Stepwise formation of the high-affinity complex of the interleukin 2 receptor.

Abstract:

:The interleukin 2 receptor (IL-2R) is composed of at least two polypeptides--a 55 kd protein (the L chain, p55, or alpha chain) and a 75 kd protein (the H chain, p75 or beta chain). The high-affinity binding of IL-2 results in the formation of a ternary complex consisting of IL-2 and the L and H chains. We found that the rate of high-affinity complex formation at 0 degrees C was about one-third of that at 37 degrees C. The reduction of high-affinity complex formation rate at lower temperatures correlates with the reduction of lateral diffusion within the membrane at lower temperatures. An anti-H chain antibody (2RB) inhibited the formation of the high-affinity complex at 0 degrees C but not at 37 degrees C. We studied the kinetics of the high-affinity complex formation at 37 degrees C after the preincubation of ATL-2 cells with the 2RB antibody and IL-2 at 0 degrees C. We found that the amount of IL-2.L complex formed initially at 0 degrees C was almost equivalent to the amount of high-affinity complex formed by subsequent incubation at 37 degrees C. These results suggest that the IL-2.L complex might be converted to the high-affinity IL-2R complex. Similar experiments using YTC3 cells, which express a smaller number of L chains, showed slower rates of high-affinity complex formation, in agreement with the affinity conversion/stepwise binding model.

journal_name

Int Immunol

journal_title

International immunology

authors

Saito Y,Ogura T,Kamio M,Sabe H,Uchiyama T,Honjo T

doi

10.1093/intimm/2.12.1167

subject

Has Abstract

pub_date

1990-01-01 00:00:00

pages

1167-77

issue

12

eissn

0953-8178

issn

1460-2377

journal_volume

2

pub_type

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