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  • Pituitary gland  (2)
  • Aromaticity  (1)
  • 1995-1999  (1)
  • 1980-1984  (2)
  • 1955-1959
  • 1
    ISSN: 1432-2307
    Keywords: Immunohistochemistry ; Pituitary gland ; Pituitary adenomas ; Cytokeratins ; Intermediate filaments
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Ten non-neoplastic pituitary glands and 22 pituitary adenomas producing different hormones were studied by immunofluorescence microscopy as well as peroxidase-antiperoxidase and biotin-avidin techniques on frozen sections and formalin-fixed, paraffin-embedded material using antibodies to cytokeratin, vimentin, GFAP, neurofilament protein and different pituitary hormones. The endocrine cells in non-neoplastic pituitary glands as well as in most pituitary adenomas were cytokeratin-positive. The cytoplasmic cytokeratin distribution patterns of non-neoplastic and tumor cells were similar and typical of the type of hormone produced: GH-producing normal cells showed a paranuclear condensation of cytokeratin-reactive intermediate filaments; this accumulation was even further accentuated in GH-producing adenomas resulting in fibrous bodies (Kovacs and Horvath 1978) decorated by cytokeratin antibodies. Prolactin-producing cells showed a less intense cytoplasmic cytokeratin-specific staining with focal paranuclear accentuation in non-neoplastic as well as in neoplastic glands. ACTH-producing cells in normal pituitary glands as well as in adenomas exhibited a strong and more uniform cytoplasmic cytokeratin staining. The cytokeratin reactivity in glycoprotein hormone-producing cells of non-neoplastic tissue and adenomas was weak. Vimentin and GFAP reactivity was confined to agranular folliculo-stellate cells. The specific and different distribution patterns of cytokeratins in pituitary cells can, therefore, provide an (indirect) indication to the production of a specific hormone if immunocytochemistry fails to demonstrate hormone production.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    ISSN: 1434-1948
    Keywords: Phosphorus heterocycles ; Aromaticity ; Phosphenium cations ; Ab initio calculations ; Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: The aromatic stabilization of cyclic phosphenium cations (general type C2N2P+) was studied by experimental methods (synthesis, multinuclear NMR, single crystal X-ray crystallography) and quantum chemical calculations (ab initio methods). The structures of the 1,3,2-diazaphosphole derivatives [(tBuN-CH=CH-NtBu)P+]Cl- (1), (tBuN-CH2-CH2-NtBu)P-Cl (2), [(tBuN-CH=CH-NtBu)P]+PF6- (3) and [(tBuN-CH2-CH2-NtBu)]P+PF6- (4) were examined by single crystal X-ray diffraction. The chloro phosphane [(tBuN-CH=CH-NtBu)P]+Cl- (1) has an ionic P-Cl bond and contains an aromatically stabilized phosphenium cation [shortest distance P···Cl = 275.9(2) pm], while the CC-saturated compound (tBuN-CH2-CH2-NtBu)P-Cl (2) is covalent. The two chloro-phosphanes 1 and 2 differ sharply in their volatility and solubility in organic solvents. Compound 2 is soluble in hydrocarbons and sublimes readily at 90 °C/0.1 Torr but 1 is insoluble in hexanes and not volatile below 180 °C/0.1 Torr. The degree of aromatic stabilization in the phosphenium cation 1 was investigated by ab initio methods. For the model cations [RN-CH2-CH2-NR]P+ and [(RN-CH=CH-NR)P]+, thermochemical stabilization energies of 25.8 kcal · mol-1 (R = H) and 28.1 kcal · mol-1 (R = Me) were obtained from isodesmic hydrogenation reactions at the RHF/MP2/6-31G*//RHF/6-31G* level.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0533
    Keywords: Immunohistochemistry ; Folliculo-stellate cells ; Pituitary gland ; Pituitary adenoma ; S-100 protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Presence and distribution of S-100 protein (S-100), neuron-specific enolase (NSE), cytokeratin polypeptides, glial fibrillary acidic protein (GFAP), vimentin, actin, lysozyme and pituitary hormones (prolactin, hGH, ACTH, β-FSH, β-LH, β-TSH, alpha subunit) in folliculo-stellate cells (FSC) were studied in seven normal human pituitary glands and 28 pituitary adenomas using peroxidase-antiperoxidase and the avidin-biotin immunohistochemical techniques. Approximately 5% of the cells of the adenohypophysis were agranular, non-hormon-producing FSC most of which showed a conspicuous and strong reaction with S-100 antibodies but some were, in addition, GFAP- and vimentin-positive. In contrast to endocrine cells (EC), FSC were not decorated by antibodies to NSE or cytokeratins. In addition to supportive functions, these cells, due to their close special relationship to EC, seem to have transport and other metabolic functions yet to be elucidated. By their S-100 reactivity and their distribution FSC are comparable to glial cells of the central and schwann and satellite cells of the peripheral nervous system (PNS) as well as to supportive cells in neuroendocrine organs and related tumors (e.g., pheochromocytomas, paragangliomas, carcinoids). With one exception, S-100 reactive FSC were not found in pituitary adenomas. The immunohistochemical demonstration of S-100 protein in pituitary tissue is, therefore, a reliable aid in the discrimination between adenomas and normal pituitary tissue, particularly in small and poorly preserved specimens. In one adenoma FSC were found in addition to ACTH-producing tumor cells. This seems to be an extremely rare event suggesting a combination tumor.
    Type of Medium: Electronic Resource
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