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Plasma cell immunoglobulin M molecules. Their biosynthesis, assembly, and intracellular transport by A Tartakoff; P Vassalli is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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Immunoglobulin M (IgM)-secreting murine plasmablasts have been used to explore the cytologic site(s) of the successive modifications of the polypeptide H and L chains (steps of glycosylation, chain assembly, and polymerization) which occur during intracellular transport (ICT) and the interrelationships between these events. A combination of pulse- chase biosynthetic labeling protocols (using amino acids and sugars), subcellular fractionation, and electron microscope autoradiography was used in conjunction with inhibitors of glycosylation and agents (carboxyl cyanide m-chlorophenyl hydrazone [CCCP] and monensin) which block Ig exit from the rough endoplasmic reticulum (RER) or Golgi cisternae. The data are consistent with the following conclusions: (1) Sugar addition and modification occur in three main steps: (a) en bloc addition of core sugars to nascent H chains, (b) partial trimming of these oligosaccharide chains in the RER, (c) quasiconcerted addition of terminal sugars (galactose, fucose, and sialic acid) in a very distal compartment between monensin-sensitive Golgi cisternae and the cell surface. (2) H and L chain assembly occurs between nascent H chains and a pool of free l

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Author

A Tartakoff; P Vassalli

Publisher

Rockefeller University Press.; The Rockefeller University Press; Rockefeller University Press; ScienceOpen (ISSN 0021-9525)

Published

1979

Language

EN

Field

Biochemistry, Genetics and Molecular Biology (Life Sciences)