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Modulation of murine complement receptor type 2 (CR2/CD21) ectodomain shedding by its cytoplasmic domain.
Journal article

Modulation of murine complement receptor type 2 (CR2/CD21) ectodomain shedding by its cytoplasmic domain.

  • 2008-02-26
Published in:
  • Molecular immunology. - 2008
Amino Acid Sequence
Animals
Antioxidants
B-Lymphocytes
Cytoplasm
Fluorescence
Male
Mice
Mice, Inbred C57BL
Molecular Sequence Data
Mutagenesis, Site-Directed
Protein Structure, Tertiary
Receptors, Complement 3d
Sequence Deletion
Sulfhydryl Compounds
Time Factors
Vanadates
English Ectodomain shedding is a mechanism that regulates numerous functions of cell surface proteins. The extracellular domain of the human complement receptor 2 (CR2/CD21) is released by proteolytic cleavage as a soluble protein through a variety of stimuli including the thiol antioxidants N-acetylcysteine (NAC) and glutathione (GSH), and the oxidant pervanadate (PV). In addition, PV mimics B cell antigen receptor (BCR) signaling. Here, we show that murine CD21 is shed upon those stimuli and that the cytoplasmic domain is an important modulator for CD21-shedding. B cells expressing a mutant CD21 cytoplasmic domain with only three amino acids (KHR) showed increased CD21-shedding and required lower stimuli concentrations. At lower PV concentrations, wildtype CD21 was up-regulated on the cell surface, whereas at higher PV concentrations the ectodomain was shed. These findings further indicate that GSH and NAC utilize different pathways than PV to activate CD21-shedding. Altogether, as pre-activated B cells express higher CD21 levels than resting mature B cells or fully activated and antigen-experienced B cells, we suggest CD21-shedding to be a mechanism to fine-tune B cell activation.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://sonar.ch/global/documents/112610
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