Cloning of two splice variants of Spalax heparanase encoding for truncated proteins

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

Research output: Contribution to journalArticlepeer-review

Abstract

Heparanase is an endoglycosidase that degrades heparan sulfate side chains of heparan sulfate-proteoglycans. It liberates heparan sulfate-bound growth factors and thereby promotes blood vessel sprouting and angiogenesis. The subterranean blind mole rat, Spalax, is a wild mammal that lives most of its life in underground tunnels where it experiences sharp fluctuations in oxygen and carbon dioxide levels. We described two splice variants of heparanase from Spalax, Splice 7 and splice 36, both devoid of heparanase enzymatic activity. Splice 7 increases tumor growth, while splice 36 functions as a dominant negative to wild-type heparanase and decreases tumor growth and metastasis. Here, we describe two novel splice variants of Spalax heparanase, splice 67 and splice 612. These splice variants result in production of a shorter heparanase proteins that are similar to the wild-type native heparanase in their N-terminal but have unique C-terminals. Both splice 67 and 612 lack heparan sulfate degradation activity.

Original languageEnglish
Pages (from-to)885-889
Number of pages5
JournalAnti-Cancer Drugs
Volume31
Issue number9
DOIs
StatePublished - 1 Oct 2020

Bibliographical note

Publisher Copyright:
© 2020 Lippincott Williams and Wilkins. All rights reserved.

Keywords

  • Spalax
  • alternative splicing
  • angiogenesis
  • cancer
  • heparanase
  • hypoxia

ASJC Scopus subject areas

  • Pharmacology (medical)
  • Oncology
  • Cancer Research
  • Pharmacology

Fingerprint

Dive into the research topics of 'Cloning of two splice variants of Spalax heparanase encoding for truncated proteins'. Together they form a unique fingerprint.

Cite this