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  • 1
    Electronic Resource
    Electronic Resource
    Distribution of protein tracers in the nervous system of the crayfish (Astacus astacus L.) following systemic and local application (1972)
    Springer
    Journal of neurocytology 1 (1972), S. 35-47 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A study was made on the penetration and cellular uptake of two protein tracers, albumin labelled with Evans blue (EBA) and horseradish peroxidase (HP), in the nervous system of the crayfish following systemic and local administration. Followingsystemic injection, EBA did not diffuse freely from the cerebral vessels into the brain parenchyma. When the tracers werelocally applied on the surface of the ventral nerve cord their penetration into the nervous parenchyma was to some extent restricted by the nerve sheath. However, unlike the perineurium of vertebrate peripheral nerves, which acts as an efficient diffusion barrier, the crayfish nerve sheath allowed the diffusion of small amounts of tracers into the ganglia. The tracers could more readily penetrate into peripheral nerves in the vicinity of ganglia. Inside the ganglion the tracers spread in extracellular spaces, between glial cell membranes and reached the neuronal surfaces. The proteins were taken up by pinocytosis in glial cells, and also in axons.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01098644
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  • 2
    Electronic Resource
    Electronic Resource
    Different stability of posttranslationally modified brain microtubules isolated from cold-temperate fish (1994)
    Springer
    Molecular and cellular biochemistry 130 (1994), S. 137-147 
    Details
    ISSN: 1573-4919
    Keywords: microtubules ; calcium ; colchicine ; posttranslational modifications ; fish ; cow
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Abstract Microtubule proteins were isolated by a temperature-dependent assembly-disassembly method from brain tissue of for cold-temperate fish; one fresh water fish (Oncorhynchus mykiss), and three marine fish (Labrus berggylta, Zoarces viviparus andGadus morhua). The α-tubulins from all four fish species were acetylated. The α-tubulins from the marine fish were composed of a mixture of tyrosinated and detyrosinated tubulin, while the fresh water fish tubulin only reacted with an antibody against detyrosinated tubulin. The isolated microtubules had a similar MAP composition. A 400 kD protein and a MAP2-like protein were found, but MAP1 was missing. All microtubules disassembled upon cooling to 0°C. In spite of these common characteristics, the assembly of microtubules fromLabrus berggylta was inhibited by colchicine and calcium, in contrast to the assembly of microtubules fromOncorhynchus mykiss andZoarces viviparus. For the latter, colchicine was not completely inhibitory even at a concentration as high as 1 mM, and calcium induced the formation of both loosely and densely coiled ribbons. The effects of calcium and colchicine on microtubules fromOncorhynchus mykiss andZoarces viviparus were modulated by either fish or cow MAPs, indicating that the effects are due to intrinsic properties of the fish tubulins and not the MAPs. In view of these findings, our results suggest that there is not correlation between colchicine sensitivity, inability of calcium to inhibit microtubule assembly, and acetylation and detyrosination.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01457395
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  • 3
    Electronic Resource
    Electronic Resource
    Differences in the effect of Ca2+ on isolated microtubules from cod and cow brain (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 59-68 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; paracrystal ; coiled ribbons ; microtubule-associated proteins ; assembly ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Isolated microtubules from cod and cow brains were compared with respect to their response to calcium ions. The effect of Ca2+ on cod microtubules was found to be temperature dependent. In contrast to cow microtubules, cod microtubules assembled at 18°C. At this temperature the assembly was inhibited by Ca2+ concentrations of 2 mM and higher. This was also found for cow microtubules at 37°C. However, at 30°C there was no effect of 2 mM Ca2+ of the amount of assembly or disassembly of cod microtubules consisting of only tubulin or of tubulin and microtubule-associated proteins (MAPs). The morphology was affected though, since some coiled ribbons formed from tubulin and MAPs. The calcium-binding calmodulin did not alter the effect of calcium on cod microtubules markedly. At higher Ca2+ concentrations (〉4 mM), coiled ribbons were formed from cod tubulin and MAPs, but mainly amorphous aggregates and very few coiled ribbons were formed from cod tubulin alone, indicating that the Ca2+ effect is modulated by cod MAPs. The modulatory effect of cod MAPs was however not species specific, since both cod and cow MAPs had the same effect on cod microtubules, in spite of a different protein composition. A MAP-dependent effect of Ca2+ was also found for cow microtubule proteins. The assembly of pure cow tubulin, as well as that of cow tubulin and MAPs, was inhibited by 2 mM Ca2+. In the presence of 10 and 20 mM Ca2+, pure cow tubulin formed amorphous aggregates, rings, and even paracrystals, while the assembly of cow tubulin and MAPs was inhibited. Our results suggest therefore that the effect of Ca2+ can be moderated by MAPs, but depends on intrinsic properties of the different tubulins. © 1994 Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970280106
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