Abstract
The effects of vinblastine on protein and lipid synthesis in rat liver have been studied with special consideration to the synthesis of albumin and lipoprotein particles (presumed VLDL) and their intracellular migration and secretion. Vinblastine inhibits secretion of VLDL and albumin, but does not seem to alter the rate of [ 14C]leucine labeling of microsomal protein. [ 14C]Glycerol labeling of phospholipids and triglycerides, however, decreases following vinblastine administration. VLDL-like particles accumulate in secretory vesicles close to the cell border. In addition VBL partially blocks the translocation of albumin and lipoprotein particles from the ER and increases the albumin and TG content in isolated microsomes and Golgi apparatus. VBL does not affect the gross lipid composition of isolated lipoprotein particles. Degradation of the accumulated secretory material takes place in lysosomes. Sequestration into the lysosomal compartment of the content of secretory vesicles occurs by two mechanisms in parallel, namely, by means of classical autophagy and by means of crinophagy, i.e., either by uptake of the entire secretory vesicles in forming autophagic vacuoles or by direct fusion of a secretory vesicle with a lysosome.
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