Structure-function relationships for the interleukin 2 receptor system
Mem. Inst. Oswaldo Cruz
;
82(supl.2): 39-43, 1987. tab, ilus, graf
Article
in English
| LILACS
| ID: lil-623762
ABSTRACT
Receptors for interleukin 2 (IL-2) esit in at least three forms which differ in their subunit compositio, their affinity for ligand and their ability to mediate a cellular reponse. Type I receptors occur following cellular acitivation and consist of the 55,000 m. w. glycoprotein Tac. These receptors bind IL-2 with a low affinity, do not internalize ligand and have not been definitively associated with any response. Type II receptors, on the other hand, conssit of one or more glycoproteins of 70,000 m. w. which have been termed "beta ([beta]) chains." They bind IL-2 with an intermediate affinity and rapidly internalize the ligand. [Beta] proteins mediate many cellular IL-2-dependent reponses, including the short-term activation of natural killer cells and the induction of Tac protein expression. Type III receptors consist of a ternary complex of the Tac protein, the [beta] chain(s) and IL-2. They are characterized by a paricularly high affinity for ligand association. Type III receptors also internalize ligand and mediate IL-2-dependent responses at low factor concentrations. The identification of two independent IL-2-binding molecules, Tac and [beta], thus provides the elusive molecular explanation for the differences in IL-2 receptor affinity and suggests the potential for selective therapeutic manipulation of IL-2 reponses.
Full text:
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Index:
LILACS (Americas)
Main subject:
Receptors, Interleukin-2
/
Interleukin-2
Type of study:
Prognostic study
Limits:
Humans
Language:
English
Journal:
Mem. Inst. Oswaldo Cruz
Journal subject:
Tropical Medicine
/
Parasitology
Year:
1987
Type:
Article
/
Congress and conference
Affiliation country:
United States
Institution/Affiliation country:
E. I. du Pont de Nemours & Co/US
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