Department of Molecular Genetics and Microbiology
Animals; B-Lymphocytes; Cell Line; Hybridomas; Immunoglobulin A; Immunoglobulin Heavy Chains; Immunoglobulin alpha-Chains; Lymphoma; Mice; Molecular Weight; Nucleic Acid Hybridization; Protein Biosynthesis; RNA, Messenger; Transcription, Genetic
Immunology and Infectious Disease | Life Sciences | Medicine and Health Sciences
We have compared the synthesis and processing of immunoglobulin alpha chains in two murine cell lines, a B cell lymphoma that expresses membrane-bound IgA and a hybridoma that secretes IgA. Results of biosynthetic labeling experiments demonstrated that membrane-bound and secreted alpha chains have two distinct intracellular precursors, of different molecular weights and isoelectric points. RNAs from both of these cell lines direct the synthesis in vitro of two alpha polypeptides of Mr 59,000 and 62,000, the larger one being the precursor for membrane-bound alpha chain and the smaller one being the precursor for secreted alpha chain. These cell lines each contain three RNAs, 1.7, 2.1, and 3.1 kilobases in length, which hybridize with cDNA for the alpha constant region and which are present in different concentrations. Our results suggest that the smallest RNA encodes the secreted alpha chain and one or both of the larger RNAs encode(s) the membrane-bound alpha chain.
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Citation: Proc Natl Acad Sci U S A. 1981 Oct;78(10):6436-40. Link to article on publisher's website
Kikutani, H.; Sitia, R.; Good, R. A.; and Stavnezer, Janet, "Synthesis and processing of the alpha heavy chains of secreted and membrane-bound IgA" (1981). Women’s Health Research Faculty Publications. 246.