Cloning, expression, and characterization of an alternatively spliced variant of human heparanase

Nicola J. Nasser, Aaron Avivi, Moran Shushy, Israel Vlodavsky, Eviatar Nevo

Research output: Contribution to journalArticlepeer-review

Abstract

Heparanase is an endoglycosidase that cleaves heparan sulfate in the extracellular matrix (ECM) and hence participates in ECM degradation and remodeling. Heparanase is involved in fundamental biological processes such as cancer metastasis, angiogenesis, and inflammation. Alternative splicing in the coding region of human heparanase was not reported. Here, we report the cloning of a splice variant of human heparanase that lacks exon 5 and is missing 174 bp compared to the wild-type cDNA. Splice 5 is expressed as a 55 kDa protein compared to the 65 and 50 kDa latent and active wild-type enzyme. Splice 5 was not detected in the incubation medium of tumor cells as opposed to the wild-type latent heparanase. Splice 5 escaped proteolytic cleavage, was devoid of HS degradation activity and exhibited diffused rather than granular cellular localization.

Original languageEnglish
Pages (from-to)33-38
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume354
Issue number1
DOIs
StatePublished - 2 Mar 2007

Bibliographical note

Funding Information:
We thank Alma Joel for technical assistance. This work was supported by grants from the Israel Science Foundation (Grant 549/06); National Cancer Institute, NIH (Grant RO1-CA106456); the Israel Cancer Research Fund; and the Rappaport Family Institute Fund.

Keywords

  • Alternative splicing
  • Extracellular matrix
  • Heparan sulfate
  • Heparanase

ASJC Scopus subject areas

  • Molecular Biology
  • Biophysics
  • Biochemistry
  • Cell Biology

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