title: The evidence on the possible interleukin-1 alpha tuftsin competition.
abstract: It was demonstrated by the experiments performed in vivo in mice (peripheral blood leukocyte number determination), and in vitro on mouse thymocytes (autologous rosette forming cell number determination) that tuftsin (Thr-Lys-Pro-Arg), a natural phagocytosis-stimulating factor, inhibits the action of interleukin 1 alpha. This effect is interpreted by us in the terms of structural correspondence between tuftsin and "retro-tuftsin"-like sequence 210-213 of the IL-1 alpha peptide chain. The analysis of tertiary structure shows that this sequence is localized in the exposed fragment of the IL-1 alpha molecule, probably responsible for the interaction with the receptor.
authors.affiliation: Institute of Chemistry, Wrocław University.
authors.forename: I Z
authors.initials: IZ
authors.lastname: Siemion
authors.forename: J
authors.initials: J
authors.lastname: Słoń
authors.forename: K
authors.initials: K
authors.lastname: Spiegel
authors.forename: Z
authors.initials: Z
authors.lastname: Wieczorek
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D066298:In Vitro Techniques; D007375:Interleukin-1 / Q000037:antagonists & inhibitors* / Q000737:chemistry; D007964:Leukocytosis / Q000139:chemically induced; D051379:Mice; D008808:Mice, Inbred CBA; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012397:Rosette Formation; D017386:Sequence Homology, Amino Acid; D014405:Tuftsin / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D007375:Interleukin-1; D014405:Tuftsin