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  • 1
    Electronic Resource
    Electronic Resource
    A calmodulin-binding peptide relaxes skinned muscle from guinea-pig taenia coli (1989)
    Springer
    Pflügers Archiv 414 (1989), S. 282-285 
    Details
    ISSN: 1432-2013
    Keywords: Calmodulin ; Myosin light chain kinase ; Calmodulin antagonist ; Smooth muscle skinned fibres
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract During smooth muscle activation the calcium calmodulin complex interacts with myosin light chain kinase (MLCK) whereby activating it. A synthetic peptide analogue (RS20) corresponding to the calmodulin recognition sequence of MLCK has been synthesized and previously found to inhibit the calmodulin stimulated light chain kinase activity. Here we studied the effect of this peptide on skinned fibers from guinea pig taenia coli. Maximal contractions induced by 30 μM Ca2+ at 0.1 μM calmodulin could be completely relaxed by the peptide at 1 μM. The inhibitory effect was accompanied by partial dephosphorylation only of the regulatory myosin light chain. Relaxation could be reversed by addition of calmodulin which also increased the extent of light chain phosphorylation.The calmodulin concentration required for reversing the inhibition depended on the concentration of the inhibitory peptide suggesting that the peptide competed with MLCK for the calmodulin binding site. As the calcium-calmodulin-peptide mixture constitutes a calmodulin buffer, our results suggest, that the peptide is a calmodulin antagonist unique in terms of its potency and that less than nanomolar concentrations of free calmodulin may be required for inducing smooth muscle contractions.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00584627
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Human stratum corneum polar lipids and desquamation (1985)
    Springer
    Archives of dermatological research 277 (1985), S. 284-287 
    Details
    ISSN: 1432-069X
    Keywords: Desquamation ; Epidermal lipids ; Ceramides ; Cholesteryl sulfate
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ceramides and steryl-sulfate components from desquamated and cohesive human stratum corneum were examined using a combination of chemical and chromatographic means. Six structurally distinct series of ceramides were identified, and the relative amounts of these species, as measured by quantitative thin-layer chromatography, did not differ in cohesive and desquamated stratum corneum. In contrast, the level of cholesteryl sulfate was significantly reduced in the desquamated material. The results are in accord with the hypothesis that cholesteryl sulfate serves in cell-to-cell cohesion within the stratum corneum, and its hydrolysis may be necessary to permit shedding of cells from the surface.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00509081
    Library Location Call Number Volume/Issue/Year Availability
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    Paper (German National Licenses)
    Fulltext
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