Discoidin domain receptor 1: a new class of receptor regulating leukocyte-collagen interaction

Immunol Res. 2005;31(3):219-30. doi: 10.1385/IR:31:3:219.

Abstract

Previous studies demonstrated that type I collagen, a major component of the extracellular matrix, could influence the differentiation and function of leukocytes; however, it is not clear whether those effects of collagen were based on its interaction with the classic collagen receptors, alpha1beta1 and alpha2beta1 integrins. We recently detected significant upregulation of discoidin domain receptor 1 (DDR1), a new class of collagen receptor, in human leukocytes, including neutrophils, monocytes, and lymphocytes, in vitro, leading to the hypothesis that the leukocyte-activating effects of collagen might be owing to its interaction with DDR1. In this review, we summarize our recent findings demonstrating that DDR1-collagen interaction facilitates the adhesion, migration, differentiation/maturation, and cytokine/chemokine production of leukocytes. We also describe the intracellular signaling pathways activated by DDR1 interaction with collagen.

Publication types

  • Review

MeSH terms

  • Cell Adhesion
  • Cell Differentiation
  • Cell Movement
  • Collagen / physiology*
  • Cytokines / biosynthesis
  • Discoidin Domain Receptor 1
  • Humans
  • Leukocytes / metabolism
  • Leukocytes / physiology*
  • Receptor Protein-Tyrosine Kinases / physiology*
  • Signal Transduction

Substances

  • Cytokines
  • Collagen
  • DDR1 protein, human
  • Discoidin Domain Receptor 1
  • Receptor Protein-Tyrosine Kinases