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Bone marrow pre‐B lymphocytes synthesize immunoglobulin mu chains of membrane type with different properties and intracellular pathways.
Author(s) -
Thorens B.,
Schulz M.F.,
Vassalli P.
Publication year - 1985
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1985.tb03637.x
Subject(s) - biology , intracellular , golgi apparatus , proteolysis , glycosylation , immunoglobulin light chain , compartment (ship) , microbiology and biotechnology , biophysics , biochemistry , antibody , cell , enzyme , genetics , oceanography , geology
Mouse normal bone marrow pre‐B lymphocytes synthesize only membrane mu chains (micron), as shown by mRNA studies and peptide analysis. The micron chains exist in two forms: free micron chains assembled into dimers, or L chain‐bound micron chains present in IgM monomers (in the case of ‘late pre‐B cells’, i.e., after productive L chain gene rearrangement). These two forms of molecules are very different in properties, fate and intracellular pathways. Free but not L chain‐bound mu chains are highly susceptible to mild proteolysis, which degrades their entire Cmu 1 and VH domains. Free mu chains are rapidly degraded within the lysosomal compartment, which they reach via the cis, avoiding the trans, part of the Golgi complex. In contrast, as soon as mu chains bind to L chains, they are directed towards the ‘trans’ Golgi compartment, where they undergo terminal glycosylation, then to the cell surface, where they progressively accumulate. It is suggested that the conformation instability of the Cmu 1 and VH domains of the free mu chains plays a critical role in the intracellular targeting of these molecules, as compared with that of L chain‐bound mu chains.