MORPHOLOGICAL ASPECTS OF PROTEIN SYNTHESIS
ABSTRACT Morphological aspects of protein synthesis have been mainly investigated by means of high resolution radioautography. Most of the cellular proteins are synthesized in the rough endoplasmic reticulum and on free cytoplasmic polysomes. Only few structural proteins (sedentary protein) remain in the vicinity of their sites of synthesis. The great majority of the newlysynthesized proteins move away (migratory protein). One portion of the migratory proteins is redistributed to various cell organelles and is referred to as "non exportable" protein. The migration of polypeptide chains from cytoplasmic polysomes ensures the renewal of protein in mitochondria, nucleus, and specialized membranes, in spite of the capacity of these organelles to incorporate slightly labelled amino acids. Plasma membrane precursors undergo a series of intracellular translocations and molecular complexification by adding carbohydrate groups before they reach the cell surface. Another portion of the migratory proteins, which includes secretory products, is referred to as "exportable" proteins. These exportable proteins are conveyed from the rough endoplasmic reticulum to the Golgi apparatus, then either stored and condensed in secretory granules or directly released by exocytosis. In some differentiated cells, the development of the cellular machinery for the synthesis of protein is triggered and maintained by the level of steroid hormones which controls both the quality and the quantity of secreted proteins.