Intermolecular complexes between three human CD1 molecules on normal thymus cells

Martine Amiot, Helene Dastot, Marina Fabbi, Laurent Degos, Alain Bernard, Laurence Boumsell

Research output: Contribution to journalArticlepeer-review

Abstract

The first cluster of differentiation (CD1) defines at least three distinct human thymic cell-surface differentiation antigens-CD1a, CD1b, and CD1c. We looked for structural homology of the three CD1 heavy chains at their peptide level by two-dimensional peptide maps. We show here that the CD1a Mr 49 000 heavy chain and the CD1b Mr 45 000 heavy chain appear to be more homologous to each other than to the CD1 c Mr 43 000 heavy chain and that only one tyrosil peptide is common to the three heavy chains. Study of the CD1 heavy chains from several individuals reveals a very limited polymorphism of these molecules. We also demonstrate here that CD1a or CD1a-like molecules and other CD1 molecules can form intermolecular complexes on the surface of normal thymus cells. Molecules that are structurally very similar to CD1a molecules are associated noncovalently either with CD1c molecules or with CD1b molecules, and only CD 1a molecules can associate covalently with CD8 molecules. In contrast, we could not find these intermolecular complexes on the surface of leukemic T-cell lines in culture.

Original languageEnglish
Pages (from-to)187-195
Number of pages9
JournalImmunogenetics
Volume27
Issue number3
DOIs
Publication statusPublished - Mar 1988

ASJC Scopus subject areas

  • Immunology
  • Genetics

Fingerprint Dive into the research topics of 'Intermolecular complexes between three human CD1 molecules on normal thymus cells'. Together they form a unique fingerprint.

Cite this