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

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          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.

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          Author and article information

          Journal
          Immunol. Res.
          Immunologic research
          Springer Nature America, Inc
          0257-277X
          0257-277X
          2005
          : 31
          : 3
          Affiliations
          [1 ] Laboratory of Molecular Immunoregulation, Center for Cancer Research, National Cancer Institute at Frederick, Frederick, MD 21702, USA. yoshimur@mail.ncifcrf.gov
          Article
          IR:31:3:219
          10.1385/IR:31:3:219
          15888913
          bce62cad-1798-4599-9f94-90739e57bd0e
          History

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