ARTICLE

IMMUNOGLOBULIN SYNTHESIS AND SECRETION : II. Radioautographic Studies of Sites of Addition of Carbohydrate Moieties and Intracellular Transport

Daniel Zagury ¹, Jonathan W. Uhr ¹, James D. Jamieson ¹, and George E. Palade ¹

¹ From Irvington House Institute and the Department of Medicine, New York University School of Medicine, New York 10016; and from the Department of Cell Biology, The Rockefeller University, New York 10021.

Dr. Zagury's address is Laboratoire de Microscopie Electronique appliquée à la Biologie du C.N.R.S. (Centre National de la Recherche Scientifique), 75-Paris, France

The subcellular sites of synthesis and route of intracellular transfer of immunoglobulin G (IgG) have been investigated by electron microscope radioautography with precursors used for the polypeptide chain (leucine-³H) and for the carbohydrate moieties (galactose-³H and glucosamine-³H). For this purpose, plasma cells from a mouse myeloma tumor were labeled with appropriate precursors and the distribution of radioautographic grains was determined at the end of the labeling period and after varying times of incubation in unlabeled medium. The results indicated that the polypeptide backbone is synthesized in a region of the cell occupied by the rough endoplasmic reticulum (RER) and is transported from there to the region of the Golgi complex. Galactose is incorporated in IgG primarily at the level of the Golgi complex, whereas the incorporation of glucosamine appears to take place both in the RER and in the Golgi complex. From the Golgi complex, the completed IgG molecules reach the plasma membrane and are discharged extracellularly. The latter route of transport and the mechanism of discharge are not understood but may be mediated via smooth-surfaced vesicles.

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