Hypoxia increases heparanase-dependent tumor cell invasion, which can be inhibited by antiheparanase antibodies

Cancer Research

Volumn 64, Issue 11, 2004, Pages 3928-3933

  He, Xiaotong ^a   Brenchley, Paul E C ^b   Jayson, Gordon C ^a   Hampson, Lynne ^a   Davies, John ^b   Hampson, Ian N ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b MANCHESTER ROYAL INFIRMARY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; HEPARANASE; HEPARANASE ANTIBODY; OXYGEN; UNCLASSIFIED DRUG;

ARTICLE; CANCER INVASION; CELL GROWTH; CONTROLLED STUDY; ENZYME ACTIVITY; GENETIC TRANSFECTION; HUMAN; HUMAN CELL; HYPOXIA; NUCLEOTIDE SEQUENCE; OVARY CARCINOMA; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; TUMOR CELL;

ANTIBODIES; CELL HYPOXIA; CELL LINE, TUMOR; DNA, ANTISENSE; ENZYME ACTIVATION; FEMALE; GLUCURONIDASE; HUMANS; NEOPLASM INVASIVENESS; OVARIAN NEOPLASMS; OXYGEN; TRANSFECTION;

EID: 2542634131     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-03-2718     Document Type: Article

References (30)

1. David G, Bernfield M. The emerging roles of cell surface heparan sulfate proteoglycans. Matrix Biol 1998;17:461-3.
2. Bai X, Bame KJ, Habuchi H, Kimata K, Esko JD. Turnover of heparan sulfate depends on 2-O-sulfation of uronic acids. J Biol Chem 1997;272:23172-9.
3. Pikas DS, Li JP, Vlodavsky I, Lindahl U. Substrate specificity of heparanases from human hepatoma and platelets. J Biol Chem 1998;273:18770-7.
4. Vlodavsky I, Goldshmidt O, Zcharia E, et al. Mammalian heparanase: involvement in cancer metastasis, angiogenesis and normal development. Semin Cancer Biol 2002;12:121-9.
5. Vlodavsky I, Friedmann Y, Elkin M, et al. Mammalian heparanase: gene cloning, expression and function in tumor progression and metastasis. Nat Med 1999;5:793-802.
6. Hulett MD, Freeman C, Hamdorf BJ, Baker RT, Harris MJ, Parish CR. Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis. Nat Med 1999;5:803-9.
7. Toyoshima M, Nakajima M. Human heparanase: purification, characterization, cloning, and expression. J Biol Chem 1999;274:24153-60.
8. Kussie PH, Hulmes JD, Ludwig DL, et al. Cloning and functional expression of a human heparanase gene. Biochem Biophys Res Commun 1999;261:183-7.
9. Fairbanks MB, Mildner AM, Leone JW, et al. Processing of the human heparanase precursor and evidence that the active enzyme is a heterodimer. J Biol Chem 1999;274:29587-90.
10. McKenzie E, Young K, Hircock M, et al. Biochemical characterisation of the active heterodimer form of human heparanase (Hpa1) protein expressed in insect cells. Biochem J 2003;373(Pt 2):423-35.
11. Friedl P, Wolf K. Tumour-cell invasion and migration: diversity and escape mechanisms. Nat Rev Cancer 2003;3:362-74.
12. Subarsky P, Hill RP. The hypoxic tumour microenvironment and metastatic progression. Clin Exp Metastasis 2003;20:237-50.
13. Shweiki D, Itin A, Soffer D, Keshet E. Vascular endothelial growth factor induced by hypoxia may mediate hypoxia-initiated angiogenesis. Nature 1992;359:843-5.
14. Sakaki T, Yamada K, Otsuki H, Yuguchi T, Kohmura E, Hayakawa T. Brief exposure to hypoxia induces bFGF mRNA and protein and protects rat cortical neurons from prolonged hypoxic stress. Neurosci Res 1995;23:289-96.
15. Graham CH, Forsdike J, Fitzgerald CJ, Macdonald-Goodfellow S. Hypoxia-mediated stimulation of carcinoma cell invasiveness via upregulation of urokinase receptor expression. Int J Cancer 1999;80:617-23.
16. Rofstad EK, Rasmussen H, Galappathi K, Mathiesen B, Nilsen K, Graff BA. Hypoxia promotes lymph node metastasis in human melanoma xenografts by up-regulating the urokinase-type plasminogen activator receptor. Cancer Res 2002;62:1847-53.
17. Vlodavsky I, Elkin M, Pappo O, et al. Mammalian heparanase as mediator of tumor metastasis and angiogenesis. Isr Med Assoc J 2000;2(Suppl):37-45.
18. Goldshmidt O, Zcharia E, Abramovitch R, et al. Cell surface expression and secretion of heparanase markedly promote tumor angiogenesis and metastasis. Proc Natl Acad Sci USA 2002;99:10031-6.
19. Wilhelm O, Weidle U, Hohl S, Rettenberger P, Schmitt M, Graeff H. Recombinant soluble urokinase receptor as a scavenger for urokinase-type plasminogen activator (uPA). Inhibition of proliferation and invasion of human ovarian cancer cells. FEBS Lett 1994;337:131-4.
20. Chomczynski P, Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 1987;162:156-9.
21. Behzad F, Brenchley PE. A multiwell format assay for heparanase. Anal Biochem 2003;320:207-13.
22. Parish CR, Freeman C, Hulett MD. Heparanase: a key enzyme involved in cell invasion. Biochim Biophys Acta 2001;1471:M99-108.
23. Postovit LM, Adams MA, Lash GE, Heaton JP, Graham CH. Oxygen-mediated regulation of tumor cell invasiveness: involvement of a nitric oxide signaling pathway. J Biol Chem 2002;277:35730-7.
24. Dempsey LA, Plummer TB, Coombes SL, Platt JL. Heparanase expression in invasive trophoblasts and acute vascular damage. Glycobiology 2000;10:467-75.
25. Irimura T, Nakajima M, Nicolson GL. Chemically modified heparins as inhibitors of heparan sulfate specific endo-β-glucuronidase (heparanase) of metastatic melanoma cells. Biochemistry 1986;25:5322-8.
26. Parish CR, Freeman C, Brown KJ, Francis DJ, Cowden WB. Identification of sulfated oligosaccharide-based inhibitors of tumor growth and metastasis using novel in vitro assays for angiogenesis and heparanase activity. Cancer Res 1999;59:3433-41.
27. Miao HQ, Elkin M, Aingorn E, Ishai-Michaeli R, Stein CA, Vlodavsky I. Inhibition of heparanase activity and tumor metastasis by laminarin sulfate and synthetic phosphorothioate oligodeoxynucleotides. Int J Cancer 1999;83:424-31.
28. Goldshmidt O, Zcharia E, Cohen M, et al. Heparanase mediates cell adhesion independent of its enzymatic activity. FASEB J 2003;17:1015-25.
29. Sanderson RD. Heparan sulfate proteoglycans in invasion and metastasis. Semin Cell Dev Biol 2001;12:89-98.
30. Gilat D, Hershkoviz R, Goldkorn I, et al. Molecular behavior adapts to context: heparanase functions as an extracellular matrix-degrading enzyme or as a T cell adhesion molecule, depending on the local pH. J Exp Med 1995;181:1929-34.