Discoidin domain receptor 1: a new class of receptor regulating leukocyte-collagen interaction.
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.
Yoshimura
Teizo
T
Laboratory of Molecular Immunoregulation, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA. yoshimur@mail.ncifcrf.gov
Matsuyama
Wataru
W
Kamohara
Hidenobu
H
D002448:Cell Adhesion; D002454:Cell Differentiation; D002465:Cell Movement; D003094:Collagen / Q000502:physiology*; D016207:Cytokines / Q000096:biosynthesis; D000070819:Discoidin Domain Receptor 1; D006801:Humans; D007962:Leukocytes / Q000378:metabolism / Q000502:physiology*; D020794:Receptor Protein-Tyrosine Kinases / Q000502:physiology*; D015398:Signal Transduction
D016207:Cytokines; D003094:Collagen; C092030:DDR1 protein, human; D000070819:Discoidin Domain Receptor 1; D020794:Receptor Protein-Tyrosine Kinases