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. 1992 Sep 15;89(18):8452–8456. doi: 10.1073/pnas.89.18.8452

The major histocompatibility complex class I antigen-binding protein p88 is the product of the calnexin gene.

K Galvin 1, S Krishna 1, F Ponchel 1, M Frohlich 1, D E Cummings 1, R Carlson 1, J R Wands 1, K J Isselbacher 1, S Pillai 1, M Ozturk 1
PMCID: PMC49938  PMID: 1326756

Abstract

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 [35S]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 mu heavy chains and may serve as a chaperone for many membrane-bound polypeptides. A partial human p90 cDNA was cloned from a lambda gt11 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.

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Selected References

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