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EnglishDiffusible protein signals of the ciliate Euplotes raikovi, denoted as pheromones, have functionally been linked with prototypic growth factors of animal cells by the demonstration that they not only induce a temporary cell union in mating pairs, by acting in a paracrine-like fashion, but can also bind to cells in autocrine fashion and promote their vegetative (mitotic) proliferation. It is now shown that pheromone Er-1 is capable of binding to the alpha and beta chains of the multimeric IL-2 receptor on mammalian cells and that IL-2 can, in turn, bind to the putative cell receptor of this pheromone. Similarities in the IL-2 and Er-1 structures support these findings and raise controversial implications with regard to their evolutionary significance.
Structure-function relationships of pheromones of the ciliate Euplotes raikovi with mammalian growth factors: cross-reactivity between Er-1 and interleukin-2 systems. / A. VALLESI; G. GIULI; G. SCAPIGLIATI; P. GHIARA; P. LUPORINI. - In: EXPERIMENTAL CELL RESEARCH. - ISSN 0014-4827. - 241:1(1998), pp. 253-259.
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| Titolo: | Structure-function relationships of pheromones of the ciliate Euplotes raikovi with mammalian growth factors: cross-reactivity between Er-1 and interleukin-2 systems. |
| Autori: | |
| Data di pubblicazione: | 1998 |
| Rivista: | |
| Citazione: | Structure-function relationships of pheromones of the ciliate Euplotes raikovi with mammalian growth factors: cross-reactivity between Er-1 and interleukin-2 systems. / A. VALLESI; G. GIULI; G. SCAPIGLIATI; P. GHIARA; P. LUPORINI. - In: EXPERIMENTAL CELL RESEARCH. - ISSN 0014-4827. - 241:1(1998), pp. 253-259. |
| Abstract: | Diffusible protein signals of the ciliate Euplotes raikovi, denoted as pheromones, have functionally been linked with prototypic growth factors of animal cells by the demonstration that they not only induce a temporary cell union in mating pairs, by acting in a paracrine-like fashion, but can also bind to cells in autocrine fashion and promote their vegetative (mitotic) proliferation. It is now shown that pheromone Er-1 is capable of binding to the alpha and beta chains of the multimeric IL-2 receptor on mammalian cells and that IL-2 can, in turn, bind to the putative cell receptor of this pheromone. Similarities in the IL-2 and Er-1 structures support these findings and raise controversial implications with regard to their evolutionary significance. |
| Handle: | http://hdl.handle.net/11581/116843 |
| Appare nelle tipologie: | Articolo |
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