J. Biochem, 1994, Vol. 115, No. 2 257-269
© 1994 Japanese Biochemical Society
research-article |
Interferon-
Induces Different Subunit Organizations and Functional Diversity of Proteasomes1
*Department of Urology, School of Medicine Tokushima 770
**Biomatenal Research Institute 1 Taya-cho, Sakae-ku, Yokohama 244
***Institute for Enzyme Research, The University of Tokushima Tokushima 770
2To whom correspondence should be addressed
To obtain information on the role of proteasomes in the immune system, we examined the effect of a major immunomodulatory cytokine, gamma interferon (IFN-
), on the expressions, structures, and functions of proteasomes. IFN- greatly increased the levels of the mRNAs encoding LMP2 and LMP7, putative immuno-proteasome subunits encoded by genes within the class II MHC region, and these two subunits synthesized were assembled completely into the proteasomal multi-subunit complex in various types of human cells. The subunit organization of the proteasome changed in response to IFN- stimulation, due to assembly of newly synthesized subunits through up- and down-expressions of at least 6 proteasome genes including LMP2/LMP7 without change in the structure of pre-existing proteasomes. Interestingly, IFN- dramatically stimulated the trypsin-like and chymotrypsin-like activities of the multifunctional proteasome and depressed the peptidylglutamyl-peptide-hydrolyzing activity, without affecting the activity for ATP-, ubiquitindependent proteolysis. These results indicate that IFN- modifies not only the structural organization of the proteasome, but also its functions. Based on these findings, we discuss the role in the antigen processing/presentation pathway of proteasomes with functional diversity acquired through alteration of their subunit assembly in response to IFN- stimulation.
1This work was supported in part by Grants-in-Aid from the Ministry of Education, Science and Culture of Japan.
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