Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 6 May 1983:
Vol. 220. no. 4597, pp. 611 - 613
DOI: 10.1126/science.6220468
Prev | Table of Contents | Next

Articles

Science, Vol 220, Issue 4597, 611-613
Copyright © 1983 by American Association for the Advancement of Science

articles

Heparan sulfate degradation: relation to tumor invasive and metastatic properties of mouse B16 melanoma sublines

M Nakajima, T Irimura, D Di Ferrante, N Di Ferrante, and GL Nicolson

After transport in the blood and implantation in the microcirculation, metastatic tumor cells must invade the vascular endothelium and underlying basal lamina. Mouse B16 melanoma sublines were used to determine the relation between metastatic properties and the ability of the sublines to degrade enzymatically the sulfated glycosaminoglycans present in the extracellular matrix of cultured vascular endothelial cells. Highly invasive and metastatic B16 sublines degraded matrix glycosaminoglycans faster than did sublines of lower metastatic potential. The main products of this matrix degradation were heparan sulfate fragments. Intact B16 cells (or their cell-free homogenates) with a high potential for lung colonization degraded purified heparan sulfate from bovine lung at higher rates than did B16 cells with a poor potential for lung colonization. Analysis of the degradation fragments indicated that B16 cells have a heparan sulfate endoglycosidase. Thus the abilities of B16 melanoma cells to extravasate and successfully colonize the lung may be related to their capacities to degrade heparan sulfate in the walls of pulmonary blood vessels.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Structure-Function Approach Identifies a COOH-Terminal Domain That Mediates Heparanase Signaling.
L. Fux, N. Feibish, V. Cohen-Kaplan, S. Gingis-Velitski, S. Feld, C. Geffen, I. Vlodavsky, and N. Ilan (2009)
Cancer Res. 69, 1758-1767
   Abstract »    Full Text »    PDF »
A Phase I Biological and Pharmacologic Study of the Heparanase Inhibitor PI-88 in Patients with Advanced Solid Tumors..
M. Basche, D. L. Gustafson, S. N. Holden, C. L. O'Bryant, L. Gore, S. Witta, M. K. Schultz, M. Morrow, A. Levin, B. R. Creese, et al. (2006)
Clin. Cancer Res. 12, 5471-5480
   Abstract »    Full Text »    PDF »
Characterization of Mechanisms Involved in Secretion of Active Heparanase.
I. Shafat, I. Vlodavsky, and N. Ilan (2006)
J. Biol. Chem. 281, 23804-23811
   Abstract »    Full Text »    PDF »
Heparanase Induces Vascular Endothelial Growth Factor Expression: Correlation with p38 Phosphorylation Levels and Src Activation.
A. Zetser, Y. Bashenko, E. Edovitsky, F. Levy-Adam, I. Vlodavsky, and N. Ilan (2006)
Cancer Res. 66, 1455-1463
   Abstract »    Full Text »    PDF »
Heparanase Is Involved in Angiogenesis in Esophageal Cancer through Induction of Cyclooxygenase-2.
T. Okawa, Y. Naomoto, T. Nobuhisa, M. Takaoka, T. Motoki, Y. Shirakawa, T. Yamatsuji, H. Inoue, M. Ouchida, M. Gunduz, et al. (2005)
Clin. Cancer Res. 11, 7995-8005
   Abstract »    Full Text »    PDF »
Expression of Heparanase by Primary Breast Tumors Promotes Bone Resorption in the Absence of Detectable Bone Metastases.
T. Kelly, L. J. Suva, Y. Huang, V. MacLeod, H.-Q. Miao, R. C. Walker, and R. D. Sanderson (2005)
Cancer Res. 65, 5778-5784
   Abstract »    Full Text »    PDF »
Structure-based design of a selective heparanase inhibitor as an antimetastatic agent.
K. Ishida, G. Hirai, K. Murakami, T. Teruya, S. Simizu, M. Sodeoka, and H. Osada (2004)
Mol. Cancer Ther. 3, 1069-1077
   Abstract »    Full Text »    PDF »
Heparanase Gene Silencing, Tumor Invasiveness, Angiogenesis, and Metastasis.
E. Edovitsky, M. Elkin, E. Zcharia, T. Peretz, and I. Vlodavsky (2004)
J Natl Cancer Inst 96, 1219-1230
   Abstract »    Full Text »    PDF »
Human T-Cell Lymphotropic Virus Type I-Infected Cells Extravasate through the Endothelial Barrier by a Local Angiogenesis-Like Mechanism.
A. Bazarbachi, R. A. Merhi, A. Gessain, R. Talhouk, H. El-Khoury, R. Nasr, O. Gout, R. Sulahian, F. Homaidan, H. de The, et al. (2004)
Cancer Res. 64, 2039-2046
   Abstract »    Full Text »    PDF »
Cell Surface Localization of Heparanase on Macrophages Regulates Degradation of Extracellular Matrix Heparan Sulfate.
N. Sasaki, N. Higashi, T. Taka, M. Nakajima, and T. Irimura (2004)
J. Immunol. 172, 3830-3835
   Abstract »    Full Text »    PDF »
Secretion of Heparanase Protein Is Regulated by Glycosylation in Human Tumor Cell Lines.
S. Simizu, K. Ishida, M. K. Wierzba, and H. Osada (2004)
J. Biol. Chem. 279, 2697-2703
   Abstract »    Full Text »    PDF »
Microenvironmental and cellular consequences of altered blood flow in tumours.
N Raghunand, R A Gatenby, and R J Gillies (2003)
Br. J. Radiol. 76, S11-S22
   Abstract »    Full Text »    PDF »
Heparanase expression is an independent prognostic factor in patients with invasive cervical cancer.
Y. Shinyo, J. Kodama, A. Hongo, M. Yoshinouchi, and Y. Hiramatsu (2003)
Ann. Onc. 14, 1505-1510
   Abstract »    Full Text »    PDF »
Structural Recognition by Recombinant Human Heparanase That Plays Critical Roles in Tumor Metastasis. HIERARCHICAL SULFATE GROUPS WITH DIFFERENTIAL EFFECTS AND THE ESSENTIAL TARGET DISULFATED TRISACCHARIDE SEQUENCE.
Y. Okada, S. Yamada, M. Toyoshima, J. Dong, M. Nakajima, and K. Sugahara (2002)
J. Biol. Chem. 277, 42488-42495
   Abstract »    Full Text »    PDF »
Characterization of Heparanase from a Rat Parathyroid Cell Line.
K. A. Podyma-Inoue, H. Yokote, K. Sakaguchi, M. Ikuta, and M. Yanagishita (2002)
J. Biol. Chem. 277, 32459-32465
   Abstract »    Full Text »    PDF »
Treatment with the novel anti-angiogenic agent PI-88 is associated with immune-mediated thrombocytopenia.
M. A. Rosenthal, D. Rischin, G. McArthur, K. Ribbons, B. Chong, J. Fareed, G. Toner, M. D. Green, and R. L. Basser (2002)
Ann. Onc. 13, 770-776
   Abstract »    Full Text »    PDF »
Cloning and Characterization of the Human Heparanase-1 (HPR1) Gene Promoter. ROLE OF GA-BINDING PROTEIN AND Sp1 IN REGULATING HPR1 BASAL PROMOTER ACTIVITY.
P. Jiang, A. Kumar, J. E. Parrillo, L. A. Dempsey, J. L. Platt, R. A. Prinz, and X. Xu (2002)
J. Biol. Chem. 277, 8989-8998
   Abstract »    Full Text »    PDF »
Antisense-mediated Suppression of Human Heparanase Gene Expression Inhibits Pleural Dissemination of Human Cancer Cells.
F. Uno, T. Fujiwara, Y. Takata, S. Ohtani, K. Katsuda, M. Takaoka, T. Ohkawa, Y. Naomoto, M. Nakajima, and N. Tanaka (2001)
Cancer Res. 61, 7855-7860
   Abstract »    Full Text »    PDF »
The Clinicopathological Significance of Heparanase and Basic Fibroblast Growth Factor Expressions in Hepatocellular Carcinoma.
O. N. El-Assal, A. Yamanoi, T. Ono, H. Kohno, and N. Nagasue (2001)
Clin. Cancer Res. 7, 1299-1305
   Abstract »    Full Text »
Heparanase expression in invasive trophoblasts and acute vascular damage.
L. A. Dempsey, T. B. Plummer, S. L. Coombes, and J. L. Platt (2000)
Glycobiology 10, 467-475
   Abstract »    Full Text »    PDF »
Substrate Specificity of Heparanases from Human Hepatoma and Platelets.
D. S. Pikas, J.-p. Li, I. Vlodavsky, and U. Lindahl (1998)
J. Biol. Chem. 273, 18770-18777
   Abstract »    Full Text »    PDF »
Review : Synthetic Polymers with Intrinsic Anticancer Activity.
L. Seymour (1991)
Journal of Bioactive and Compatible Polymers 6, 178-216
   PDF »
Molecular Characterization of a Novel beta -Glucuronidase from Scutellaria baicalensis Georgi.
K. Sasaki, F. Taura, Y. Shoyama, and S. Morimoto (2000)
J. Biol. Chem. 275, 27466-27472
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)