Subcellular localization of ferritin and iron taken up by rat hepatocytes. 1989

J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461.

The subcellular localization of ferritin and its iron taken up by rat hepatocytes was investigated by sucrose-density-gradient ultracentrifugation of cell homogenates. After incubation of hepatocytes with 125I-labelled [59Fe]ferritin, cells incorporate most of the labels into structures equilibrating at densities where acid phosphatase and cytochrome c oxidase are found, suggesting association of ferritin and its iron with lysosomes or mitochondria. Specific solubilization of lysosomes by digitonin treatment indicates that, after 8 h incubation, most of the 125I is recovered in lysosomes, whereas 59Fe is found in mitochondria as well as in lysosomes. As evidenced by gel chromatography of supernatant fractions, 59Fe accumulates with time in cytosolic ferritin. To account for these results a model is proposed in which ferritin, after being endocytosed by hepatocytes, is degraded in lysosomes, and its iron is released and re-incorporated into cytosolic ferritin and, to a lesser extent, into mitochondria.

UI MeSH Term Description Entries
D007501 Iron A metallic element with atomic symbol Fe, atomic number 26, and atomic weight 55.85. It is an essential constituent of HEMOGLOBINS; CYTOCHROMES; and IRON-BINDING PROTEINS. It plays a role in cellular redox reactions and in the transport of OXYGEN. Iron-56,Iron 56
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D008247 Lysosomes A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured or undergoes MEMBRANE FUSION. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed). Autolysosome,Autolysosomes,Lysosome
D008930 Mitochondria, Liver Mitochondria in hepatocytes. As in all mitochondria, there are an outer membrane and an inner membrane, together creating two separate mitochondrial compartments: the internal matrix space and a much narrower intermembrane space. In the liver mitochondrion, an estimated 67% of the total mitochondrial proteins is located in the matrix. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p343-4) Liver Mitochondria,Liver Mitochondrion,Mitochondrion, Liver
D002458 Cell Fractionation Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS. Cell Fractionations,Fractionation, Cell,Fractionations, Cell
D003600 Cytosol Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components. Cytosols
D005293 Ferritins Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types. Basic Isoferritin,Ferritin,Isoferritin,Isoferritin, Basic
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
August 1972, Endocrinology,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
February 1989, Biochimica et biophysica acta,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
February 1993, Clinical and investigative medicine. Medecine clinique et experimentale,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
October 1980, Biochimica et biophysica acta,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
April 1993, Alcoholism, clinical and experimental research,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
March 1985, Zhonghua yi xue za zhi,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
January 1989, Acta biochimica Polonica,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
January 1968, Acta physiologica Scandinavica,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
June 1981, Biochimica et biophysica acta,
J C Sibille, and M Ciriolo, and H Kondo, and R R Crichton, and P Aisen
January 1998, Journal of biochemistry,
Copied contents to your clipboard!