium-dependent annexin I has been reported as requiring N-and 2-O-sulfate groups for binding [150].…”

Section: Cation Binding To Heparan Sulfate/heparin and Its Effectsmentioning

confidence: 99%

Heparan sulfate and heparin interactions with proteins

Meneghetti

Hughes

Rudd

et al. 2015

J. R. Soc. Interface.

256

241

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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.

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Section: Cation Binding To Heparan Sulfate/heparin and Its Effectsmentioning

confidence: 99%

Heparan sulfate and heparin interactions with proteins

Meneghetti

Hughes

Rudd

et al. 2015

J. R. Soc. Interface.

256

241

View full text Add to dashboard Cite

show abstract

“…Among separation and interaction techniques, CE has been proved to be very attractive due to the advantages of high separation efficiency, great flexibility, simple operation, short analysis time, and low consumption of samples and buffers [9]. In addition, the interaction between molecules can be directly observed under physiological conditions, without prior immobilization steps, as is required in affinity chromatography and surface plasmon resonance spectrometry [28][29][30][31][32][33][34][35][36] that pose a problem of steric hindrance [37][38][39]. It would also be possible, by using CE, to study interactions of individual components in a mixture and to determine binding parameters simultaneously [40].…”

Section: Introductionmentioning

confidence: 99%

Separation, identification, and interaction of heparin oligosaccharides with granulocyte-colony stimulating factor using capillary electrophoresis and mass spectrometry

et al. 2005

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A capillary electrophoresis (CE) method was developed for the separation of heparin oligosaccharides compatible to study the interactions between the oligosaccharides and granulocyte-colony stimulating factor (G-CSF). Unfractionated heparin was eliminitively degraded to heparin oligosaccharides by an endolytic heparinase. The degraded smaller oligosaccharides (M(r) < 1000) were baseline-separated by CE under a 50 mM phosphate buffer (pH 9.0) in 10 min. Standard heparin disaccharides and larger oligosaccharides (1000 < M(r) < 8000) were all separated under optimized separation conditions. Compared with standard heparin disaccharides, smaller oligosaccharides contained one nonsulfated, two monosulfated, and two disulfated disaccharides, but trisulfated disaccharides were not found. The smaller oligosaccharides were also identified and molecular mass was deduced by electrospray ionization-mass spectrometry (ESI-MS). Furthermore, interactions between G-CSF and the oligosaccharides were studied by using capillary zone electrophoresis (CZE) under the above separation conditions. It was found that larger oligosaccharides could interact with G-CSF while smaller oligosaccharides were not observed to bind to G-CSF under the experimental conditions. In conclusion, the purified heparinase could selectively degrade heparin into oligosaccharides and the interaction between G-CSF and heparin was correlated with the chain length of heparin.

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“…Anx V binds with high affinity to such negatively charged phospholipids as phosphatidylserine. They also bind to another polyanion group, glycosaminoglycans, such as heparin [18][19][20]. Therefore, it is reasonable to assume that Anx V was thus adsorbed by DS bound cellulose beads because DS also contain repeating negatively charged units.…”

Section: Discussionmentioning

confidence: 99%