Cited by 30Neutrophil, Myeloperoxidase and Oxidative MechanismsInflammation biomarkers and pathwaysImmune Response and Inflammation

The ITIM-bearing CLECSF6 (DCIR) is down-modulated in neutrophils by neutrophil activating agents

Richard, Manon, Thibault, Nathalie, Veilleux, Patricia, Breton, Rock, Beaulieu, André D·2003·Biochemical and Biophysical Research Communications

Abstract

The recently discovered CLECSF6 protein displays the features of a receptor involved in the down-modulation of leukocyte activation. Although CLECSF6 has been the focus of the interest of many researchers lately, a Western blot characterization of the protein is still lacking. This highly reduces our ability to gain full knowledge of the biological relevance of this protein in cell responses. We produced two rabbit polyclonal antisera that detected a glycosylated protein at approximately 35kDa in neutrophils. Four different CLECSF6 mRNA species have been discovered to date. When deglycosylated, the protein displayed the molecular weight expected for the longest CLECSF6 form. Neutrophil membrane fractions were strongly enriched in the protein. We showed a down-modulation of the expression of this protein in neutrophils treated with granulocyte-macrophage-colony stimulating factor (GM-CSF), tumor necrosis factor (TNF-alpha), lipopolysaccharide (LPS), and interleukin (IL)-4. This work supports the hypothesis that CLECSF6 is involved in the control of inflammation in neutrophils.

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Crossref · 10.1016/j.bbrc.2003.09.077

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  • IL1R1 and IL15 were strongly co-expressed with the Mac-1 complex and with CLEC4A.

    “To the same group of pro-inflammatory molecules belong also interleukin (IL)1 receptor type I (IL1R1), which modulates many cytokine induced immune and inflammatory responses, and IL15 (IL15), which regulates T and natural killer cell activation and proliferation [31,32]. Both of them were strongly co-expressed with the Mac-1 complex and with C-type lectin domain family 4 member A (CLEC4A), known”

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Authors
Richard, M., Thibault, N., Veilleux, P., Breton, R., & Beaulieu, A. D.
Affiliations
Centre hospitalier de l'Université Laval (CA)
Corresponding author
Beaulieu, André D
Venue
Biochemical and Biophysical Research Communications
Publisher
Elsevier BV
Published
2003-10
Volume
310
Issue
3
Pages
767-773
ISSN
0006-291X (ISSN-L)
OpenAlex
W2052482830
Cited by
30
References
12
Citations by year
2025: 1 · 2020: 1 · 2015: 3 · 2014: 1 · 2013: 5 · 2012: 2
FWCI
0.65
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical and Biophysical Research Communications (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Life Sciences › Immunology and Microbiology › Immunology › Inflammation biomarkers and pathways
  • Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
Keywords
DCIR, neutrophils, leukocyte activation, GM-CSF, TNF-α, lipopolysaccharide, IL-4, protein glycosylation, membrane protein expression, inflammation control, polyclonal antisera
MeSH terms
Animals, Cell Line, Cell Membrane, Electrophoresis, Polyacrylamide Gel, Genetic Vectors, Glycosylation, Humans, Insecta, Leukocytes, Lipopolysaccharides, Membrane Glycoproteins, Neutrophils, Peptides, Rabbits, Receptors, Immunologic, Recombinant Proteins, RNA, Messenger, Tumor Necrosis Factor-alpha, Immunoblotting, Blotting, Western, Down-Regulation, Interleukin-4, Cytokines, Baculoviridae, DNA, Complementary, Lectins, C-Type

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