Topology of Asialoglycoprotein Receptor in Rat Liver Subcellular Fractions: A Ferritin Immunoelectron Microscopic Study

• Published in: Cell Structure and Function Vol. 9; no. 4; pp. 391 - 406
• Main Authors: Nakada, Hiroshi, Matsuura, Shiro, Sawamura, Takaya, Tashiro, Yutaka
• Format: Journal Article
• Language: English
• Published: Kyoto Japan Society for Cell Biology 01-01-1984
• Subjects: Animals; Asialoglycoprotein Receptor; Biological and medical sciences; Cell Membrane - metabolism; Cell receptors; Cell structures and functions; Ferritins; Fundamental and applied biological sciences. Psychology; Golgi Apparatus - metabolism; Histocytochemistry; Liver - metabolism; Liver - ultrastructure; Male; Microscopy, Electron; Microsomes, Liver - metabolism; Molecular and cellular biology; Rats; Rats, Inbred Strains; Receptors, Immunologic - metabolism; Subcellular Fractions - metabolism; Vertebrata; Membrane receptor; Mammalia; Rat; Liver; Rodentia
• ISSN: 0386-7196; 1347-3700
• DOI: 10.1247/csf.9.391

Direct ferritin immunoelectron microscopy was used to visualize the asialoglycoprotein receptor in various rat liver subcellular fractions. The cytoplasmic surfaces of cytoplasmic organelles such as the rough and smooth microsomes, Golgi cisternae and lysosomes showed hardly any ferritin label exception for the slight labeling of secretory granules found mainly in the light Golgi fraction (GF1). Occasionally, however, open membrane sheet structures, smooth vesicular or tubular structures heavily labeled with ferritin, were present in all these subcellular fractions. These structures probably cor-respond to fragmented sinusoidal or lateral hepatocyte plasma membranes recovered to these subcellular fractions. When the limiting membranes of the secretion granules were partially broken by mechanical force, a number of ferritin particles frequently were seen attached in large clusters to the luminal surface of the membrane, the cytoplamsic surface of the corresponding domain being slightly labeled. These observations are strong evidence that the receptor protein is never translocated vertically throughout the intracellular transport from ER to plasma membrane via Golgi apparatus and from plasma membrane back to trans-Golgi elements and also in lysosomes, always exposing the major antigenic sites to the luminal or extracellular surface and the minor counter-parts to the cytoplasmic surface of the membranes. The receptor protein also is suggested to be concentrated in clusters on the luminal surface of secretion granules when they form on the trans-side of the Golgi apparatus.