Neutralization of heparin-related saccharides by histidine-rich glycoprotein and platelet factor 4.

Lane, David A.; Pejler, Gunnar; Flynn, A; Thompson, Elizabeth A.; Lindahl, Ulf

doi:10.1016/s0021-9258(17)35610-7

Cited by 177 publications

(15 citation statements)

References 36 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…It will be of interest to determine whether the chemotactic factor also exerts some of the other biological properties ascribed to the platelet factors OTG and PF-4, such as affinity for heparin (26), immunoregulatory activity (27), histamine release from basophils (28), stimulation of leukocyte elastase (29), inhibition of PGI2 production in endothelial cells (30), chemotaxis for fibroblasts (31) . It will also be important to further clarify the relation between this new neutrophilchemotactic factor and other agents that have been described to possess similar activities but that are still not fully characterized (19,(32)(33)(34)(35) .…”

Section: Discussionmentioning

confidence: 99%

A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

Damme

Beeumen

Opdenakker

et al. 1988

The Journal of Experimental Medicine

295

139

View full text Add to dashboard Cite

A factor able to induce an early local inflammation in rabbit skin was detected in the supernatant of mitogen-stimulated human blood leukocytes. The factor was different from IL-1 which, although present in the supernatants, was chemically separable from the factor and induced a late rather than an early skin response. Other biological effects of the principal factor were its in vitro chemotactic effects on granulocytes and its ability to induce rapid granulocytosis upon intravenous injection in rabbits. When tested under the same conditions, IL-1 beta did not act chemotactically and induced granulocytosis at a later time. The factor was purified to homogeneity and identified by electrophoretic mobility as a protein of Mr 6,500. Amino acid sequence analysis revealed the presence of an uncontaminated NH2-terminal sequence identical to a segment of the sequence previously predicted from the cDNA clone (3-10C) copied from an mRNA isolated from human leukocytes and coding for a protein of unknown function. The NH2-terminal sequence of the factor also showed extensive homology to that of the platelet factors beta-thromboglobulin (beta TG) and platelet factor 4 (PF-4). Studies done to identify the cell source of the factor revealed that it was produced by adherent mononuclear cells but not by platelets, while the opposite was true for beta TG.

show abstract

Section: Discussionmentioning

confidence: 99%

A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

Damme

Beeumen

Opdenakker

et al. 1988

The Journal of Experimental Medicine

295

139

View full text Add to dashboard Cite

show abstract

“…The interaction of human HRG with the anticoagulant heparin (a single-stranded negatively charged polysaccharide) has been the subject of several studies. The heparin binding activity of HRG has been examined indirectly by monitoring the formation of platelet aggregates (Kindness et al, 1984) and the inhibition of proteases by antithrombin III (Lijnen et al, 1983; Lane et al, 1986) and heparin cofactor II (Tollefsen & Pestka, 1985). HRG was found to bind heparin with similar affinity to antithrombin III and platelet factor 4 (Tollefsen & Pestka, 1985) and to bind dermatan sulfate only weakly.…”

mentioning

confidence: 99%

“…HRG was found to bind heparin with similar affinity to antithrombin III and platelet factor 4 (Tollefsen & Pestka, 1985) and to bind dermatan sulfate only weakly. In addition, HRG binds heparin of molecular weight larger than 5400 better than smaller forms and has no preference for high-affinity heparin (Lane et al, 1986). In view of the known metal-binding ability of HRG, 0006-2960/87/0426-7477S01.50/0 © 1987 American Chemical Society an interesting observation in former studies (Lijnen et al, 1983; Tollefsen & Pestka, 1985; Lane et al, 1986) was that ethylenediaminetetraacetic acid (EDTA) was reported to prevent the formation of the human HRG-heparin complex.…”

mentioning

confidence: 99%

“…In addition, HRG binds heparin of molecular weight larger than 5400 better than smaller forms and has no preference for high-affinity heparin (Lane et al, 1986). In view of the known metal-binding ability of HRG, 0006-2960/87/0426-7477S01.50/0 © 1987 American Chemical Society an interesting observation in former studies (Lijnen et al, 1983; Tollefsen & Pestka, 1985; Lane et al, 1986) was that ethylenediaminetetraacetic acid (EDTA) was reported to prevent the formation of the human HRG-heparin complex. However, major questions remain as to the stoichiometry of the heparin-HRG complex, the mechanism of binding, and the location of the heparin binding site(s) on the HRG molecule.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding

Burch¹,

Blackburn²,

Morgan³

1987

Biochemistry

View full text Add to dashboard Cite

Rabbit histidine-rich glycoprotein (HRG, 94 kDa) binds heparin with high affinity (apparent Kd 60-110 nM). Eosin Y (1 equiv) bound to HRG was used as a reporter group to monitor associations of HRG with heparins of molecular mass 10, 17.5, and 30 kDa. The stoichiometries of the heparin-HRG complexes were determined by fluorescence and absorbance measurements as well as by analytical ultracentrifugation. Two types of complex form: complexes of 1 heparin:1 HRG and of 1 heparin:2 HRG. The 1:2 complex formation requires a minimum heparin chain length since 17.5-kDa but not 10-kDa heparin binds two HRG molecules. The formation of the 1:2 complexes of the larger heparin fractions is enhanced by divalent copper or zinc (1-10 equiv) bound to HRG. However, metal is not required for complex formation since all sizes of heparin examined interact tightly with HRG in the presence of ethylenediaminetetraacetic acid. Between 0.1 and 0.3 M ionic strength, both 1:1 and 1:2 complexes of heparin with HRG are progressively destabilized. No heparin-HRG complex is found at ionic strengths of 0.5 M. Between pH 8.5 and pH 6.5 both 1:2 and 1:1 complexes are found with 17.5-kDa heparin, but at pH 5.5 only 1:1 complexes are formed. The heparin-HRG interaction is progressively decreased by modification of the histidine residues of HRG, whereas modification of 22 of the 33 lysine residues of HRG has little effect.(ABSTRACT TRUNCATED AT 250 WORDS)

show abstract

“…PF4 is a glycosaminoglycan-binding protein able to neutralize the anticoagulant properties of antithrombin towards thrombin and the coagulation factor Xa [69][70][71][72].…”

Section: Platelets and Immunothrombosismentioning

confidence: 99%

Prothrombotic Phenotype in COVID-19: Focus on Platelets

Barale

Melchionda

Morotti

et al. 2021

IJMS

View full text Add to dashboard Cite

COVID-19 infection is associated with a broad spectrum of presentations, but alveolar capillary microthrombi have been described as a common finding in COVID-19 patients, appearing as a consequence of a severe endothelial injury with endothelial cell membrane disruption. These observations clearly point to the identification of a COVID-19-associated coagulopathy, which may contribute to thrombosis, multi-organ damage, and cause of severity and fatality. One significant finding that emerges in prothrombotic abnormalities observed in COVID-19 patients is that the coagulation alterations are mainly mediated by the activation of platelets and intrinsically related to viral-mediated endothelial inflammation. Beyond the well-known role in hemostasis, the ability of platelets to also release various potent cytokines and chemokines has elevated these small cells from simple cell fragments to crucial modulators in the blood, including their inflammatory functions, that have a large influence on the immune response during infectious disease. Indeed, platelets are involved in the pathogenesis of acute lung injury also by promoting NET formation and affecting vascular permeability. Specifically, the deposition by activated platelets of the chemokine platelet factor 4 at sites of inflammation promotes adhesion of neutrophils on endothelial cells and thrombogenesis, and it seems deeply involved in the phenomenon of vaccine-induced thrombocytopenia and thrombosis. Importantly, the hyperactivated platelet phenotype along with evidence of cytokine storm, high levels of P-selectin, D-dimer, and, on the other hand, decreased levels of fibrinogen, von Willebrand factor, and thrombocytopenia may be considered suitable biomarkers that distinguish the late stage of COVID-19 progression in critically ill patients.

show abstract

Neutralization of heparin-related saccharides by histidine-rich glycoprotein and platelet factor 4.

Cited by 177 publications

References 36 publications

A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

A novel, NH2-terminal sequence-characterized human monokine possessing neutrophil chemotactic, skin-reactive, and granulocytosis-promoting activity.

Further characterization of the interaction of histidine-rich glycoprotein with heparin: evidence for the binding of two molecules of histidine-rich glycoprotein by high molecular weight heparin and for the involvement of histidine residues in heparin binding

Prothrombotic Phenotype in COVID-19: Focus on Platelets

Contact Info

Product

Resources

About