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Science 2 July 1999:
Vol. 285. no. 5424, pp. 33 - 34
DOI: 10.1126/science.285.5424.33

News Focus

CANCER RESEARCH:
Potential Target Found for Antimetastasis Drugs

Elizabeth Finkel

In the July issue of Nature Medicine, researchers report that they have finally cloned the gene for the enzyme heparanase, which helps cancer cells escape to new sites in the body and may thus be a good target for anticancer drugs. In previous work, researchers had cloned several genes for the enzymes, called proteases, that cancer cells use to break down the protein portion of the extracellular matrix, the glue that holds cells together in tissues, and the basement membranes that surround the blood vessels. Although metastasizing cancer cells may produce as many as 15 different matrix-digesting proteases, the new work suggests that there is only one heparanase. Thus, if its activity can be inhibited--and indications are that it can be--other heparanases shouldn't be around to cover for it.

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Alternatively spliced Spalax heparanase inhibits extracellular matrix degradation, tumor growth, and metastasis.
N. J. Nasser, A. Avivi, I. Shafat, E. Edovitsky, E. Zcharia, N. Ilan, I. Vlodavsky, and E. Nevo (2009)
PNAS 106, 2253-2258
   Abstract »    Full Text »    PDF »
Bystander Effect in Herpes Simplex Virus-Thymidine Kinase/Ganciclovir Cancer Gene Therapy: Role of Gap-junctional Intercellular Communication1.
M. Mesnil and H. Yamasaki (2000)
Cancer Res. 60, 3989-3999
   Abstract »    Full Text »
Processing of the Human Heparanase Precursor and Evidence That the Active Enzyme Is a Heterodimer.
M. B. Fairbanks, A. M. Mildner, J. W. Leone, G. S. Cavey, W. R. Mathews, R. F. Drong, J. L. Slightom, M. J. Bienkowski, C. W. Smith, C. A. Bannow, et al. (1999)
J. Biol. Chem. 274, 29587-29590
   Abstract »    Full Text »    PDF »



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