Literature DB >> 18618498

Heparanase is overexpressed in lung cancer and correlates inversely with patient survival.

Esti Cohen1, Ilana Doweck, Inna Naroditsky, Ofer Ben-Izhak, Ran Kremer, Lael A Best, Israel Vlodavsky, Neta Ilan.   

Abstract

BACKGROUND: Heparanase is an endo-beta-D-glucuronidase that is capable of cleaving heparan sulfate (HS) side chains at a limited number of sites, yielding HS fragments of still appreciable size (approximately 5-7 kDa). Heparanase activity has been detected frequently in several cell types and tissues. Heparanase activity correlates with the metastatic potential of tumor-derived cells, a correlation that has been attributed to enhanced cell dissemination as a consequence of HS cleavage and remodeling of the extracellular matrix barrier.
METHODS: In this study, the authors examined heparanase expression in 114 patients with lung cancer by means of immunohistochemistry and correlated clinical-pathologic data with heparanase immunostaining and cellular localization.
RESULTS: Heparanase was overexpressed in 75% of the study patients. Heparanase expression was correlated with lung cancer lymph node status and metastasis classification (P = .04 and P = .01, respectively) and was correlated inversely with patient survival (P = .007). It is noteworthy that this adverse effect depended largely on the cellular localization of heparanase. Thus, whereas cytoplasmic staining of heparanase is associated with a poor prognosis, nuclear heparanase predicts a favorable outcome for patients with lung cancer.
CONCLUSIONS: The current findings suggest that heparanase expression and cellular localization are decisive for lung cancer patients' prognosis, most likely because of heparanase-mediated tumor cell dissemination by blood and lymph vessels. (c) 2008 American Cancer Society.

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Year:  2008        PMID: 18618498      PMCID: PMC2625296          DOI: 10.1002/cncr.23680

Source DB:  PubMed          Journal:  Cancer        ISSN: 0008-543X            Impact factor:   6.860


  45 in total

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Review 2.  Molecular properties and involvement of heparanase in cancer metastasis and angiogenesis.

Authors:  I Vlodavsky; Y Friedmann
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3.  Processing and activation of latent heparanase occurs in lysosomes.

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Journal:  J Cell Sci       Date:  2004-05-01       Impact factor: 5.285

4.  Heparanase protein and gene expression in bladder cancer.

Authors:  K Gohji; M Okamoto; S Kitazawa; M Toyoshima; J Dong; Y Katsuoka; M Nakajima
Journal:  J Urol       Date:  2001-10       Impact factor: 7.450

5.  Function of heparanase in prostate tumorigenesis: potential for therapy.

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6.  Heparanase expression correlates with invasion and poor prognosis in gastric cancers.

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7.  Expression of heparanase gene, CD44v6, MMP-7 and nm23 protein and their relationship with the invasion and metastasis of gastric carcinomas.

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8.  Heparanase: a key enzyme in invasion and metastasis of gastric carcinoma.

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10.  Regulation of heparan sulfate proteoglycan nuclear localization by fibronectin.

Authors:  T P Richardson; V Trinkaus-Randall; M A Nugent
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  24 in total

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Journal:  Transcription       Date:  2012 May-Jun

Review 2.  Glycosylation alterations in lung and brain cancer.

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3.  Genetic and epigenetic inactivation of extracellular superoxide dismutase promotes an invasive phenotype in human lung cancer by disrupting ECM homeostasis.

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4.  Heparanase enhances local and systemic osteolysis in multiple myeloma by upregulating the expression and secretion of RANKL.

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Review 5.  Update in lung cancer 2008.

Authors:  Sarita Dubey; Charles A Powell
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6.  Significance of heparanase in cancer and inflammation.

Authors:  Israel Vlodavsky; Phillip Beckhove; Immanuel Lerner; Claudio Pisano; Amichai Meirovitz; Neta Ilan; Michael Elkin
Journal:  Cancer Microenviron       Date:  2011-08-03

7.  Chemical Tumor Biology of Heparan Sulfate Proteoglycans.

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8.  Heparanase expression correlates with poor survival in oral mucosal melanoma.

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9.  Heparanase overexpression participates in tumor growth of cervical cancer in vitro and in vivo.

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10.  Heparanase inhibits osteoblastogenesis and shifts bone marrow progenitor cell fate in myeloma bone disease.

Authors:  Jian Ruan; Timothy N Trotter; Li Nan; Rongcheng Luo; Amjad Javed; Ralph D Sanderson; Larry J Suva; Yang Yang
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