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The Major Histocompatibility Complex Class I Antigen-Binding Protein p88 is the Product of the Calnexin Gene
K. Galvin, S. Krishna, F. Ponchel, M. Frohlich, D. E. Cummings, R. Carlson, J. R. Wands, K. J. Isselbacher, S. Pillai and M. Ozturk
Proceedings of the National Academy of Sciences of the United States of America
Vol. 89, No. 18 (Sep. 15, 1992), pp. 8452-8456
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/2360203
Page Count: 5
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A 90-kDa phosphoprotein (p90) of the endoplasmic reticulum was identified by a monoclonal antibody generated against human hepatoma cells. Pulse-chase experiments with [32P]phosphate and [k35S]methionine demonstrated that p90 formed both stable and transient complexes with other cellular proteins, suggesting its role as a molecular chaperone. This protein associates with heavy chains of major histocompatibility complex class I proteins, suggesting that it is the human homolog of the recently described 88-kDa protein that transiently associates with murine class I molecules in the endoplasmic reticulum. The p90 protein also associates in B lymphocytes with membrane immunoglobulin μ heavy chains and may serve as a chaperone for many membrane-bound polypeptides. A partial human p90 cDNA was cloned from a λgt11 expression library and identified as the human homolog of calnexin, a major canine calcium-binding protein found to be associated with the signal-sequence receptor in endoplasmic reticulum membranes.
Proceedings of the National Academy of Sciences of the United States of America © 1992 National Academy of Sciences