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  • Articles  (12)
  • lysosomes  (12)
  • Wiley-Blackwell  (12)
  • 1980-1984  (12)
  • Medicine  (12)
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  • Articles  (12)
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  • 1
    Electronic Resource
    Electronic Resource
    Intracellular accumulation of a fluorescent derivative of paromomycin in human fibroblasts (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 71-80 
    Details
    ISSN: 0730-2312
    Keywords: aminoglycoside ; fluorescent paromomycin ; human fibroblasts ; lysosomes ; endocytosis ; exocytosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Human fetal lung fibroblasts grown in the presence of dansyl-paromomycin (DNS-Pm), a fluorescent derivative of the aminoglycoside antibiotic, paromomycin, probably accumulate DNS-Pm in the lysosomes. The intracellular concentration of DNS-Pm is proportional to the extracellular concentration and to the length of time cells are exposed to the compound. The accumulation of DNS-Pm by human fibroblasts continued to increase for several days, reaching a saturation after 7 days. The kinetic data are consistent with the establishment of a steady state in the cell between fluid-phase pinocytosis and exocytosis of DNS-Pm. About 80% of the intracellular DNS-Pm was released in 24 hr when fresh medium without the analogue was added. The residual 20% remained within the cells, suggesting that it may be irreversibly bound to the lysosomes, endoplasmic reticulum, or ribosonius. The uptake of paromomycin by cells in culture may be a useful means to study error propagation during growth and lifespan of cells in vitro.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200108
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  • 2
    Electronic Resource
    Electronic Resource
    Intracellular processing of 125I-epidermal growth factor in rat embryo fibroblasts (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 259-276 
    Details
    ISSN: 0730-2312
    Keywords: epidermal growth factor ; intracellular processing ; endocytosis ; lysosomes ; degradation ; internalization ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The intracellular fate of endocytosed 125I-epidermal growth factor was examined in Rat-1 fibroblasts. Cells were pulse-labeled for 5 min in 125I-EGF and chased for 3 hr with an excess of unlabeled EGF. At various times after application of the cold chase, cells were harvested and processed for isopycnic gradient centrifugation on Percoll gradients. Within the period of the 125I-EGF pulse, about 50% of the 125I activity appeared in an organelle containing peak in the gradients. By 20 min after application of the cold chase, 125I activity in the organelle peak began to decrease, and the decrease continued over the next few hours. The 125I activity which exited from its organelle-associated location appeared to be present in the cytosol and was apparently not confined within organelles. Lysosomotropic amines inhibited the egress of 125I activity from the organelle compartment. The 125I activity from both organelle and nonorganelle compartments reacted as completely as authentic 125I-EGF with anti-EGF antibodies and was similar in size to authentic 125I-EGF. Little or no intracellular low molecular weight 125I-containing compounds were detected, although they accumulated in the culture medium. Analytical isoelectric focusing revealed that the organelle-bound form of endocytosed 125I-EGF was more acidic than authentic 125I-EGF and, upon exiting from the organelle compartment, was processed to an even more acidic form. It was the second macromolecular form of processed 125I-EGF that was ultimately degraded to low molecular weight compounds which were then externalized from the cells.
    Additional Material: 11 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200306
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  • 3
    Electronic Resource
    Electronic Resource
    Replacement perfusion of cultured eucaryotic cells: A method for the accurate measurement of the rates of growth, protein synthesis, and protein turnover (1984)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 26 (1984), S. 47-64 
    Details
    ISSN: 0730-2312
    Keywords: cellular growth ; protein synthesis ; protein turnover ; lysosomes ; proteolysis ; myeloma ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The fractional rates of protein synthesis (ks) and degradation (kp) were studied in the myeloma cell line SP2/0-AG14 grown at different rates (kg). Cells in spinner flask suspension cultures were maintained at constant cellular density for prolonged periods by replacement perfusion of labeling medium at a rate equivalent to the rate of growth. Total protein synthesis was calculated from the specific-radioactivity of labeled L-leucine in the precursor (medium) and cellular protein. Fractional synthesis rates determined by approach to equilibrium labeling were the same as those determined by equilibrium-pulse labeling kinetics and pulse-chase kinetics. The rate of protein degradation was determined from the established relationship kg = ks - kp. Protein synthesis rates remained constant over a threefold range in the rate of cell growth. At relatively slow growth rates (kg = 0.017/hr) turnover represented a major fraction of total synthesis (kp = 0.032/hr = 0.65ks). At rapid growth rates (kg = 0.058/hr) the value of kp was less than 0.005/hr. No major difference was observed between the ks determined for individual cellular proteins (separated by SDS-polyacrylamide (7.5%) gel electro-phoresis) from rapid- and slow-growing cultures. Thus, with an invariable ks, any change in growth rate is due to an inverse change in the rate of turnover. Since turnover is the balance between synthesis and degradation and since synthesis is unchanging then changes in the growth rate of SP2/0-AG14 should be due to changes in the rate of protein degradation. Experiments were therefore performed to determine the origin of the degradative machinery, ie, cytosolic or lysosomal; autolysis of prelabeled cellular protein (in vitro) was observed only at acidic pH (4.2) and WUS totally inhibited by addition of lcupcptin (10 μM) and pepstatin (2 μM), the specific inhibitors of lysosomal cathepsins B (L) and D, respectively. Since growth rate appears to be regulated by the alterations in the rate of protein degradation and degradation (in vitro) in SP2/0-AG14 appearsto be lysosomal, then one should be able to alter the rate of cellular growth by interfering with rate of lysosomal proteolysis. Indeed, when the lysosomotropic amine NH 4Cl (10 mM) is added to cells growing with a kg of 0.018/hr ± 0.001 (ks = 0.050/hr ± 0.002) the growth rate increased to 0.051/hr ± 0.002 without change in the rate of protein synthesis (ks = 0.049/hr ± 0.003). It is suggested from our data that the cellular growth rate of SP2/0-AG14 is regulated by the lysosomal apparatus; whether this regulation is itself regulated by either a specific compartmentalization of the lysosomal proteinases and/or their substrates or by endogenous protease inhibitors, should prove to be an exciting area for future investigation.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240260105
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  • 4
    Electronic Resource
    Electronic Resource
    The uptake of swainsonine, a specific inhibitor of α-D-mannosidase, into normal human fibroblasts in culture (1983)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 21 (1983), S. 107-117 
    Details
    ISSN: 0730-2312
    Keywords: swainsonine ; lysosomes ; α-D-mannosidase ; uptake ; human fibroblasts ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Swainsonine, an indolizidine alkaloid, found in plants of the genus Swainsona, has been shown to be a strong inhibitor in vitro of the α-D-mannosidase activity in normal human fibroblasts. Therefore, inhibition of α-D-mannosidase activity in extracts of harvested cells grown with swainsonine in the medium has been used to follow the association of the alkaloid with normal human fibroblasts in culture. Swainsonine that could not be removed by extensive washing became associated with the cells within 1 min, and it is concluded that the alkaloid is internalized rapidly by the cells. The amount of swainsonine taken up into the cells depended on the length of time in contact and the concentration of swainsonine in the medium, but at 37°C a plateau of internalized swainsonine occurred after 2 hr with extracellular concentrations of swainsonine of 100 μM or greater. At lower concentrations of swainsonine the rate of uptake was found to be temperature-dependent, increasing greatly at 20°C. The rapidity and temperature sensitivity of the uptake, together with the observation that mannose or mannose-6-phosphate did not prevent the association, suggest that swainsonine enters the cells by permeation rather than by endocytosis. When swainsonine is withdrawn from the culture medium, there is a decrease with time of cell-associated swainsonine. The kinetics of uptake and release of swainsonine and its slightly basic nature make it likely that swainsonine is concentrated initially in the lysosomes. This rapid, but reversible, concentration of swainsonine in lysosomes would be consistent with the observed effects of the toxin in vivo.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240210202
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  • 5
    Electronic Resource
    Electronic Resource
    Involvement of multiple subcellular compartments in intracellular processing of epidermal growth factor (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 20 (1982), S. 41-50 
    Details
    ISSN: 0730-2312
    Keywords: hormone receptors ; Golgi ; lysosomes ; Percoll gradient ; endocytosis ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The intracellular translocation and processing of epidermal growth factor (EOF) in 3T3 cells has been studied utilizing Percoll density gradients. EGF is internalized and rapidly becomes associated with two types of intracellular compartments. The extent to which EGF is delivered to these two compartments is apparently regulated depending upon the cell's physiological condition. In growth medium, an increased proportion of EGF is taken up into a Golgi-like element. Uptake through this pathway correlates with a decrease in degradation of the ligand. In the absence of scrum and amino acids, an increased proportion of EGF is taken up into a component which has a density of 1.05. Uptake through this pathway correlates with increased degradation of the ligand. The ligand taken up through both pathways is transferred to dense vesicles which comigrate with lysosomes. In the presence of growth medium, however, dense vesicles containing EGF can be shown to be lysosomal enzyme-deficient upon further fractionation. In addition, in the presence of serum, a portion of the internalized EGF is apparently released from the cells, intact, and then re-bound. The processes described may be important in the production of a mitogenic response and the ability of cells to self-regulate their responsiveness to the growth factor.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240200105
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  • 6
    Electronic Resource
    Electronic Resource
    Subcellular structures involved in internalization and degradation of epidermal growth factor (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 15 (1981), S. 235-251 
    Details
    ISSN: 0275-3723
    Keywords: EGF ; coated vesicles ; internalization ; lysosomes ; NH4C1 ; hormone degradation ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Epidermal Growth Factor (EGF), a small polypeptide which acts as a mitogen for many cell types, has previously been shown to bind to a specific plasma membrane receptor on 3T3 cells. If 125I-EGF is bound to 3T3 cells for one hour at 4°C, it remains predominantly associated with the plasma membrane-containing fractions obtained by subjecting cell supernatants to equilibrium sedimentation on sucrose gradients. When binding is followed by a 10-minute incubation at 37°C, over 50% of the 125I-EGF is associated with two internal membrane-containing peaks having higher densities than the plasma membrane. After one hour at 37°C, over 80% of the 125I-EGF is degraded and removed from the cells.The most rapidly labeled internal peak corresponds in density to brain-coated vesicles (CVs). Antiserum prepared against coated vehicles from brain precipitates the 125I-EGF in this peak. In addition, CVs containing 125I-EGF can be co-purified from 3T3 cells exposed to 125I-EGF, using brain as a carrier. Several lines of evidence suggest that the other 125I-EGF-labeled intracellular peak is 125I-EGF in lysosomes.These results provide kinetic and biochemical evidence for a unidirectional pathway for EGF catabolism by 3T3 cells. EGF first binds to the plasma membrane bound receptors, is then moved to the cytoplasm in CVs, and finally appears in lysosomes, where it is degraded and released from the cells. Ten-millimolar NH4Cl blocks lysosomal hydrolysis of EGF almost completely. Subsequently, EGF internalization is inhibited. This finding suggests that the pathway for EGF internalization and degradation is tightly coupled.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380150304
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  • 7
    Electronic Resource
    Electronic Resource
    Possible mechanism for target cell lysis by cytotoxic T-cells (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 2 (1984), S. 89-94 
    Details
    ISSN: 0263-6484
    Keywords: Immunology ; cytotoxic T cells ; lysosomes ; quantitative cytochemistry ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The mechanism of the lysis of target cells by cytotoxic T-cells (Tc) is still obscure; there is no evidence for transfer of material from the Tc and prior to lysis, despite intimate contact, the plasma membranes of both types of cell appear to remain intact. The effects on the target cell lysosomes of brief contact between anti-viral Tc and targets bearing both the appropriate histocompatibility and viral antigens, have been examined cytochemically. Both the distribution of acid phosphatase activity and the percentage bound lysosomal naphthylamidase activity indicated that, in virus-infected target cells exposed to Tc, the lysosomal membranes became totally labilized. Thus the contact between Tc and targets appears to cause sufficient perturbation of the target plasma membrane as to cause the intracellular release of some agent that activates ‘suicide capsule’ lysosomes.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290020207
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  • 8
    Electronic Resource
    Electronic Resource
    Haemosiderin and tissue damage (1984)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 2 (1984), S. 186-194 
    Details
    ISSN: 0263-6484
    Keywords: Iron ; ferritin ; haemosiderin ; lysosomes ; haemochromatosis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: High levels of haemosiderin occur in iron overload syndromes such as idiopathic haemochromatosis or secondary iron overload in thalassaemic patients; haemosiderin is the predominant iron-storage compound in such cases. It consists of a large aggregate of FeOOH cores, many of which have an incomplete shell of protein, and is probably derived from ferritin by lysosomal proteolysis. In addition, some chemical degradation of the ferritin cores appears to occur on conversion to haemosiderin. Other biochemical components are phosphate and magnesium, which may be adsorbed to the core surface, and perhaps certain lipids. Haemosiderin may have a central role, either directly or indirectly, in iron cytotoxicity and therefore the chemistry and biochemistry of this material warrants further study.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290020402
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  • 9
    Electronic Resource
    Electronic Resource
    Genetics of receptors for bioactive polypeptides: A variant of swiss/3T3 fibroblasts resistant to a cytotoxic insulin accumulates lysosome-like vesicles (1981)
    New York, NY : Wiley-Blackwell
    Journal of Supramolecular Structure and Cellular Biochemistry 16 (1981), S. 105-113 
    Details
    ISSN: 0275-3723
    Keywords: hormone receptors ; diphtheria toxin ; lysosomes ; hybrid proteins ; Chemistry ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Recently we have isolated six variants of Swiss/3T3 mouse fibroblasts that are resistant to the cytotoxic insulin-diphtheria toxin A fragment. All of the variants proved to have greatly reduced or no insulin binding capacity, and several variants showed altered morphologies and growth characteristics. We now report on the further characterization of one of these variants, CI-3. which displays a massive accumulation of membranous vesicles in its cytoplasm. By electron microscopy these vesicles resemble lysosomes. They also appear to fluorcsce bright orange after treatment of viable cells with acridine orange. However, the specific activity of several lysosomal enzymes is depressed in CI-3. Additionally, there is an apparent shift in the density of vesicles containing lysosomal enzymes in this variant. These alterations may be directly related to CI-3′s resistance to the cytotoxic insulin and have some important bearings on the mechanism of insulin action.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jsscb.1981.380160110
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  • 10
    Electronic Resource
    Electronic Resource
    Quantitative cytochemistry of blood neutrophils in myelodysplastic syndromes and chronic granulocytic leukaemia (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Cell Biochemistry and Function 1 (1983), S. 92-96 
    Details
    ISSN: 0263-6484
    Keywords: Blood cells ; leukaemia ; myelodysplasia ; cytochemistry ; neutrophils ; microdensitometer ; lysosomes ; preleukaemia ; maturation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Quantitative cytochemistry of components of blood neutrophil azurophilic granules (myeloperoxidase, chloroacetate esterase, β-glucuronidase, and acid phosphatase) and specific granules (lactoferrin) has been performed by scanning and integrating micro-densitometry in 13 patients with a myelodysplastic syndrome and 11 patients with chronic granulocytic leukaemia. Both patient groups showed a reduction of enzyme activity in azurophilic granules, and also of lactoferrin, consistent with abnormal development of neutrophil granules. These cytochemical changes in blood neutrophils are similar to those found in acute myeloid leukaemia, are consistent with a leukaemic maturation defect, and may be of diagnostic value.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cbf.290010209
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