Prelysosomal convergence of autophagic and endocytic pathways

• Published in: Biochemical and biophysical research communications Vol. 151; no. 1; pp. 40 - 47
• Main Authors: Gordon, Paul B., Seglen, Per O.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 29.02.1988; Elsevier
• Subjects: Animals; Asparagine - pharmacology; Autophagy; beta-Galactosidase - metabolism; Biological and medical sciences; Cell physiology; Cells, Cultured; Endocytosis; Fundamental and applied biological sciences. Psychology; Lactose - metabolism; Liver - cytology; Liver - metabolism; Lysosomes - metabolism; Male; Molecular and cellular biology; Phagocytosis; Rats; Rats, Inbred Strains; Vacuoles - metabolism; Vinblastine - pharmacology
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/0006-291X(88)90556-6

[ 14C]Lactose, electroinjected into the cytosol of isolated rat hepatocytes, was sequestered by autophagy, transferred to lysosomes and eventually hydrolysed. Asparagine prevented the fusion between prelysosomal autophagic vacuoles and lysosomes, and caused lactose to accumulate in the former. However, if the hepatocytes were simultaneously allowed to endocytose added β-galactosidase, no lactose accumulation occurred. These results suggest that autophagically sequestered lactose and endocytosed β-galactosidase were delivered to the same prelysosomal vacuole, where the lactose was hydrolysed by the enzyme. The name amphisome is suggested for this new functional compartment, common to the autophagic and endocytic pathways.