Cloning of mammalian heparanase, an important enzyme in tumor invasion and metastasis

Nat Med. 1999 Jul;5(7):803-9. doi: 10.1038/10525.

Abstract

The endoglycosidase heparanase is an important in the degradation of the extracellular matrix by invading cells, notably metastatic tumor cells and migrating leukocytes. Here we report the cDNA sequence of the human platelet enzyme, which encodes a unique protein of 543 amino acids, and the identification of highly homologous sequences in activated mouse T cells and in a highly metastatic rat adenocarcinoma. Furthermore, the expression of heparanase mRNA in rat tumor cells correlates with their metastatic potential. Exhaustive studies have shown only one heparanase sequence, consistent with the idea that this enzyme is the dominant endoglucuronidase in mammalian tissues.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenocarcinoma / enzymology*
  • Adenocarcinoma / genetics
  • Adenocarcinoma / pathology
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Blood Platelets / enzymology*
  • Cloning, Molecular
  • DNA, Complementary
  • Extracellular Matrix / physiology
  • Female
  • Glucuronidase*
  • Glycoside Hydrolases / genetics*
  • Glycoside Hydrolases / metabolism*
  • Humans
  • Mammals
  • Mammary Neoplasms, Experimental / enzymology*
  • Mammary Neoplasms, Experimental / genetics
  • Mammary Neoplasms, Experimental / pathology
  • Mice
  • Molecular Sequence Data
  • Neoplasm Invasiveness / physiopathology*
  • Neoplasm Metastasis / physiopathology*
  • RNA, Messenger / analysis
  • Rats
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Transcription, Genetic

Substances

  • DNA, Complementary
  • RNA, Messenger
  • Glycoside Hydrolases
  • heparanase
  • Glucuronidase

Associated data

  • GENBANK/AF165154