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  • 1
    ISSN: 1573-4943
    Keywords: CNS proteins ; CNS neoplasms ; two-dimensional gel electrophoresis ; tumor proteins ; glial fibrillary acidic protein ; vimentin ; neuron-specific enolase ; G-proteins ; glutamate oxaloacetic transaminase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Two-dimensional gel electrophoresis (2DE) is being increasingly employed for protein separation, and silver staining has greatly enhanced its sensitivity. However, the identity of most of the protein spots demonstrated by 2DE has yet to be established. Using immunoblotting and comigration techniques, this study describes the identification of 12 of the major spots seen on 2D gels of normal human cerebral cortex and of certain human brain tumors. These proteins include: actin, albumin, α-tubulin, β-tubulin, neuron-specific enolase (NSE), nonneuronal enolase, glutamate oxaloacetic transaminase, glial fibrillary acidic protein (GFAP), vimentin, a 66-kD intermediate filament protein, the 68-kD neurofilament protein, and the β subunit of the guanine nucleotide regulatory proteins(G-proteins). In addition, the application of this technique to the study of human brain tumors has been described. A large amount of GFAP is seen in astrocytomas; the meningioma gel is characterized by a prominent vimentin complex; and the presence of NSE in medulloblastomas is confirmed. The identification of the β subunit of the G-proteins introduces a valuable means of screening for this important messenger protein, which is only beginning to be studied. While being derived from normal and pathological CNS tissue, these data are widely applicable to the study of other biological materials.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cell & tissue research 298 (1999), S. 11-19 
    ISSN: 1432-0878
    Keywords: Key words Calcium-binding protein ; Calcium buffering ; Calbindin D28k ; Calretinin ; Oxytocin ; Vasopressin ; Supraoptic nucleus ; Rat (Sprague Dawley)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The aim of the present study was to examine quantitatively whether two calcium-binding proteins, calbindin D28k and calretinin, are localized in oxytocin and vasopressin neurons of the supraoptic nucleus of the male rat. We used a triple-labeling immunofluorescence method with a confocal laser scanning microscope. Of the oxytocin-labeled cells, 70% were stained for both calbindin D28k and calretinin, 15% were stained for only calbindin D28k, 13% were stained for only calretinin, and 2% were stained for neither protein. Of the vasopressin-labeled cells, 73% were stained for neither calbindin D28k nor calretinin, 21% were stained for only calbindin D28k, 4% were stained for only calretinin, and 2% were stained for both proteins. Calbindin D28k and calretinin have been shown previously to contribute to calcium homeostasis by buffering [Ca2+]i. Therefore, these findings suggest that most of the oxytocin neurons may have a higher Ca2+-buffering capacity than most of the vasopressin neurons.
    Type of Medium: Electronic Resource
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