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Histidine-rich glycoprotein binds heparanase and regulates its enzymatic activity and cell surface interactions

Date

Authors

Poon, Ivan

Yee, Dean

Jones, Allison

Wood, Robert

Simon Davis (S Davis), David

Freeman, Craig

Hulett, Mark

Parish, Christopher

Publisher

Pergamon-Elsevier Ltd

Abstract

Heparanase, an endo-β-d-glucuronidase, is involved in numerous normal physiological and pathological processes, such as inflammation, wound healing and tumour metastasis/angiogenesis, through its ability to mediate the degradation of heparan sulfate, a k

Keywords

Keywords: cell surface receptor; heparanase; histidine rich glycoprotein; plasma protein; unclassified drug; animal cell; animal cell culture; article; enzyme activity; enzyme assay; enzyme linked immunosorbent assay; extracellular matrix; flow cytometry; genetic t Heparan sulfate; Heparanase; Histidine-rich glycoprotein

URI

http://hdl.handle.net/1885/36395

Collections

ANU Research Publications

Source

The International Journal of Biochemistry and Cell Biology

Type

Journal article

DOI

10.1016/j.biocel.2010.05.008

Restricted until

2037-12-31

Downloads

File

Description

01_Poon_Histidine-rich_glycoprotein_2010.pdf (520.94 KB)