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CD36- TSP- HRGP interactions in the regulation of angiogenesis. Paper-13446260.
Type 3 cystatins; fetuins, kininogen and histidine-rich glycoprotein. Paper-13656386.
We found that binding of HRGP to TSP-1 was similarly mediated by TSP type I repeats. Paper-8689729.
Their results show that HRG, like PF 4, has an affinity, not only for heparin, but also for DS. Paper-7331981.
In contrast, HPRG abrogates the stimulatory effects of fibrinogen on Plg activation in solution. Paper-10911023.
Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1. Paper-8689729.
Effects of histidine-proline-rich glycoprotein on plasminogen activation in solution and on surfaces. Paper-10911023.
In addition, HRG was able to displace biologically active bFGF from the ECM. Paper-139834.
These results strongly suggest additional physiological functions of HRG and PF4 as modulators of PCI. Paper-7523895.
The heparin-neutralizing ability of HRG in the thrombin inhibition by PCI was not affected by Ca2+. Paper-7523895.
No species differences were found, as either rabbit or human HPRG bound readily to rabbit or human PLG. Paper-172840.
Platelet thrombospondin forms a trimolecular complex with plasminogen and histidine-rich glycoprotein. Paper-5079045.
ERK activation remained elevated for 2 h following high doses of HRG which induce differentiation. Paper-1577501.
Common variants of large effect in F12, KNG1, and HRG are associated with activated partial thromboplastin time. Paper-15232576.
HPRG also augments the increase in Plg activation caused by fibrinogen fragments either in solution or on GAG surfaces. Paper-10911023.
The heparin-binding site(s) of histidine-rich glycoprotein as suggested by sequence homology with antithrombin III. Paper-5330668.
Three members of the human cystatin gene superfamily, AHSG, HRG, and KNG, map within one megabase of genomic DNA at 3q27. Paper-220647.
Human histidine-rich glycoprotein: simultaneous purification with antithrombin III and characterization of its gross structure. Paper-5006659.
Plasminogen is tethered with high affinity to the cell surface by the plasma protein, histidine-rich glycoprotein. Paper-10643946.
In this study we have demonstrated that purified human platelet TSP formed a trimolecular complex with human Plg and HRGP. Paper-5079045.
In fact, HRG is 10 times less effective than PF 4 in neutralizing the 50% antithrombin activity of HC II in the presence of DS. Paper-7331981.
In contrast, a transient 5 min peak of ERK activation in response to doses of HRG which induce proliferation was observed. Paper-1577501.
Similarly, interferon-gamma ( IFN-gamma) was not capable of blocking the functional activity of HRG. Paper-7471719.
The ternary complex model implies that, HRG being responsible for efficient G protein activation, it should be as stable as possible. Paper-10490383.
No correlation between HRGP level and t-PA- mediated plasminogen activation was observed.(ABSTRACT TRUNCATED AT 250 WORDS) Paper-7862153.
Platelet factor 4 abolishes the activation of heparin cofactor II by dermatan sulfate, but plasma histidine-rich glycoprotein does not. Paper-11924208.
Plasminogen binding by alpha 2-antiplasmin and histidine-rich glycoprotein does not inhibit plasminogen activation at the surface of fibrin. Paper-7453301.
Interaction of histidine-proline-rich glycoprotein with plasminogen: effect of ligands, pH, ionic strength, and chemical modification. Paper-172840.
Interaction between histidine-rich glycoprotein and platelet factor 4 with dermatan sulfate and low-molecular-weight dermatan sulfate. Paper-7331981.
However, both intact and plasmin-cleaved HRG enhanced the binding of plasminogen to heparin-coated surfaces to a similar extent. Paper-14059337.
At saturation the relative molar stoichiometry of Plg:TPA was 3:1 within the TSP-containing complexes and 1:1 within HRGP-containing complexes. Paper-5126593.
Familial association of high levels of histidine-rich glycoprotein and plasminogen activator inhibitor-1 with venous thromboembolism. Paper-7862153.
In contrast to HRG, there was no significant difference in the heparin-neutralizing ability of PF4 in the presence or absence of 1 mM Ca2+. Paper-7523895.
A recent study revealed that HRG suppressed heparin-dependent basic fibroblast growth factor (bFGF)-induced angiogenesis. Paper-14073116.
Of the ligands of HPRG tested, mesoheme (20 microM) but not heparin (M(r) 10,000, 10 microM) inhibits the formation of the HPRG- PLG complex. Paper-172840.
Kinetic analysis demonstrated a marked increase in the affinity of TPA for plasminogen in the presence of surface- associated TSP or HRGP. Paper-5126593.
Apparent Kd values were approximately 12-36 nM for the interaction of TPA with TSP- Plg complexes and 15-31 nM with HRGP- Plg complexes. Paper-5126593.
HRGP covalently cross- linked to Sepharose 4B simultaneously bound both 125I- TSP and 131I- Plg, confirming trimolecular complex formation. Paper-5079045.
The authors studied the interaction of DS and low molecular weight DS, in a purified system with HRG, platelet factor 4 ( PF 4), and with HC II. Paper-7331981.
These studies suggest that HRG regulates macrophage function via a novel pathway different from that of heparin or IFN-gamma. Paper-7471719.
Histidine-proline rich glycoprotein ( HPRG) binds and transduces anti-angiogenic signals through cell surface tropomyosin on endothelial cells. Paper-10533417.
HRGP colocalized with TSP-1 in the stroma of human breast cancer specimens, and this interaction masked the antiangiogenic epitope of TSP-1. Paper-8689729.
Plasmin-mediated cleavage partially inhibited HRG binding to cell surface HS, but enhanced HRG binding to necrotic cells and to plasminogen. Paper-14059337.
These data indicate that sustained activation of the MEK/ ERK pathway is both essential and sufficient for HRG-induced differentiation of AU565 cells. Paper-1577501.
Effects of zinc and calcium ions on the heparin-neutralizing abilities of histidine-rich glycoprotein ( HRG) and platelet factor 4 ( PF4) were examined. Paper-7523895.
At least two binding sites for HPRG, tropomyosin and heparan sulfate proteoglycans (HSPs), were identified on the surface of FGF-2-activated endothelial cells. Paper-10533417.
The activation of Glu-plasminogen in alpha 2-AP-depleted plasma containing a normal concentration of HRGP produced a time-dependent increase in the generation of plasmin. Paper-7453301.
We have shown previously that HRGP binds with high affinity to thrombospondin-1 ( TSP-1), a homotrimeric glycoprotein that is a potent inhibitor of angiogenesis. Paper-8689729.
These studies suggest that HRGP can modulate the antiangiogenic activity of TSP-1, and identify a potential mechanism of resistance to the antiangiogenic effect of TSP-1. Paper-8689729.
These results suggest that HPRG binds to endothelial cell surface tropomyosin which at least partially mediates the antiangiogenic effects of HPRG. Paper-10533417.
The stoichiometry and dissociation constant (KD) of the complex were determined from the equilibrium distribution of fluorescein-isothiocyanate-labeled PLG in the presence of HPRG. Paper-172840.
In terms of their relative binding affinity for cell-surface HSPGs, the hierarchy was shown to be PF4 > or = bFGF > aFGF = cHRG > hHRG. Paper-139834.
These observations demonstrate that HPRG can act as either a positive or negative effector of Plg activation in vitro and may serve as a modulator of fibrinolysis in vivo. Paper-10911023.
The purpose of this study was to assay the plasma levels of tPA, PAI, histidine-rich glycoprotein ( HRG), and other fibrinolytic proteins in 15 severely stressed newborns. Paper-7491617.
Histidine-rich glycoprotein and platelet factor 4 mask heparan sulfate proteoglycans recognized by acidic and basic fibroblast growth factor. Paper-139834.
In contrast, the addition of 1.5 microM- HRGP to HRGP-depleted plasma containing a normal amount of alpha 2-AP produced only a modest (17%) decrease in the amount of plasmin(ogen) bound. Paper-7453301.
Histidine-proline-rich glycoprotein ( HPRG) has long been known to associate with plasminogen ( Plg) in solution, but the consequences of this interaction have not been defined. Paper-10911023.
Thus proteolytic cleavage of HRG by plasmin may provide a feedback mechanism to regulate the effects of HRG on the plasminogen/plasmin system and other functions of HRG. Paper-14059337.
Here we show, based on optical biosensor analyses, that immobilized HRG interacts with soluble plasminogen with high affinity and with an extremely slow dissociation rate. Paper-10643946.
HRG has been shown to function as an adaptor molecule to tether plasminogen to GAG (glycosaminoglycan)-bearing surfaces and to regulate plasminogen activation via various mechanisms. Paper-14059337.
In assays performed in vitro of endothelial cell migration and tube formation, and in vivo corneal angiogenesis assays, HRGP inhibited the antiangiogenic effect of TSP-1. Paper-8689729.
Indeed, both HRG and PF4, at physiological concentrations, were shown to effectively inhibit the binding of 125I- aFGF and 125I- bFGF to ECM. Paper-139834.
The activation of Plg to plasmin by TPA on TSP- and HRGP-coated surfaces was studied using a synthetic fluorometric plasmin substrate (D-Val-Leu-Lys-7-amino-4-trifluoromethyl coumarin). Paper-5126593.
The interpretation of the significance of these observations suggests a physiological mutual dependence between skeletal muscle HPRG and AMPD polypeptides with regard to their stability. Paper-14726502.
Addition of PLG shifts the S-value of 125I- labeled HPRG from 4.8S to 6.8S, providing the first direct evidence that HPRG associates with the zymogen form of plasmin in solution. Paper-172840.
The simple and simultaneous purification of histidine-rich glycoprotein ( HRG) and antithrombin III (AT III) from human plasma and gross structural characterization of HRG have been performed. Paper-5006659.
These results indicate that HPRG has independent binding sites for heparin and PLG and confirm that one or more lysine residues of HPRG are involved in its recognition by PLG. Paper-172840.
Immunohistochemical analysis of human skeletal muscle AMP deaminase deficiency. Evidence of a correlation between the muscle HPRG content and the level of the residual AMP deaminase activity. Paper-14726502.
Translocation of tropomyosin to the surface of HUVEC occurred in response to FGF-2, and the anti-angiogenic activity of HPRG in a Matrigel plug model was partially inhibited by soluble tropomyosin. Paper-10533417.
Modulation of protein C inhibitor activity by histidine-rich glycoprotein and platelet factor 4: role of zinc and calcium ions in the heparin-neutralizing ability of histidine-rich glycoprotein. Paper-7523895.
The measured upwelling radiance was converted to % reflectance; and we integrated the hyperspectral reflectance to match the Red and NIR bands of three satellite sensors: Landsat 7 ETM, SPOT 5 HRG, and ASTER. Paper-13548169.
The sample consists of the adenosine monophosphate deaminase ( AMPD) histidine proline rich glycoprotein ( HPRG) complex that contains 3-4 Zn(II) ions per dimer of approximately 320 kDa molecular weight. Paper-9822831.
Specifically, Plg complexed with HPRG on a GAG surface is more readily activated by tissue-type Plg activator than free Plg, with a 10-fold difference in apparent catalytic efficiency (kcat/Km). Paper-10911023.
Complex formation was detected by a specific binding enzyme-linked immunosorbent assay ( ELISA) which demonstrated simultaneous binding of fluid-phase Plg and HRGP to TSP adsorbed to microtitration wells. Paper-5079045.
The TSP- HRGP- Plg complex bound a similar amount of heparin as the TSP- HRGP complex, demonstrating that the HRGP within the trimolecular complex maintained functional capability. Paper-5079045.
Complex formation of locally released tissue plasminogen activator with Plg immobilized on TSP or HRGP surfaces may thus play an important role in effecting proteolytic events in nonfibrin-containing microenvironments. Paper-5126593.
This review describes the properties of four structurally related, abundant plasma proteins denoted fetuin-A/alpha-2-Heremans Schmid-glycoprotein (AHSG), fetuin-B (FETUB), kininogen ( KNG) and histidine-rich glycoprotein ( HRG). Paper-13656386.
A high degree of sequence homology has been found between the N-terminal region of histidine-rich glycoprotein ( HRG) and that of antithrombin III (AT III) where the putative heparin-binding site of AT III is located. Paper-5330668.
High levels of histidine-rich glycoprotein ( HRGP) and plasminogen activator inhibitor-1 ( PAI-1) have been claimed to contribute to the hypofibrinolytic state observed in patients with venous thrombosis. Paper-7862153.
HRG was also shown to tether plasminogen to cell surfaces, with this interaction being potentiated by elevated Zn(2+) levels and low pH, conditions that prevail at sites of tissue injury, tumor growth, and angiogenesis. Paper-10643946.
On the basis of these findings, it is proposed that HRG and PF4 may act as positive regulators of FGF activity by displacing FGF from the ECM or basement membrane and making FGF available to responsive cells. Paper-139834.
In conclusion, HRGP330, which we define as the minimal antiangiogenic domain of HRGP, exerts its effects through signal transduction targeting focal adhesions, thereby interrupting VEGF-induced endothelial cell motility. Paper-11320446.
Thus, HRG, PF4, aFGF, and bFGF all interact with the same HS chains on the 3T3 cell surface, either binding to the same or binding to adjacent saccharide sequences on the chains. Paper-139834.
In contrast, the enzyme model suggests that although a limited stabilization of HRG facilitates GDP release, HRG should not be "too stable" as this might trap the G protein in an inactive state and actually hinder G protein activation. Paper-10490383.
Here we show that HPRG adsorbed to a glycosaminoglycan (GAG) surface also binds Plg with a Kd value of 0.7 micromol/l. Moreover, we present evidence that HPRG acts as a modulator of the activation of Plg by tissue-type Plg activator. Paper-10911023.
Thrombospondin ( TSP), a multifunctional alpha-granule glycoprotein of platelets, binds fibrinogen, fibronectin, heparin, and histidine-rich glycoprotein and thus may play an important role in regulating thrombotic influences at vessel surfaces. Paper-4810289.
The association of plasma histidine-proline-rich glycoprotein ( HPRG) with plasminogen ( PLG) was examined using a sucrose density gradient assay in order to evaluate the effects of several relevant conditions on complex formation. Paper-172840.
Previous studies have reported that the plasma protein, histidine-rich glycoprotein ( HRG), interacts with plasminogen and cell surfaces, raising the possibility that HRG may immobilize plasminogen/plasmin to cell surfaces. Paper-10643946.
While neither ligand inhibited complex formation of the other with TSP, 10 mM epsilon-amino-n-caproic acid selectively blocked incorporation of Plg into the complex, suggesting that TSP contains independent binding sites for Plg and HRGP. Paper-5079045.
Furthermore, the HRG- plasminogen interaction is lysine-dissociable and involves predominately the amino-terminal domain of HRG, and the fifth kringle domain of plasminogen, but not the carboxyl-terminal lysine of HRG. Paper-10643946.
HRG ( histidine-rich glycoprotein), a relatively abundant (approx. 100-150 microg/ml) plasma glycoprotein, has a multi-domain structure that can interact with many ligands, including Zn2+, heparin, HS ( heparan sulfate) and plasminogen. Paper-14059337.
APC-resistance (FV:Q506), protein C, protein S, antithrombin, heparin cofactor II ( HCII), histidine-rich glycoprotein ( HRGP), and prothrombin (F.II), factor XII (F.XII), plasminogen, homocysteine and lipoprotein (a) (Lp(a)) were investigated. Paper-2085622.
There is a controversy about whether or not histidine-rich glycoprotein ( HRG), the most abundant plasma protein with glycosaminoglycans-neutralizing capacity, is able to prevent the inhibition of human thrombin by heparin cofactor II ( HC II) in the presence of dermatan sulfate (DS). Paper-7331981.
We conducted a genome-wide association study for aPTT and identified significant associations with SNPs in three coagulation cascade genes, F12 (rs2731672, combined p = 2.16 x 10(-30)), KNG1 (rs710446, combined p = 9.52 x 10(-22)), and HRG (rs9898, combined p = 1.34 x 10(-11)). Paper-15232576.
Based on these data we propose that HRG acts as a soluble adaptor molecule that binds to cells at sites of tissue injury, tumor growth, and angiogenesis, providing a high affinity receptor for tethering plasminogen to the cell surface and thereby enhancing the migratory potential of cells. Paper-10643946.
The patients affected by Primary and Coincidental AMPD deficiency, which were characterized by an absence of enzyme activity and AMPD immunoreactivity, showed the lowest HPRG immunoreactivity that was clearly detectable by Western blot analysis, but not by immunohistochemistry. Paper-14726502.
In this study, we demonstrate that HPRG binds with high affinity to FGF-2- stimulated human umbilical vein endothelial cells (HUVEC) and immobilized tropomyosin in a Zn2+ or pH-dependent manner, and that this interaction is mediated by the H/ P domain of HPRG. Paper-10533417.
Thrombospondin ( TSP), a multifunctional alpha-granule glycoprotein of human platelets binds fibrinogen, fibronectin, heparin, histidine-rich glycoprotein ( HRGP), and plasminogen ( Plg), and thus, may play an important role in regulating thrombotic influences at vessel surfaces. Paper-5079045.
Ternary complex formation of tissue plasminogen activator (TPA) and plasminogen ( Plg) with thrombospondin ( TSP) or histidine-rich glycoprotein ( HRGP) has been demonstrated using an enzyme-linked immunosorbent assay, an affinity bead assay, and a rocket immunoelectrophoresis assay. Paper-5126593.
It can be concluded that interference of the binding of plasminogen to fibrin by alpha 2-AP during plasminogen activation, does not play a significant role in inhibition of fibrinolysis, and that the plasminogen-binding effect of HRGP, if any, is obscured by the important inhibitory effect of alpha 2-AP. Paper-7453301.
To determine whether plasminogen binding by HRGP may influence plasminogen activation, we studied the fibrinolytic activity of members of this family cohort with a system that detects modifications in plasmin generation by proteins interfering with the binding of plasminogen to fibrin. Paper-7862153.
The microsatellite marker D16Mit2, which has the strongest linkage to skin tumor susceptibility, was used to screen a bacterial artificial chromosome (BAC) library, leading to the identification of the histidine-rich glycoprotein ( Hrg) and Fetuin-B as the most tightly linked genes. Paper-10653395.
HPRG is evolutionarily, functionally and structurally related to cleaved high molecular weight kininogen (HKa), an anti-angiogenic polypeptide that stimulates apoptosis of proliferating endothelial cells through binding to cell-surface tropomyosin (Zhang J-C, et al. Proc Natl Acad Sci USA 2002; 99: 12224-9). Paper-10533417.
Eight proteins, transthyretin ( TTHY), ceruloplasmin ( CERU), afamin (AFAM), alpha-1-microglobulin (AMBP), apolipoprotein E (APOE), serum amyloid P-component (SAMP), histidine-rich glycoprotein ( HRG) and alpha-1-antitrypsin ( A1AT) were up-regulated and one, clusterin ( CLUS), down-regulated. Paper-12892046.
Because of the known evolutionary and structural relationship of KNG to other members of the cystatin gene superfamily, we tested the physical linkage of the genes encoding alpha-2HS-glycoprotein ( AHSG), KNG, and histidine-rich glycoprotein ( HRG), all of which were previously mapped to the long arm of chromosome 3. Paper-220647.
Heterozygous FV:Q506 was found in combination with heterozygous type I deficiency states of protein C (n = 2), protein S (n = 13), antithrombin (n = 8) and HCII (n = 1), increased Lp(a) (n = 13), and once each with elevated levels of F.II, moderate hyperhomocysteinemia, fibrinogen concentrations > 700 mg/dl and increased HRGP. Paper-2085622.
Significant amounts of plasmin were generated from the TSP- HRGP- Plg complex (equivalent to that from the TSP- Plg complex), but the rate of plasmin generation from the trimolecular complex was greater than from the bimolecular complex, suggesting an important interaction of HRGP with Plg when both are complexed to TSP. Paper-5079045.
alpha 2-antiplasmin ( alpha 2-AP) exerts its inhibitory effect on fibrinolysis by rapidly inhibiting the plasmin evolved; in addition, it has been suggested that interference with the binding of plasminogen to fibrin, a function shared with histidine-rich glycoprotein ( HRGP), may also be significant in inhibition of fibrinolysis. Paper-7453301.
These synonyms are used for gene HRG (histidine-rich glycoprotein): HRGP, HPRG, Histidine-rich glycoprotein, Histidine-proline-rich glycoprotein, DKFZp779H1622.
These accession numbers are used for gene HRG: M13149 (NCBI_GENBANK__AC), D3DNU7 (UNIPROT__AC), BC150591 (NCBI_GENBANK__AC), B9EK35 (UNIPROT__AC).
HRG is a homologue of HRG (histidine-rich glycoprotein) from Pan troglodytes.
HRG is a homologue of HRG (histidine-rich glycoprotein) from Bos taurus.
HRG is a homologue of HRG (histidine-rich glycoprotein) from Gallus gallus.
HRG is a homologue of Hrg (histidine-rich glycoprotein) from Mus musculus.
HRG is a homologue of Hrg (histidine-rich glycoprotein) from Rattus norvegicus.
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