Literature DB >> 8828808

Comparison of the heparanase enzymes from mouse melanoma cells, mouse macrophages, and human platelets.

L D Graham1, P A Underwood.   

Abstract

The intracellular heparanases from mouse macrophage and melanoma cells are very similar in terms of their size (60-80 kDa), pI (5.3-4.1), pH optimum (< or = 5.5), and interactions with heparin. These proteins are therefore likely to be identical, suggesting that tumour and blood cells utilise the same heparanase enzyme. The human platelet enzyme is similar to the mouse enzymes in terms of pH optimum (< or = 5.5) and pI value (5.3-4.8), but appears to be smaller in size (40-60 kDa). It also seems to differ from the mouse enzymes in aspects of its surface charge, and in its interactions with heparin. There was no indication that proteolysis was of significance for the enzymes, nor that they contained any sialic acid residues.

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Year:  1996        PMID: 8828808     DOI: 10.1080/15216549600201621

Source DB:  PubMed          Journal:  Biochem Mol Biol Int        ISSN: 1039-9712


  4 in total

1.  Evidence that platelet and tumour heparanases are similar enzymes.

Authors:  C Freeman; A M Browne; C R Parish
Journal:  Biochem J       Date:  1999-09-01       Impact factor: 3.857

2.  Expression of heparanase mRNA in anti-sense oligonucleotide-transfected human esophageal cancer EC9706 cells.

Authors:  Kui-Sheng Chen; Lan Zhang; Lin Tang; Yun-Han Zhang; Dong-Ling Gao; Liang Yan; Lei Zhang
Journal:  World J Gastroenterol       Date:  2005-08-21       Impact factor: 5.742

3.  Human platelet heparanase: purification, characterization and catalytic activity.

Authors:  C Freeman; C R Parish
Journal:  Biochem J       Date:  1998-03-15       Impact factor: 3.857

4.  Partial purification of heparanase activities in Chinese hamster ovary cells: evidence for multiple intracellular heparanases.

Authors:  K J Bame; A Hassall; C Sanderson; I Venkatesan; C Sun
Journal:  Biochem J       Date:  1998-11-15       Impact factor: 3.857

  4 in total

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