Journal
JOURNAL OF IMMUNOLOGY
Volume 164, Issue 9, Pages 4713-4719Publisher
AMER ASSOC IMMUNOLOGISTS
DOI: 10.4049/jimmunol.164.9.4713
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- NCI NIH HHS [CA 69618] Funding Source: Medline
- NIAID NIH HHS [AI 33507] Funding Source: Medline
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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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