Specific high-affinity binding sites for a synthetic gliadin heptapeptide on human peripheral blood lymphocytes

Donald G. Payan, Károly Horváth, László Gráf

Research output: Contribution to journalArticle

6 Citations (Scopus)

Abstract

The synthetic peptide containing residues 43-49 of α-gliadin, the major protein component of gluten, has previously been shown to inhibit the production of lymphokine activities by mononuclear leukocytes. We now demonstrate using radiolabeled α-gliadin(43-49) that human peripheral blood lymphocytes express approximately 20,000-25,000 surface receptors for this peptide, with a dissociation constant (KD) of 20 nM. In addition, binding is inhibited by naloxone and an enkephalin analog, thus confirming the functional correlate which demonstrates inhibition by these agents of α-gliadin(43-49) functional effects. Furthermore, B-lymphocytes bind specifically a greater amount of [125I]α-gliadin(43-49) than T-lymphocytes. The lymphocyte α-gliadin(43-49) receptor may play an important role in mediating the immunological response to α-gliadin.

Original languageEnglish
Pages (from-to)1229-1236
Number of pages8
JournalLife sciences
Volume40
Issue number12
DOIs
Publication statusPublished - Mar 23 1987

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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