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  • Cell & Developmental Biology  (270)
  • Barium; Columbia District, NY, USA; DEPTH, sediment/rock; Description; Dredge; DRG; Elevation of event; Event label; Goodsell_D; Gott-Mesick_D; Iron; Latitude of event; Longitude of event; Manganese; Method/Device of event; NOAA and MMS Marine Minerals Geochemical Database; NOAA-MMS; Palmer_D; Parsons_D; Phosphorus; Wet chemistry
  • 1980-1984  (264)
  • 1915-1919  (7)
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Year
  • 1
    Electronic Resource
    Electronic Resource
    Intracellular concentration of elements in normal and dystrophic skeletal muscles of the chicken (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 103 (1980), S. 193-200 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: In this study, the intracellular concentrations of six elements (mmole/kg dry weight) were directly measured in the muscle fibers of pectoralis major muscles of eight week old, genetically dystrophic and normal chickens by the X-ray microanalysis technique. The extent of muscle degeneration was evaluated by morphometric measurements of muscle fiber diameter and other histological changes. A significant increase in the concentration of intracellular sodium and chlorine was evident in dystrophic muscles. The concentration of intracellular sodium was 127.0 ± 35.0 in the muscle fibers of dystrophic chicks compared to 65.7 ± 16.5 in normal controls. The concentration of chlorine was 90.5 ± 27.5 and 54.1 ± 5.5 in the muscle fibers of dystrophic and normal chicks respectively. The intracellular concentrations of potassium, magnesium, phosphorous, and sulfur remained unchanged in the dystrophic condition. Morphometric studies revealed that the dystrophic pectoralis muscles contain fewer but thicker fibers per unit area compared to normal pectoralis muscles. The importance of these findings are discussed in relation to the results of earlier investigations.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041030204
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  • 2
    Electronic Resource
    Electronic Resource
    Insulin inhibition of protein degradation in cell monolayers (1980)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 105 (1980), S. 335-346 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protein degradation has been measured in confluent monolayers of eleven lines of contact-inhibited cells and ten transformed lines as the rate of release of trichloroacetic acid-soluble radioactivity after prelabeling cell protein with [3H]leucine. Insulin, at concentrations from 10-12 M to 10-6 M, has been added at the beginning of the 4-hour degradation period to detect selective effects of this hormone as an inhibitor of the inducible proteolysis occurring in serumfree medium. In addition insulin binding measurements have been performed on selected cell lines in an attempt to relate receptor properties to insulin action. Substantial effects of insulin are found in most cells with a selective inhibition at low insulin concentrations noted in several of the transformed lines. The difference in insulin sensitivity is not entirely definitive because temperature-sensitive transformation mutants of NRK cells are not more sensitive to insulin at a temperature where they show the transformed phenotype. Although insulin receptors on different cell lines have similar binding properties, two of the hepatomas used, H35 and MH1C1, show inhibition of protein degradation at insulin concentrations where receptor occupancy is extremely low. Calvarial osteoblast-like cells have a high rate of protein degradation which can be reduced by growth factors but not by insulin. The lack of an insulin response is a consequence of poor insulin binding to the cells. Insulin binds to the osteogenic sarcoma cells in substantial amounts. However, its normal action to inhibit the induced proteolysis is restricted because with these cells no increase of proteolysis occurs in serum-free medium. Generally higher rates of protein degradation are observed in the contact-inhibited lines than the transformed cells. We suggest that this difference may provide a selective growth advantage to transformed cells.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041050216
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  • 3
    Electronic Resource
    Electronic Resource
    Nuclear magnetic resonance study of muscle water protons in muscular dystrophy of chickens (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 107 (1981), S. 139-145 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Using the pulsed nuclear magnetic resonance (NMR) spectroscopy, the spin-lattice (T1) and the spin-spin (T2) relaxations times of water protons from samples of pectoralis major muscles of normal (line 412) and homozygous dystrophic (line 413) chickens were measured. Both the T1 and T2 were significantly increased (P 〈 0.05) in the dystrophic muscles. The mean values of the relaxation times are given ± S.D. The T1 values were 654 ± 22 msec in normal and 692 ± 41 msec in dystrophic muscles. The T2 values for normal and dystrophic muscles were 39 ± 4 msec and 52 ± 7 msec, respectively. Although the water content of dystrophic muscles (78.9 ± 0.6%) determined by gravimetric methods was significantly higher than normal muscles (74.9 ± 1.1%), this difference in tissue hydration could not explain quantitatively the increase of T1 and T2 values in the dystrophic muscles. The results of the measurements of the relaxation times seem to suggest that there are changes in the composition and/or conformational state of the proteins.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041070115
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  • 4
    Electronic Resource
    Electronic Resource
    Quantitative analysis of axonemal bends and twists in the quiescent state of ciona sperm flagella (1983)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 3 (1983), S. 247-259 
    Details
    ISSN: 0886-1544
    Keywords: spermatozoa ; Ciona ; axoneme ; quiescence ; twist ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A simple planar model of sliding can predict the amount of sliding required to form a certain degree of bend. The accuracy of this prediction relies on the assumptions that no twists occur in the axoneme and that no sliding occurs at the base. However, previous studies indicated that twists may occur.This paper explores a new method for quantitating and analyzing twists. Preliminary results using this method showed that there were twists. In order to control for possible artifacts due to fixation and other preparative procedures, the characteristic S-shaped quiescent state of Ciona spermatozoa was studied.Analyses of platinum replicas of those flagella in which this waveform is well preserved suggest that most, if not all, of the twists observed are due to the artifact of a curved shape settling onto a surface. Detailed analyses indicate that if twists do occur in quiescent sperm, they are probably less than 0.4 radian. Since axonemes are evidently easily twisted in rigor, and even after fixation, caution should be exercised in interpretation of axonemal twists.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970030305
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  • 5
    Electronic Resource
    Electronic Resource
    Physarum myosin light chain binds calcium (1980)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 1 (1980), S. 63-71 
    Details
    ISSN: 0886-1544
    Keywords: Physarum polycephalum ; myosin light chains ; polyacrylamide gel electrophoresis ; calcium ; cytoplasmic streaming ; actomyosin ATPase regulation ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Myosin from the slime mold Physarum polycephalum contains three sizes of polypeptides: a heavy chain and two light chains, LC-1 and LC-2. Using a simple qualitative test for calcium binding by comparing electrophoretic migration of the polypeptides in sodium dodecy1 sulfate (SDS) acrylamide gels in the presence and absence of calcium, we have found that Physarum myosin light chain LC-2 migrates with an apparent molecular weight of 16,900 daltons in the presence of the metal ion chelator ethylene glycol bis (B-aminoethyl ether) N,N′-tetraacetic acid (EGTA). However, if calcium chloride is added to the sample prior to electrophoresis, the apparent molecular weight decreases to 16,100. Lanthanide and cadmium ions, but not magnesium, can substitute for calcium. Because the ionic radii of Ca2+, La3+, and Cd2+ are almost identical, we conclude that Physarum myosin LC-2 possesses a very size-specific binding site for calcium. Physarum myosin LC-1 and the heavy chain give no evidence for binding calcium by this test. Since cytoplasmic streaming in the plasmodium of Physarum requires calcium, our evidence indicates that the calcium-binding property of Physarum myosin LC-2 may be important in regulating the production of force by actomyosin in the ectoplasm. Unexpectedly, the myosin light chain in Physarum capable of binding calcium, LC-2, is the essential light chain, while LC-1 is a member of the regulatory class of myosin light chains [V. T. Nachmias, personal communication]. Until now, essential myosin light chains have not been shown to have high affinity divalent cation binding sites. This means a new version of the myosin-based model for actomyosin regulation by calcium may be required to explain cytoplasmic movement in Physarum, and perhaps in other motile systems involving cytoplasmic myosins as well.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970010106
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  • 6
    Electronic Resource
    Electronic Resource
    The intermediate circulation in the nonsinusal spleen of the cat, studied by scanning electron microscopy of microcorrosion casts (1983)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 178 (1983), S. 125-138 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Scanning electron microscopy of microcorrosion casts was used to visualize circulatory pathways of the intermediate circulation in nonsinusal spleen of cat. The marginal sinus (MS) around lymphatic nodules is a distinct vascular space which fills preferentially before the filling of the marginal zone (MZ) and surrounding red pulp occurs. The MS, which has a plentiful vascular supply, does not usually enclose the nodule completely. From the MS, flow occurs radially outwards into the MZ. Corrosion casts and histological sections both showed that a diversity of forms of the MZ exists: The thickness of MZ and the arrangement of its reticulum vary among nodules and between different areas of the same nodule, from a complete absence to a region of up to 50 μn width.No direct arteriovenous connections were found (in contrast to dog spleen: Schmidt et al., '83b). Aside from capillary endings in the MS and MZ, all arterial capillaries terminate in the reticular spaces of the red pulp, i.e., the circulation appears to be entirely “open.” From each capillary termination a great variety of flow pathways through the reticular meshwork to the pulp venules is available; some of these routes are quite long but others may involve distances as short as 15-25 μm. Evidence of flow into ellipsoid sheaths was abundant in casts from dilated spleens, but scarce in contracted spleens. In contrast to the extensive system of interconnected venous sinuses in dog spleen, the pulp venules found in cat spleen are nonanastomosing, shorter, and much smaller in caliber, and all receive flow freely from the reticular mesh-work via open ends and fenestrations in their walls.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051780205
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  • 7
    Electronic Resource
    Electronic Resource
    Circulatory pathways in the sinusal spleen of the dog, studied by scanning electron microscopy of microcorrosion casts (1983)
    New York, NY : Wiley-Blackwell
    Journal of Morphology 178 (1983), S. 111-123 
    Details
    ISSN: 0362-2525
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Scanning electron microscopy of microcorrosion casts was used to visualize circulatory pathways in the sinusal spleen of dog. The examination of contracted versus dilated organs and variations of the volume of material injected gave an indication of flow dynamics. Minimal injections of material into contracted spleens produced filling of mainly the fastest routes for flow, whereas injections into dilated spleens primarily filled slower routes. This procedure yielded a more complete, three-dimensional picture of the arterial, intermediate, and venous pathways as a whole, and of the relative amounts of flow through different arterial routes. Evidence of flow from capillary lumina out into ellipsoid sheaths was plentiful in casts from dilated spleens, but rare in casts from contracted organs. The pattern of flow within and out of the marginal sinus has been elucidated: A circumferential filling occurs first, followed by a flow that radiates outward into the marginal zone and red pulp. Venous sinuses filled via two routes in addition to the generally accepted path from the reticular meshwork via fenestrations in sinus walls. First, many venous sinuses extending out from the marginal sinus and surrounding marginal zone originated as open-ended tubes continuous with the reticular spaces of the marginal sinus or marginal zone. Second, direct connections of arterial capillaries with venous sinuses in the red pulp were found. Evidence indicating that some mechanism is controlling the flow via these routes is discussed. The strikingly different arrangement of venous sinuses in the subcapsular region is demonstrated.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jmor.1051780204
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  • 8
    Electronic Resource
    Electronic Resource
    Variable coupling of active NA+ + K+ transport in Ehrlich ascites tumor cells: Regulation by external NA+ and K+ (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 106 (1981), S. 407-418 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of altered external sodium and potassium concentrations on steady state, active Na+ + K+ transport in Ehrlich ascites tumor cells have been investigated. Membrane permeability to Na+ and K+, intracellular [Na+] and [K+], and membrane potential were measured. Active cation fluxes were calculated as equal and membrane potential were measured. Active cation fluxes were calculated as equal and opposite to the net, diffusional leak fluxes. Elevation of external K+ (6-60 Mm)by equivalent replacement of Na+ (154-91 mM) inhibits both active Na+ and K+ fluxes, but not proportionally. This results in a decrease of the coupling ratio (rp = -Jkp/JpNa) as external K+ is increased. Elevation of external K+ (3-68 mM) at constant Na+ (92mM) inbibits Jpk, but is without effect on JpNa. The coupling ratio declines from 1.01 ± 0.14 to 0.07 ± 0.05, a 14-fold alteration. Reduction of external Na+ (154-25 mM) at constant K+ (6mM) depresses JpNa, but is without effect on Jpk. The coupling ratio increases from 0.63 ± 0.04 at 154 mM Na+ to 4.5 ± 2.04 at 25 mM Na+. The results of this investigation are consistent with the independent regulation of active cation fluxes by the transported species. Kinetic analysis of the data indicates that elevation of external sodium stimulates active sodium efflux by interacting at “modifier sites” at the outer cell surface. Similarly, external potassium inhibits active potassium influx by interaction at separate modifier sites.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041060310
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  • 9
    Electronic Resource
    Electronic Resource
    Change in water proton relaxation time during erythrocyte maturation (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 116 (1983), S. 409-414 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Erythrocyte populations from newborn and mature mice were characterized according to: size; ultrastructural features; water content; concentration of intraerythrocyte elements including Na, Cl, K, P, S, Mg, and Fe; and the spin-lattice (T1) and spin-spin relaxation times of water protons as measured by nuclear magnetic resonance (NMR) spectroscopy. A significant increase in the T2 time from 142 ± 3 msec to 184 ± 3 msec occurred during erythrocyte maturation. This change in T2 time was correlated with a change from a polyribosome-rich hemoglobin-poor cell type to a polyribosome-absent hemoglobin-rich cell type. The change in T2 time could also be correlated to a significantly higher K and P concentration in the mature erythrocytes. The change in T2 time was not correlated to a change in cellular water content or to the concentration of any of the other elements measured by electron probe X-ray microanalysis. If the NMR relaxation times of water molecules truly reflect their average motional freedom, then the findings suggest that greater water ordering interaction occurs in the ribosome containing immature erythrocyte.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041160320
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  • 10
    Electronic Resource
    Electronic Resource
    The membrane potential of Ehrlich ascites tumor cells: An evaluation of the null point method (1981)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 106 (1981), S. 399-406 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The effects of valinomycin (25 pM) on the membrane potential and on initial, passive Na+ and K+ movements have been determined in Ehrlich ascites tumor cells. The membrane potential of steady-state cells in a physiologic environment was - 23.2 mV. Addition of valinomycin induced a small, significant hyperpolarization (Vm = -29.6 mV) when averaged over the population tested. However, analyses of the response of individual cells to valinomycin showed two different potential effects: (1) the majority of cells hyperpolarized after treatment; but (2) a significant fraction depolarized when exposed to valinomycin. The Vm of steady-state cells incubated in saline with K+ at concentrations of 21 mM or 75 mM was - 21.4 mV and -22.0 mV, respectively. Addition of valinomycin to these cells was without effect on Vm, thus establishing the “null point” responses. Only for cells incubated in saline with a K+ of 75 mM was there agreement between Vm and K+ equilibrium potential (Vk). Determinations of cellular Na+ and K+ showed that valinomycin induced net losses of K+ and gains of Na+ by cells incubated in either physiologic saline or saline with a K+ concentration of 21 mM. However, the celular K+ of cells incubated in saline with a K+ concentration of 75 mM was unaltered by valinomycin. There was a two- to threefold increase in K+ permeability of the cell membrane in the presence of valinomycin. These results are consistent with the existence of two null points in the membrane-potential response to valinomycin: One is established when the membrane potential corresponds to Vk; the second occurs when the effects of valinomycin on K+ loss from the cell are exactly offset by its inhibition of active Na+ + K+ transport.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041060309
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