Tuftsin (an Ig-associated tetrapeptide) triggers the immunogenic function of macrophages: implications for activation of programmed cells. | Zendy

Esther Tzehoval | Zendy; S. Segal | Zendy; Y. Stabinsky | Zendy; Mati Fridkin | Zendy; Z Spirer | Zendy; M. Feldman | Zendy

Open Access

Tuftsin (an Ig-associated tetrapeptide) triggers the immunogenic function of macrophages: implications for activation of programmed cells.

Author(s) -

Esther Tzehoval,

S. Segal,

Y. Stabinsky,

Mati Fridkin,

Z Spirer,

M. Feldman

Publication year - 1978

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.75.7.3400

Subject(s) - tetrapeptide , tuftsin , peptide , oligopeptide , chemistry , dipeptide , phagocytosis , receptor , muramyl dipeptide , immune system , macrophage , biochemistry , stereospecificity , microbiology and biotechnology , biology , immunology , in vitro , catalysis

The immunoglobulin heavy-chain-associated tetrapeptide, tuftsin (Thr-Lys-Pro-Arg), known for its phagocytosis-stimulating activity, was found to augment the antigen-specific, macrophage-dependent education of T lymphocytes. The investigation of stereospecific characteristics of the tetrapeptide, by use of structural analogs with different modifications, revealed strict structural requirements for eliciting the immunogenic activity of macrophages. It was found that the most important moiety for its activity is the dipeptide Pro-Arg. This finding is of interest in view of the appearance of this particular dipeptide in other bioregulatory peptides, including many of the peptide hormones. The significance of the appearance of a common structure in such molecules, which may act through specific receptors on different target cells, is discussed.

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