Human epidermal Langerhans cells secrete a soluble receptor for IgG (Fc gamma RII/CD32) that inhibits the binding of immune complexes to Fc gamma R+ cells

A Astier, H de la Salle, C de la Salle, T Bieber, M E Esposito-Farese, M Freund, J P Cazenave, W H Fridman, J L Teillaud, D Hanau

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Langerhans cells (LC) express Fc gamma RII on their cell surface. In this paper, we demonstrate that these cells also release soluble Fc gamma RII (sFc gamma RII) molecules. LC express transcripts encoding a membrane-associated receptor and a transmembrane-deleted Fc gamma RIIA. The latter form was identified in LC culture supernatants using specific antibodies. CHO cells, transfected with LC-derived cDNA encoding the transmembrane-deleted Fc gamma RIIA, secrete sFc gamma RIIA that include the intracellular domain and exhibit the same backbone as the protein identified in LC supernatants. Secreted sFc gamma RIIA exhibits the same pattern of binding to human and mouse IgG subclasses as do membrane Fc gamma RII and inhibits the binding of immune complexes to Fc gamma RII+ cells. In addition, CHO cells expressing the membrane-associated Fc gamma RIIA release truncated and unstable Fc gamma RIIA molecules that lack the intracellular domain. Thus, sFc gamma RII can result from shedding of membrane molecules and/or from secretion of soluble receptors lacking the transmembrane domain.
Original languageEnglish
Pages (from-to)201-12
Number of pages12
JournalThe Journal of Immunology
Volume152
Issue number1
Publication statusPublished - 1994

Keywords / Materials (for Non-textual outputs)

  • Alternative Splicing
  • Amino Acid Sequence
  • Animals
  • Antigen-Antibody Complex
  • Base Sequence
  • CHO Cells
  • Cells, Cultured
  • Cricetinae
  • Escherichia coli
  • Humans
  • Langerhans Cells
  • Molecular Sequence Data
  • Polymerase Chain Reaction
  • RNA, Messenger
  • Receptors, IgG
  • Recombinant Proteins
  • Solubility

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