IVIg modulates BCR signaling through CD22 and promotes apoptosis in mature human B lymphocytes

Autor: Pierre Youinou, Yves Renaudineau, Rizgar A. Mageed, Divi Cornec, Sophie Hillion, Jean-François Séité
Přispěvatelé: Immunologie et Pathologie (EA2216), Université de Brest (UBO)-IFR148, CHRU Brest - Service de Rhumatologie (CHU - BREST - Rhumato), Centre Hospitalier Régional Universitaire de Brest (CHRU Brest), Laboratoire d'Immunologie et Immunothérapie, William Harvey Research Institute, Barts and the London Medical School, LabEX IGO Immunothérapie Grand Ouest
Jazyk: angličtina
Rok vydání: 2010
Předmět:
MAPK/ERK pathway
MESH: Signal Transduction
Time Factors
Sialic Acid Binding Ig-like Lectin 2
Apoptosis
MESH: Flow Cytometry
MESH: Cell Cycle
Biochemistry
MESH: Dose-Response Relationship
Drug
chemistry.chemical_compound
0302 clinical medicine
hemic and lymphatic diseases
MESH: Child
MESH: Microscopy
Confocal
MESH: Immunoglobulins
Intravenous
Child
Receptor
Cells
Cultured
Mitogen-Activated Protein Kinase 1
B-Lymphocytes
0303 health sciences
Microscopy
Confocal
Mitogen-Activated Protein Kinase 3
biology
MESH: Immunologic Factors
Cell Cycle
CD22
Immunoglobulins
Intravenous
Hematology
Cell cycle
Flow Cytometry
3. Good health
Cell biology
MESH: Cell Survival
MESH: Sialic Acid Binding Ig-like Lectin 2
[SDV.IMM]Life Sciences [q-bio]/Immunology
Antibody
Signal transduction
MESH: N-Acetylneuraminic Acid
MESH: Mitogen-Activated Protein Kinase 3
Protein Binding
Signal Transduction
MESH: Cells
Cultured
MESH: Mitogen-Activated Protein Kinase 1
MESH: Enzyme Activation
MESH: Cell Line
Tumor
Cell Survival
Blotting
Western
Immunology
Receptors
Antigen
B-Cell
MESH: Receptors
Antigen
B-Cell
03 medical and health sciences
LYN
Cell Line
Tumor
MESH: B-Lymphocytes
Humans
Immunologic Factors
MESH: Protein Binding
MESH: Blotting
Western
030304 developmental biology
MESH: Humans
Dose-Response Relationship
Drug
MESH: Apoptosis
MESH: Time Factors
Tyrosine phosphorylation
Cell Biology
N-Acetylneuraminic Acid
Enzyme Activation
chemistry
biology.protein
030215 immunology
Zdroj: Blood
Blood, American Society of Hematology, 2010, 116 (10), pp.1698-704. ⟨10.1182/blood-2009-12-261461⟩
ISSN: 0006-4971
1528-0020
DOI: 10.1182/blood-2009-12-261461⟩
Popis: Among various mechanisms for interactions with B cells, intravenous immunoglobulin (IVIg) may operate through the insertion of its Fc part into the Fc-γ receptor, or the binding of its sialic acid (SA)–bearing glycans to the negatively regulating CD22 lectin. It appeared that IVIg reduces B lymphocyte viability in a dose- and time-dependent manner. Furthermore, we show by confocal microscopy that SA-positive IgG, but not SA-negative IgG bind to CD22. This interaction reduces the strength of B-cell receptor–mediated signaling trough down-regulating tyrosine phosphorylation of Lyn and the B-cell linker proteins, and up-regulating phospholipase Cγ2 activation. This cascade resulted in a sustained activation of Erk 1/2 and arrest of the cell cycle at the G1 phase. These changes may be accounted for the efficacy of IVIg in autoimmune diseases.
Databáze: OpenAIRE
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