Virus-like Bodies in a Transplantable Mouse Plasma Cell Tumour

Nature ◽  
1958 ◽  
Vol 181 (4617) ◽  
pp. 1213-1214 ◽  
Author(s):  
A. F. HOWATSON ◽  
E. A. McCULLOCH
1971 ◽  
Vol 125 (1) ◽  
pp. 241-247 ◽  
Author(s):  
Fritz Melchers

Incorporation of radioactive fucose into the immunoglobulin G1 myeloma protein secreted by mouse plasma-cell tumour MOPC 21 is stereospecific for the l-isomer. Heavy chains of the secreted form of the myeloma protein carry 90% of the label in fucose residues of their carbohydrate moieties. A small but significant amount of the intracellular immunoglobulin G1 of the mouse plasma-cell tumour MOPC 21 appears to be labelled. Serum in the incubation medium supplies low-molecular-weight diffusible substances necessary to maintain continuous secretion of fucose-labelled myeloma protein beyond 2–3h, and of leucine-labelled myeloma protein beyond 6–8h. In medium containing extensively dialysed serum the secretion of leucine- and fucose-labelled myeloma protein can be restored by the addition of 250μm-d-mannose, 250μm-d-galactose and 250μm-glucosamine. Synthesis and secretion appear to be facilitated in the presence of these sugars, although secretion of myeloma protein devoid of terminal fucose residues is possible for a limited time-period.


1971 ◽  
Vol 125 (1) ◽  
pp. 235-240 ◽  
Author(s):  
R. M. E. Parkhouse ◽  
Fritz Melchers

Incorporations of radioactive mannose, galactose and fucose into MOPC 104E mouse plasma-cell tumour suspensions suggest a stepwise addition of carbohydrate residues to immunoglobulin M (IgM) during the process of secretion. Mannose and glucosamine residues are added at an early stage, whereas galactose and fucose are added just before, or at the time that, IgM leaves the cell. Free light chains secreted in excess by the same tumour cells incubated with mannose, galactose or fucose contained barely detectable amounts of radioactivity.


1962 ◽  
Vol 116 (4) ◽  
pp. 423-432 ◽  
Author(s):  
Richard A. Rifkind ◽  
Elliott F. Osserman ◽  
Konrad C. Hsu ◽  
Councilman Morgan

Ferritin- and fluorescein-conjugated antibody staining has been applied to a study of a mouse plasma cell tumor. The presence of myeloma globulin within cisternae of the endoplasmic reticulum was observed at a stage of the secretory process when the remainder of the cytoplasm was essentially free of labeled globulin. The distribution of ferritin suggested a functional heterogeneity among units of the endoplasmic reticulum. Apparently, progressive accumulation of globulin results in distension of the endoplasmic reticulum and, occasionally, in the appearance of considerable quantities of this secretory protein in the extracisternal cytoplasmic matrix. Participation of the Golgi apparatus in the packaging and release of small quantitites of globulin seems likely. In addition, however, fragmentation of the peripheral cytoplasm with rupture of distended ergastoplasmic vesicles appeared to be another pathway whereby globulin is secreted.


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