Histidine-Rich Glyco (HRG) ELISA Kit for Human

This histidine-rich glycoprotein contains two cystatin-like domains and is located in plasma and platelets. The physiological function has not been determined but it is known that the protein binds heme, dyes and divalent metal ions. The encoded protein also has a peptide that displays antimicrobial activity against C. albicans, E. coli, S. aureus, P. aeruginosa, and E. faecalis. It can inhibit rosette formation and interacts with heparin, thrombospondin and plasminogen. Two of the protein's effects, the inhibition of fibrinolysis and the reduction of inhibition of coagulation, indicate a potential prothrombotic effect. Mutations in this gene lead to thrombophilia due to abnormal histidine-rich glycoprotein levels. [provided by RefSeq, Nov 2014]

HRG: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Binds to N-sulfated polysaccharide chains on the surface of liver endothelial cells. Inhibits rosette formation. Acts as an adapter protein and is implicated in regulating many processes such as immune complex and pathogen clearance, cell chemotaxis, cell adhesion, angiogenesis, coagulation and fibrinolysis. Mediates clearance of necrotic cells through enhancing the phagocytosis of necrotic cells in an heparan sulfate-dependent pathway. This process can be regulated by the presence of certain HRG ligands such as heparin and zinc ions. Binds to IgG subclasses of immunoglobins containing kappa and lambda light chains with different affinities regulating their clearance and inhibiting the formation of insoluble immune complexes. Tethers plasminogen to the cell surface. Binds T-cells and alters the cell morphology. Modulates angiogenesis by blocking the CD6-mediated antiangiongenic effect of thrombospondins, THBS1 and THBS2. Acts as a regulator of the vascular endothelial growth factor (VEGF) signaling pathway; inhibits endothelial cell motility by reducing VEGF-induced complex formation between PXN/paxillin and ILK/integrin-linked protein kinase and by promoting inhibition of VEGF-induced tyrosine phosphorylation of focal adhesion kinases and alpha-actinins in endothelial cells. Also plays a role in the regulation of tumor angiogenesis and tumor immune surveillance. Normalizes tumor vessels and promotes antitumor immunity by polarizing tumor-associated macrophages, leading to decreased tumor growth and metastasis. Defects in HRG are the cause of thrombophilia due to histidine-rich glycoprotein deficiency (THPH11). A hemostatic disorder characterized by a tendency to thrombosis.

Protein type: Secreted, signal peptide; Secreted

Chromosomal Location of Human Ortholog: 3q27

Cellular Component: extracellular region; plasma membrane

Molecular Function: cysteine protease inhibitor activity; heme binding; heparan sulfate proteoglycan binding; heparin binding; immunoglobulin binding; metal ion binding; protein binding; receptor binding; serine-type endopeptidase inhibitor activity; zinc ion binding

Biological Process: angiogenesis; blood coagulation; chemotaxis; defense response to fungus; fibrinolysis; heme transport; negative regulation of angiogenesis; negative regulation of blood vessel endothelial cell migration; negative regulation of cell adhesion; negative regulation of cell adhesion mediated by integrin; negative regulation of cell growth; negative regulation of cell proliferation; negative regulation of fibrinolysis; platelet activation; platelet degranulation; positive regulation of apoptosis; positive regulation of focal adhesion formation; positive regulation of immune response to tumor cell; regulation of actin cytoskeleton organization and biogenesis; regulation of blood coagulation; regulation of gene expression; regulation of peptidyl-tyrosine phosphorylation; regulation of protein complex assembly

Disease: Thrombophilia Due To Histidine-rich Glycoprotein Deficiency