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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Anatomy and embryology 177 (1988), S. 307-310 
    ISSN: 1432-0568
    Keywords: Vitamin D ; Receptor ; Spinal cord ; Autoradiography ; Motor neuron ; Substantia gelatinosa ; Spinal ganglion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Autoradiographic studies revealed concentration of 3H 1,25(OH)2 vitamin D3 in nuclei of certain neurons in the spinal cord of adult and neonatal mice, fed a normal or a vitamin D deficient diet. Nuclear uptake and retention was strongest in motor neurons in lamina IX. Nuclear concentration also existed in neurons of lamina II, lamina VIII, lamina X and intermediate nucleus of the lateral column. The results indicate that these neurons are target neurons which contain nuclear receptors for 1,25(OH)2 vitamin D3. this suggests that 1,25(OH)2 vitamin D3 has direct genomic actions on the innervation of skeletal muscle by exerting related trophic, secretory, and electrophysiological effects. In addition, these data point to direct genomic actions of 1,25(OH)2 vitamin D3 on spinal sensory perception, and on certain autonomic functions. Nuclear binding in certain neurons in the peripheral ganglion of the trigeminal nerve further suggests that sensory perception is influenced by 1,25(OH)2 vitamin D3 not only at the level of the substantia gelatinosa, but also at the level of spinal ganglia.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-5001
    Keywords: 15N,13C,2H-labeled proteins ; 2H spin relaxation ; 15N, NH correlations
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract A triple-resonance pulse scheme is described which records15N, NH correlations of residues that immediately follow amethyl-containing amino acid. The experiment makes use of a15N, 13C and fractionally deuterated proteinsample and selects for CH2D methyl types. The experiment isthus useful in the early stages of the sequential assignment process as wellas for the confirmation of backbone 15N, NH chemical shiftassignments at later stages of data analysis. A simple modification of thesequence also allows the measurement of methyl side-chain dynamics. This isparticularly useful for studying side-chain dynamic properties in partiallyunfolded and unfolded proteins where the resolution of aliphatic carbon andproton chemical shifts is limited compared to that of amide nitrogens.
    Type of Medium: Electronic Resource
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