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H. Haigler, J. Mckanna, S. Cohen (1979)
Direct visualization of the binding and internalization of a ferritin conjugate of epidermal growth factor in human carcinoma cells A-431The Journal of Cell Biology, 81
(1977)
In vitro absorption of peroxidase-conjugated IgG by human placental villi
(1978)
Molecular mechanisms of mitogen action : Processing of receptor induced by epidermal growth factor
Jon LaBadie, Kristi Chapman, N. Aronson (1975)
Glycoprotein catabolism in rat liver: Lysosomal digestion of iodinated asialo-fetuin.The Biochemical journal, 152 2
(1978)
Traffic of products and membranes through the Golgi complex
(1978)
Degradation ofreceptor-bound human choringonadotropin by marine Leydig tumor cells
D. Fawcett (1965)
SURFACE SPECIALIZATIONS OF ABSORBING CELLSJournal of Histochemistry and Cytochemistry, 13
(1978)
1211_ Insulin binding to cultured human lymphocytes. Initial localization and fate of hormone determined by quantitative electron microscopic autoradiography
(1979)
Binding and uptake of "''I-insulin into rat liver hepatocytes and endothelium
(1964)
Yolk protein uptake into the oocyte of the mosquito
A. Hubbard, Z. Cohn (1975)
Externally disposed plasma membrane proteins. I. Enzymatic iodination of mouse L cellsThe Journal of Cell Biology, 64
Nelson Dm, Smith Rm, L. Jarett (1978)
Nonuniform Distribution and Grouping of Insulin Receptors on the Surface of Human Placental Syncytial TrophoblastDiabetes, 27
M. Salpeter, H. Fertuck, E. Salpeter (1977)
Resolution in electron microscope autoradiography. III. Iodine-125, the effect of heavy metal staining, and a reassessment of critical parametersThe Journal of Cell Biology, 72
G. Carpenter, S. Cohen (1976)
125I-labeled human epidermal growth factor. Binding, internalization, and degradation in human fibroblastsThe Journal of Cell Biology, 71
W. Pricer, G. Ashwell (1976)
Subcellular distribution of a mammalian hepatic binding protein specific for asialoglycoproteins.The Journal of biological chemistry, 251 23
G. Gregoriadis, A. Morell, I. Sternlieb, I. Scheinberg (1970)
Catabolism of desialylated ceruloplasmin in the liver.The Journal of biological chemistry, 245 21
(1972)
Degradatio n of ""1-insulin by rat liver. Studies in vitro
We would like to thank Ms. A. Ma for technical assistance , Ms . J. Reid for the ARG grain and point counting, Ms. L. Herzman for preparation of the manuscript
G. Wilson, G. Ashwell, H. Stukenbrok (1979)
An electron microscope autoradiographic study of the carbohydrate recognition systems in rat liver. I. Distribution of 125I-ligands among the liver cell typesThe Journal of Cell Biology, 83
E. Wisse (1972)
An ultrastructural characterization of the endothelial cell in the rat liver sinusoid under normal and various experimental conditions, as a contribution to the distinction between endothelial and Kupffer cells.Journal of ultrastructure research, 38 5
Intracellular Fates of Rat Liver 125 '7-Ligands
J. Goldstein, M. Brown (1977)
The low-density lipoprotein pathway and its relation to atherosclerosis.Annual review of biochemistry, 46
T. Brown, L. Henderson, S. Thorpe, J. Baynes (1978)
The effect of α-mannose-terminal oligosaccharides on the survival of glycoproteins in the circulation
L. Orci, L. Orci, J. Carpentier, J. Carpentier, A. Perrelet, A. Perrelet, Richard Anderson, Richard Anderson, Joseph Goldstein, Joseph Goldstein, Michael Brown, Michael Brown (1978)
Occurrence of low density lipoprotein receptors within large pits on the surface of human fibroblasts as demonstrated by freeze-etching.Experimental cell research, 113 1
Stenard-Ossorio for photographic work, and Dr
R. Anderson, J. Goldstein, Michael Brown (1976)
Localization of low density lipoprotein receptors on plasma membrane of normal human fibroblasts and their absence in cells from a familial hypercholesterolemia homozygote.Proceedings of the National Academy of Sciences of the United States of America, 73 7
P. Gorden, J. Carpentier, S. Cohen, L. Orci (1978)
Epidermal growth factor: morphological demonstration of binding, internalization, and lysosomal association in human fibroblasts.Proceedings of the National Academy of Sciences of the United States of America, 75 10
R. Przybylski (1961)
Electron microscope autoradiography.Experimental cell research, 24
T. Roth, J. Cutting, S. Atlas (1976)
Protein transport: a selective membrane mechanism.Journal of supramolecular structure, 4 4
D. Achord, F. Brot, A. González-Noriega, W. Sly, P. Stahl (1977)
Human β-GIucuronidase. II. Fate of Infused Human Placental β-Glucuronidase in the RatPediatric Research, 11
(1979)
Received for publication 5 March 1979, and in revised form 11
P. Gorden, J. Carpentier, P. Freychet, A. LeCam, L. Orci (1978)
Intracellular translocation of iodine-125-labeled insulin: direct demonstration in isolated hepatocytes.Science, 200 4343
Electron microscope autoradiographic and biochemical methods were used to study the intracellular fates of several 125I-glycoproteins, known to be specifically bound and internalized by the different cell types in the liver. At the earliest times examined (1--2 min), 125I-glycoproteins (ASGP) were localized predominantly along the sinusoidal front of hepatocytes. Analysis of the distribution of autoradiographic grains indicated that: (a) approximately 40--60% of the 125I-ligand could be ascribed to the plasmalemma; (b) a significant fraction had already been internalized; yet (c) very little 125I-ligand was present in the lysosome-Golgi region. Between 4 and 15 min after administration of 125I-ASGPs, there was a dramatic redistribution of autoradiographic grains from regions of the plasmalemma and peripheral cytoplasm (30% decrease) to the lysosome-Golgi region (30% increase). At longer times (30 min), there was continued drainage of 125I-ASGP into this region. The grain density over secondary lysosomes was 60--90 times higher than that over recognizable Golgi elements, clearly indicating that lysosomes were the ultimate destination of the 125I-ASGP. However, no more than 60% of the total 125I-ligand could be localized to lysosome-rich regions of the hepatocyte, with the remaining 40% primarily in the intermediate cytoplasm. Biochemical evidence for proteolysis of the internalized 125I-ASGP (presumably within lysosomes) was obtained when 125I-mono-iodotyrosine was found in the liver (i.e., hepatocytes) at times later than 15 min. The temporal redistribution observed for mannose and N-acetylglucosamine-terminated glycoproteins (ahexosamino-orosomucoid and agalacto-orosomucoid, respectively) in endothelial cells indicated that the 125I-ligands resided in macropinocytic vesicles (1--15 min) before their ultimate residence in dense bodies (15 min). The same 125I-ligands were also localized to structures resembling secondary lysosomes in Kupffer cells. The lysosomal nature of "these organelles" was implied from the appearance of 125Imono-iodotyrosine in the liver at later times. 125I-beta-glucuronidase followed the same intracellular pathway in both cell types but was not degraded.
The Journal of Cell Biology – Rockefeller University Press
Published: Oct 1, 1979
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