| Protein disulfide isomerase cleaves allosteric disulfides in histidine-rich glycoprotein to regulate thrombosis. | Protein disulfide isomerase cleaves allosteric disulfides in histidine-rich glycoprotein to regulate thrombosis.
Lv K, Chen S, Xu X, Chiu J, Wang HJ, Han Y, Yang X, Bowley SR, Wang H, Tang Z, Tang N, Yang A, Yang S, Wang J, Jin S, Wu Y, Schmaier AH, Ju LA, Hogg PJ, Fang C., Free PMC Article | 04/30/2024 |
| Histidine-rich glycoprotein in metabolic dysfunction-associated steatohepatitis-related disease progression and liver carcinogenesis. | Histidine-rich glycoprotein in metabolic dysfunction-associated steatohepatitis-related disease progression and liver carcinogenesis.
Foglia B, Sutti S, Cannito S, Rosso C, Maggiora M, Casalino A, Bocca C, Novo E, Protopapa F, Ramavath NN, Provera A, Gambella A, Bugianesi E, Tacke F, Albano E, Parola M., Free PMC Article | 03/14/2024 |
| Other HBPs such as alpha 2-HS glycoprotein (AHSG) and histidine-rich glycoprotein (HRG) need further investigation for potential applications in the management of Acute pancreatitis (AP) . Pancreas HBPs are extracellular and so easily accessible and are potential drug targets in AP, whereas plasma HBPs represent potential biomarkers for AP. | The heparin-binding proteome in normal pancreas and murine experimental acute pancreatitis.
Nunes QM, Su D, Brownridge PJ, Simpson DM, Sun C, Li Y, Bui TP, Zhang X, Huang W, Rigden DJ, Beynon RJ, Sutton R, Fernig DG., Free PMC Article | 02/22/2020 |
| HRG binds to alpha2 integrin through low-affinity interactions in a heparin sulfate-independent manner, thereby blocking endothelial cells adhesion to collagen I. | Histidine-rich glycoprotein blocks collagen-binding integrins and adhesion of endothelial cells through low-affinity interaction with α2 integrin.
Roche F, Sipilä K, Honjo S, Johansson S, Tugues S, Heino J, Claesson-Welsh L. | 09/10/2016 |
| Mice deficient in HRG have normal hemostasis, but demonstrate accelerated thrombosis via the contact system. | Arterial thrombosis is accelerated in mice deficient in histidine-rich glycoprotein.
Vu TT, Zhou J, Leslie BA, Stafford AR, Fredenburgh JC, Ni R, Qiao S, Vaezzadeh N, Jahnen-Dechent W, Monia BP, Gross PL, Weitz JI., Free PMC Article | 07/4/2015 |
| mononuclear phagocytes have specific binding sites for HRG and that these cells are essential for uptake of HRG from blood and distribution of HRG in tissues. Thus, inflammatory cells mediate the effect of HRG on tumor growth and metastatic spread. | Histidine-rich glycoprotein uptake and turnover is mediated by mononuclear phagocytes.
Tugues S, Roche F, Noguer O, Orlova A, Bhoi S, Padhan N, Akerud P, Honjo S, Selvaraju RK, Mazzone M, Tolmachev V, Claesson-Welsh L., Free PMC Article | 06/20/2015 |
| Results show that HRG is a novel transcriptional target gene of FXR in human hepatoma cells, human upcyteVR primary hepatocytes and 3D human liver microtissues in vitro and in mouse liver in vivo. | The nuclear bile acid receptor FXR controls the liver derived tumor suppressor histidine-rich glycoprotein.
Deuschle U, Birkel M, Hambruch E, Hornberger M, Kinzel O, Perović-Ottstadt S, Schulz A, Hahn U, Burnet M, Kremoser C. | 06/6/2015 |
| HRG-deficiency promotes tumor progression via enhanced platelet activity. HRG is a potent tumor suppressor, with capacity to attenuate the angiogenic switch, tumor growth, EMT and subsequent metastatic spread, by regulating platelet activity. | HRG regulates tumor progression, epithelial to mesenchymal transition and metastasis via platelet-induced signaling in the pre-tumorigenic microenvironment.
Cedervall J, Zhang Y, Ringvall M, Thulin A, Moustakas A, Jahnen-Dechent W, Siegbahn A, Olsson AK. | 05/3/2014 |
| CD36-mediated anti-angiogenic activity has context-dependent role in the tumor microenvironment in the presence of TSP-1 while HRG modulates this activity. | Context dependent role of the CD36--thrombospondin--histidine-rich glycoprotein axis in tumor angiogenesis and growth.
Hale JS, Li M, Sinyuk M, Jahnen-Dechent W, Lathia JD, Silverstein RL., Free PMC Article | 03/30/2013 |
| HRG loss influences macrophage gene regulation, leading to excessive stimulation of tumor angiogenesis, suppression of tumor immune response, and increased tumor growth and metastatic spread | Genetic deficiency in plasma protein HRG enhances tumor growth and metastasis by exacerbating immune escape and vessel abnormalization.
Tugues S, Honjo S, König C, Noguer O, Hedlund M, Botling J, Deschoemaeker S, Wenes M, Rolny C, Jahnen-Dechent W, Mazzone M, Claesson-Welsh L. | 06/2/2012 |
| the identification and characterization of a novel peptide, VTIP-peptide (VTIP-P), which binds and enhances the activation of CREM/CREB | Identification and characterization of a novel peptide interacting with cAMP-responsive elements binding and cAMP-responsive elements modulator in mouse liver.
Brunacci C, Piobbico D, Bartoli D, Castelli M, Pieroni S, Bellet MM, Viola-Magni M, Della Fazia MA, Servillo G. | 05/11/2011 |
| role for HRG as a regulator of inflammation and in the defense at the local site of bacterial infection | Histidine-rich glycoprotein promotes bacterial entrapment in clots and decreases mortality in a mouse model of sepsis.
Shannon O, Rydengård V, Schmidtchen A, Mörgelin M, Alm P, Sørensen OE, Björck L. | 10/30/2010 |
| antifungal role of HRG in innate immunity | Histidine-rich glycoprotein protects from systemic Candida infection.
Rydengård V, Shannon O, Lundqvist K, Kacprzyk L, Chalupka A, Olsson AK, Mörgelin M, Jahnen-Dechent W, Malmsten M, Schmidtchen A., Free PMC Article | 01/21/2010 |
| CD36 mediates the antiangiogenic effect of thrombospondin-2, which is modulated by histidine-rich glycoprotein | The antiangiogenic effect of thrombospondin-2 is mediated by CD36 and modulated by histidine-rich glycoprotein.
Simantov R, Febbraio M, Silverstein RL. | 01/21/2010 |
| HRG plays a role as both an anticoagulant and an antifibrinolytic modifier, and may regulate platelet function in vivo | Enhanced blood coagulation and fibrinolysis in mice lacking histidine-rich glycoprotein (HRG).
Tsuchida-Straeten N, Ensslen S, Schäfer C, Wöltje M, Denecke B, Moser M, Gräber S, Wakabayashi S, Koide T, Jahnen-Dechent W. | 01/21/2010 |
| HRG acts as a soluble adaptor molecule that binds to cells at sites of tissue injury, tumor growth, and angiogenesis | Plasminogen is tethered with high affinity to the cell surface by the plasma protein, histidine-rich glycoprotein.
Jones AL, Hulett MD, Altin JG, Hogg P, Parish CR. | 01/21/2010 |