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...

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Bibliographic Details
Published in:Immunologic research 2005-01, Vol.31 (3), p.219-230
Main Authors: Yoshimura, Teizo, Matsuyama, Wataru, Kamohara, Hidenobu
Format: Article
Language:English
Subjects:
Cell Adhesion
Cell adhesion & migration
Cell Differentiation
Cell Movement
Collagen
Collagen - physiology
Cytokines - biosynthesis
Discoidin Domain Receptor 1
Humans
Immunology
Leukocytes
Leukocytes - metabolism
Leukocytes - physiology
Proteins
Receptor Protein-Tyrosine Kinases - physiology
Signal Transduction
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Summary: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.
ISSN:0257-277X
0257-277X
1559-0755
DOI:10.1385/IR:31:3:219