Selective removal of alpha heavy-chain glycosylation sites causes immunoglobulin A degradation and reduced secretion.
نویسندگان
چکیده
منابع مشابه
Glycosylation causes an apparent block in translation of immunoglobulin heavy chain.
Analysis of nascent heavy chains isolated from MPC11 (gamma 2b heavy chains) and MOPC 21 (gamma 1 heavy chains) mouse myeloma cells demonstrates an accumulation of nascent heavy chains which are slightly smaller in mass (approximately 35,000 daltons) than nascent heavy chains which have just been glycosylated (approximately 38,000 daltons). The accumulation of 35,000-dalton nascent heavy chain ...
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Immunoglobulin heavy-chain-associated amyloidosis.
Immunoglobulin- or multiple myeloma-associated amyloidosis has been distinguished by the tissue deposition of Congophilic, fibrillar protein consisting of light chains or light-chain fragments (AL amyloidosis). We now report the isolation and characterization of another form of immunoglobulin-associated amyloid obtained from a patient who had extensive systemic amyloidosis and in whom the amylo...
متن کاملMouse myeloma cells that make short immunoglobulin heavy chains: pleiotropic effects on glycosylation and chain assembly
Two variants in immunoglobulin heavy chain production, derived from the MPC 11 mouse myeloma cell line, make short heavy (H) chains with identical precise deletions of the CH3 domain. The CH3 domain is expressed in the H chain mRNA from both variants. Although in vitro translation of this mRNA produces one H chain species, deleted heavy chains are secreted as heavy-light (HL) and H2L2 moieties ...
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ژورنال
عنوان ژورنال: Molecular and Cellular Biology
سال: 1988
ISSN: 0270-7306,1098-5549
DOI: 10.1128/mcb.8.10.4197