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Histidine-rich glycoprotein specifically binds to necrotic cells via its amino-terminal domain and facilitates necrotic cell phagocytosis

Jones, Allison; Poon, Ivan; Hulett, Mark; Parish, Christopher

Description

Cells that become necrotic or apoptotic through tissue damage or during normal cellular turnover are usually rapidly cleared from the circulation and tissues by phagocytic cells. A number of soluble proteins have been identified that facilitate the phagocytosis of apoptotic cells, but few proteins have been defined that selectively opsonize necrotic cells. Previous studies have shown that histidine-rich glycoprotein (HRG), an abundant (∼100 μg/ml) 75-kDa plasma glycoprotein, binds to cell...[Show more]

dc.contributor.authorJones, Allison
dc.contributor.authorPoon, Ivan
dc.contributor.authorHulett, Mark
dc.contributor.authorParish, Christopher
dc.date.accessioned2015-12-13T22:55:38Z
dc.identifier.issn0021-924X
dc.identifier.urihttp://hdl.handle.net/1885/82606
dc.description.abstractCells that become necrotic or apoptotic through tissue damage or during normal cellular turnover are usually rapidly cleared from the circulation and tissues by phagocytic cells. A number of soluble proteins have been identified that facilitate the phagocytosis of apoptotic cells, but few proteins have been defined that selectively opsonize necrotic cells. Previous studies have shown that histidine-rich glycoprotein (HRG), an abundant (∼100 μg/ml) 75-kDa plasma glycoprotein, binds to cell surface heparan sulfate on viable cells and cross-links other ligands, such as plasminogen, to the cell surface. In this study we have demonstrated that HRG also binds very strongly, in a heparan sulfate-independent manner, to cytoplasmic ligand(s) exposed in necrotic cells. This interaction is mediated by the amino-terminal domain of HRG and results in enhanced phagocytosis of the necrotic cells by a monocytic cell line. In contrast, it was found that HRG binds poorly to and does not opsonize early stage apoptotic cells. Thus, HRG has the unique property of selectively recognizing necrotic cells and may play an important physiological role in vivo by facilitating the uptake and clearance of necrotic, but not apoptotic, cells by phagocytes.
dc.publisherJapanese Biochemical Society
dc.sourceJournal of Biochemistry
dc.subjectKeywords: Amino acids; Cells; Cytology; Molecular structure; Physiological models; Tissue; Histidine-rich glycoprotein (HRG); Necrotic cells; Phagocytes; Plasminogen; Proteins; glycoprotein; heparan sulfate; histidine; histidine rich glycoprotein; plasminogen; uncl
dc.titleHistidine-rich glycoprotein specifically binds to necrotic cells via its amino-terminal domain and facilitates necrotic cell phagocytosis
dc.typeJournal article
local.description.notesImported from ARIES
local.description.refereedYes
local.identifier.citationvolume280
dc.date.issued2005
local.identifier.absfor110704 - Cellular Immunology
local.identifier.ariespublicationMigratedxPub10852
local.type.statusPublished Version
local.contributor.affiliationJones, Allison, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationPoon, Ivan, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationHulett, Mark, College of Medicine, Biology and Environment, ANU
local.contributor.affiliationParish, Christopher, College of Medicine, Biology and Environment, ANU
local.description.embargo2037-12-31
local.bibliographicCitation.issue42
local.bibliographicCitation.startpage35733
local.bibliographicCitation.lastpage35741
local.identifier.doi10.1074/jbc.M504384200
dc.date.updated2015-12-11T11:11:27Z
local.identifier.scopusID2-s2.0-27444447371
CollectionsANU Research Publications

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