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Volume 272, Number 1, Issue of January 3, 1997 pp. 353-361
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

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Synthesis and Turnover of ₂-Microglobulin in Ad12-transformed Cells Defective in Assembly and Transport of Class I Major Histocompatibility Complex Molecules

(Received for publication, June 19, 1996)

From the Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Ramat Aviv 64978, Israel

In primary embryonal fibroblasts from transgenic mice expressing H-2 genes and a miniature swine class I transgene (PD1), transformation with the highly oncogenic Ad12 results in a reduction in peptide transporter and proteasome-associated (LMP2 and LMP7) gene expression, and suppression in transport and cell surface expression of all class I antigens. The selective suppression in transport of H-2 (but not of PD1) molecules in cells reconstituted for the expression of peptide transporter and LMP genes implied that an additional factor(s) is involved in the assembly of class I complexes. Here we show that the ₂m, H-2D^b, and H-2K^b genes are transcribed and translated in Ad12-transformed cells. However, unlike normal and E1Ad5-transformed cells, in which ₂m is either secreted unbound or bound to class I heavy chains, in Ad12-transformed cells significant amounts of ₂m are retained in the cell bound to the membrane, but free of class I heavy chains. This abnormal turnover of ₂m in the Ad12-transformed cells suggests the existence of a novel ₂m-binding molecule(s) that sequesters ₂m, and this process may provide a mechanism by which transformation with Ad12 may subvert class I complex formation.

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