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  • Immunohistochemistry  (2)
  • Binding specifity  (1)
  • Chemistry  (1)
  • GTP binding protein  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/General Subjects 1117 (1992), S. 97-103 
    ISSN: 0304-4165
    Keywords: Binding specifity ; ELISA ; Ganglioside ; Glycolipid ; Monoclonal antibody
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 55 (1994), S. 38-45 
    ISSN: 1432-0827
    Keywords: Vacuolar-type H+-ATPase ; Carbonic anhydrase II ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract The localization of vacuolar-type H+-ATPase and carbonic anhydrase II (CA II) in rat incisor enamel organs at maturation was examined by light and electron microscopy. The immunoreactivity for both vacuolar-type H+-ATPase and CA II was intense on the ruffled border of ruffle-ended ameloblasts (RA), but moderate at the distal end of smooth-ended ameloblasts (SA). Immuno-gold particles indicated that CA II was not confined to the ruffled border of RA alone, but also distributed in the cytoplasm of RA and SA. These findings suggest that RA may secrete protons produced by CA II via the ruffled border into enamel by active transport of vacuolar-type H+-ATPase. Secreted protons may activate hydrolytic enzymes to degrade the organic components of enamel matrix. Vacuolar-type H+-ATPase on vesicles of SA suggests that a specific configuration of ruffled borders in RA may be formed by the fusion of vesicle membranes in the distal end of cytoplasm of SA.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0878
    Keywords: Key words Glucocorticoid receptor (GR) ; Immunohistochemistry ; In situ hybridization ; Pituitary ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract By means of double immunohistochemical techniques and a nonradioisotopic in situ hybridization method, we determined the colocalization pattern of glucocorticoid receptor (GR) and pituitary hormones and the GR messenger RNA (mRNA) expression in the pituitaries of Wistar adult male rats. Immunoreactivity for GR was detected in the nuclei of cells in the anterior and posterior pituitary. Double immunohistochemistry revealed that the colocaliza- tion of GR and anterior pituitary hormones occurred in almost 99% of the growth hormone (GH)-producing cells and adrenocorticotropic hormone (ACTH)-producing cells, and in 67% of the thyroid stimulating hormone (TSH)-producing cells. Almost all of the folliculostellate cells (93%), marginal layer cells (94%) in the anterior pituitary, and pituicytes (96%) in the posterior pituitary immunostained for S100 protein antibody were also immunostained with GR. GR mRNA was abundant in the cytoplasm of anterior and intermediate pituitary cells but scattered sparsely in that of the posterior pituitary. These results suggest that glucocorticoids directly influence certain pituitary cells in order to regulate cell function, including the synthesis and/or secretion of hormones.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1435-1463
    Keywords: Depression ; GTP binding protein ; human brain ; photoaffmity labeling ; signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The amounts of various G protein subunits in postmortem brain samples from the parietal and temporal cortices were the same in controls and depressive patients as demonstrated by immunoblotting. However, photoaffinity GTP labeling (AAGTP) of Gi/oα, but not Gsα, was significantly increased in depressives in both cortex regions. Furthermore, the ratio of Gs/Gi/o AAGTP incorporation revealed a significant reduction in depressives in these regions. The present findings suggest that an imbalance of second messengers via G protein function may be involved in the pathophysiology of depression.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ : Wiley-Blackwell
    Journal of Biomedical Materials Research 17 (1983), S. 261-274 
    ISSN: 0021-9304
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine , Technology
    Notes: Deposits on soft contact lenses of high water content were investigated morphologically and chemically and compared with those on conventional soft contact lenses of poly(2-hydroxyethyl methacrylate). The material of the lenses examined in this investigation was the crosslinked copolymer of methyl methacrylate and N-vinylpyrrolidone with a water content higher than 70%. Morphologically, the deposits on the lenses with high water content were found to have no characteristics distinguishable from those on conventional lenses. By the electron microscopic observation of the cross section of a lens that had become opaque, it was confirmed that the deposit was on the lens surface and that no deposit was within the lens. Some spots on the lenses were recognized as colonies of microorganisms, but the majority of the spots had no involvement by microorganisms. Surface analysis with Fourier transform infrared spectrometer (FT-IR) confirmed that the main component of the filmy deposit was protein. Protein was detected in most of the deposits. The amino acid compositions of the proteins were found to be close to that of lysozyme. From the elemental analysis of several spots, silicon, aluminum, iron, and some other elements were detected. The structural analysis of some spots by a laser Raman microprobe (MOLE) revealed the existence of lipids. In several cases, the deposits were found to have grown around a defect of the lens surface. A mechanism for the formation of deposits is suggested.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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