Soluble antigen induces T lymphocytes to secrete an endoglycosidase that degrades the heparan sulfate moiety of subendothelial extracellular matrix. Academic Article uri icon

Overview

abstract

  • The antigen-mediated induction of heparanase, an endoglycosidase capable of degrading heparan sulfate from the subendothelial extracellular matrix (ECM), was investigated in a rat T lymphocyte cell line reactive against the basic protein (BP) of myelin. We found that nonactivated T lymphocytes could be induced to express heparanase activity following exposure to soluble but not to ECM-bound BP. The induction of heparanase was immunologically specific and independent of the presence of syngeneic or allogeneic antigen presenting cells (APC). However, anti-IA antibodies inhibited heparanase expression. Soluble BP induced secretion of heparanase into the culture medium within minutes, despite inhibition of protein synthesis. Cell lysates of T lymphocytes contained heparanase activity. Thus, T lymphocytes secrete a preformed heparanase following exposure to specific antigen.

publication date

  • January 1, 1987

Research

keywords

  • Endothelium
  • Extracellular Matrix
  • Glucuronidase
  • Glycosaminoglycans
  • Glycoside Hydrolases
  • Heparitin Sulfate
  • Myelin Basic Protein
  • T-Lymphocytes

Identity

Scopus Document Identifier

  • 0023112112

PubMed ID

  • 2433294

Additional Document Info

volume

  • 130

issue

  • 1