Immunoglobulin Assembly and Secretion

Lina M. Hendershot, Roberto Sitia

Research output: Chapter in Book/Report/Conference proceedingChapter

Abstract

This chapter discusses the mechanism of immunoglobulin (Ig) assembly and secretion. Like all proteins destined to exocytic compartments, heavy chains (HC) and light chains (LC) are co-translationally translocated in the endoplasmic reticulum (ER). In this organelle, they undergo post-translational modifications (that is, folding, assembly, disulfide bond formation, and glycosylation) that play fundamental roles in controlling, both intracellular transport and functional activities of antibodies. In the case of recombination, transcription, and splicing, the studies on Ig synthesis has revealed the basic principles of cell biology that control protein folding, transport, and degradation. These concepts have not only entered text books, but have also contributed to biotechnology and medicine. It looks forward to the experiments aimed at dissecting the adaptive regulation of protein synthesis, cell morphology, and intercellular communication, as the results will surely offer new exploitable paradigms.

Original languageEnglish
Title of host publicationMolecular Biology of B Cells
PublisherElsevier Inc.
Pages261-273
Number of pages13
ISBN (Print)9780080479507, 9780120536412
DOIs
Publication statusPublished - Feb 18 2003

ASJC Scopus subject areas

  • Medicine(all)
  • Immunology and Microbiology(all)

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