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The Journal of Immunology, 2000, 164: 4713-4719.
Copyright © 2000 by The American Association of Immunologists

Accelerated Proteasomal Degradation of Membrane Ig Heavy Chains1

Siew C. Ho2, Subhra Chaudhuri2, Anand Bachhawat3, Kenneth McDonald4 and Shiv Pillai5

Massachusetts General Hospital Cancer Center and Harvard Medical School, Boston, MA 02129

Membrane IgG H chains turn over considerably more rapidly than secretory Ig H chains in the 18-81 A2 pre-B cell line. This rapid degradation occurs in proteasomes. N-Glycosylated membrane Ig H chains accumulate in the endoplasmic reticulum in the presence of proteasomal inhibitors, suggesting that retrotranslocation and proteasomal degradation of membrane Ig H chains may be closely coupled processes. Accelerated proteasomal degradation of membrane Ig H chains was also observed in transfected nonlymphoid cells. At steady state, the membrane form of the H chain associates more readily with Bip and calnexin than its secretory counterpart. The preferential recognition of membrane, as opposed to secretory, Ig H chains by some endoplasmic reticulum chaperones, may provide an explanation for the accelerated proteasomal degradation of the former.




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