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  • 1
    Electronic Resource
    Electronic Resource
    Identification of lung major GTP-binding protein as Gi2 and its distribution in various rat tissues determined by immunoassay (1989)
    s.l. : American Chemical Society
    Biochemistry 28 (1989), S. 4749-4754 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00437a035
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  • 2
    Electronic Resource
    Electronic Resource
    Role of cell-surface lysines in plasminogen binding to cells: identification of .alpha.-enolase as a candidate plasminogen receptor (1991)
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 1682-1691 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00220a034
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  • 3
    Electronic Resource
    Electronic Resource
    Mutations in SIP1 , encoding Smad interacting protein-1, cause a form of Hirschsprung disease (2001)
    [s.l.] : Nature Publishing Group
    Nature genetics 27 (2001), S. 369-370 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] Hirschsprung disease (HSCR) is sometimes associated with a set of characteristics including mental retardation, microcephaly, and distinct facial features, but the gene mutated in this condition has not yet been identified. Here we report that mutations in SIP1, encoding Smad interacting protein-1, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/86860
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  • 4
    Electronic Resource
    Electronic Resource
    Ontogeny of GTP-binding proteins, Gi and Go, in rat retina (1996)
    Springer
    Histochemistry and cell biology 106 (1996), S. 235-240 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The distribution and the levels of Gi1 (plus Gi3), Gi2, and Go in rat retina were studied immunohistochemically and immunochemically during development. At embryonic day (E) 15, Gi1α/Gi3α was observed in the inner layer of the neural retina, the future nerve fiber layer (NFL), while Gi2α was observed both in the inner and outer layers of the neural retina. No immunoreactivity for Goα was observed. At E18, Gi1α/Gi3α and Gi2α appeared in the inner plexiform layer (IPL), while Goα was faintly immunoreactive only in the NFL. At birth, Gi2α/Gi3α and Goα appeared in the ganglion cell layer. Gi2α was intensely immunoreactive in the NFL and IPL. At postnatal day (P) 10, the inner portions of the retina, from the NFL to the outer plexiform layer, were immunoreactive to Gi1α/Gi3α, Gi2α, and Goα. Gi1α/Gi3α and Goα were distributed characteristically in a laminated pattern in the IPL, but Gi2α was present homogeneously in the IPL. At P12, Gi2α appeared in the outer nuclear layer. As the postnatal days advanced, the laminated pattern of immunoreactivity to Goα in the IPL became diffuse, but immunoreactivity to Gi1α/Gi3α remained. The results of enzyme immunoassays showed that the concentration of Goα increased rapidly from P10 to P15 and reached almost the adult level at P20–P30, while Gi2α decreased until P15 and was almost constant thereafter. These results showed that the distribution of Gi1α/Gi3α, Gi2α, and Goα differs during development, suggesting that each G protein in the developing retina has a unique function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050037
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  • 5
    Electronic Resource
    Electronic Resource
    Ontogeny of alpha-crystallin subunits in the lens of human and rat embryos (1994)
    Springer
    Cell & tissue research 276 (1994), S. 151-154 
    Details
    ISSN: 1432-0878
    Keywords: Key words: Eye – Lens – Development, ontogenetic –αA-crystallin –αB-crystallin – Immunohistochemistry – Human – Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract. The distribution of αA- and αB-crystallin in the developing lens of human (Carnegie stages 13 to 23) and rat embryos (embryonic days E11 to 18) was examined immunohistochemically. In a human embryo at stage 13, the lens placode was already immunoreactive to αB-crystallin, but not to αA-crystallin. At stage 15, the lens vesicle was intensely immunoreactive both to αA- and αB-crystallin. From stages 16 to 23, the lens epithelial cells and fiber cells were immunoreactive to αA- and αB-crystallin. In rat embryos, αA-crystallin appeared in the lens pit at E12, and αB-crystallin appeared in the elongating lens fiber cells at E14. From E15 to E18, the lens epithelial cells and fiber cells were immunoreactive to αA-crystallin. The lens fiber cells were also immunoreactive to αB-crystallin, but the epithelial cells were not. These findings suggest that αB-crystallin appears earlier than αA-crystallin in the human lens, but at a later period than αA-crystallin in the rat lens. αB-Crystallin was not detected in the epithelial cells of the rat lens, but was persistently present in the epithelial cells of the human lens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00354794
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  • 6
    Electronic Resource
    Electronic Resource
    Ontogeny of alpha-crystallin subunits in the lens of human and rat embryos (1994)
    Springer
    Cell & tissue research 276 (1994), S. 151-154 
    Details
    ISSN: 1432-0878
    Keywords: Eye ; Lens ; Development, ontogenetic ; αA-crystallin ; αB-crystallin ; Immunohistochemistry ; Human ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The distribution of αA- and αB-crystallin in the developing lens of human (Carnegie stages 13 to 23) and rat embryos (embryonic days E11 to 18) was examined immunohistochemically. In a human embryo at stage 13, the lens placode was already immunoreactive to αB-crystallin, but not to αA-crystallin. At stage 15, the lens vesicle was intensely immunoreactive both to αA- and αB-crystallin. From stages 16 to 23, the lens epithelial cells and fiber cells were immunoreactive to αA- and αB-crystallin. In rat embryos, αA-crystallin appeared in the lens pit at E12, and αB-crystallin appeared in the elongating lens fiber cells at E14. From E15 to E18, the lens epithelial cells and fiber cells were immunoreactive to αA-crystallin. The lens fiber cells were also immunoreactive to αB-crystallin, but the epithelial cells were not. These findings suggest that αB-crystallin appears earlier than αA-crystallin in the human lens, but at a later period than αA-crystallin in the rat lens. αB-Crystallin was not detected in the epithelial cells of the rat lens, but was perisistently present in the epithelial cells of the human lens.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00354794
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  • 7
    Electronic Resource
    Electronic Resource
    Protein kinase C activation inhibits stress-induced synthesis of heat shock protein 27 in osteoblast-like cells: Function of arachidonic acid (1996)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 62 (1996), S. 69-75 
    Details
    ISSN: 0730-2312
    Keywords: heat shock protein 27 ; arachidonic acid ; protein kinase C ; osteoblast ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Exposure of osteoblast-like MC3T3-E1 cells to sodium arsenite (arsenite) increased the level of heat shock protein 27 (hsp27). The effect of arsenite was dose-dependent in the range of 50 to 200 μM. Arsenite also stimulated arachidonic acid release dose-dependently in the range between 50 and 200 μM in these cells. Both indomethacin, an inhibitor of cyclooxygenase, and nordihydroguaiaretic acid, a lipoxygenase inhibitor, significantly enhanced the arsenite-induced accumulation of hsp27. Melittin, an activator of phospholipase A2, significantly enhanced the arsenite-induced accumulation of hsp27. 12-O-Tetradecanoylphorbol-13-acetate (TPA), a protein kinase C (PKC)-activating phorbol ester, inhibited the arsenite-induced accumulation of hsp27. In contrast, 4α-phorbol 12, 13-didecanoate (4α-PDD), a PKC-nonactivating phorbol ester, had little effect. TPA suppressed the arsenite-induced arachidonic acid release, but 4α-PDD had little effect. Arsenite no longer affected cAMP accumulation, inositol phosphates formation nor the formation of choline and phosphocholine in these cells. These results suggest that the response to stress of hsp27 is coupled with the metabolic activity of the arachidonic acid cascade, and the activation of PKC inhibits the induction of hsp27 through the suppression of arachidonic acid release in osteoblast-like cells. © 1996 Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Receptor-associated changes of the catecholamine-sensitive adenylate cyclase in glioma cells doubly transformed with Moloney sarcoma virus (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 110 (1982), S. 107-113 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: A doubly transformed rat glioma cell line, designated C6V-1, was obtained from rat glioma C6 cells by infection with a rat-adapted variant of Moloney sarcoma virus (MSV-M-os). The C6V-1 cells show karyotypic changes in chromosome number (43) and structure, while C6 cells possess a normal male karyotype. C6V-1 and C6 cells were employed for characterization of a receptor-adenylate cyclase system of the surface membrane. C6V-1 cells showed lower adenylate cyclase activity than that of C6 cells, though the apparent Km for ATP in both types of cells was the same. The maximal stimulation of adenylate cyclase by isoproterenol was significantly reduced, and Kact for isoproterenol was approximately 18-fold lower in C6V-1 cells. When the concentration of β-adrenergic receptors was measured by various concentration of [3H] dihydroalprenolol (DHA), the maximal binding sites of C6 and C6V-1 cells were 760 and 230 fmol/mg protein, respectively, without any changes in the association constant for DHA. The concentration of isoproterenol required for 50% displacement of the [3H] DHA binding (Kd) was the same (around 1.5 × 10-6M) in both cells, measured in the presence of GTP. Thus the 19-fold drop in the Kd/Kact ratio in C6V-1 cells suggests an incomplete coupling of β-receptors to adenylate cyclase. Cyclic AMP phosphodiesterase activity and cAMP content in C6V-1 were lower than in C6 cells. Mitochondrial monoamine oxidase and cytosomal enolase activities, however, were somewhat higher in C6V-1 cells. The results indicate that a set of changes in the receptors and in the cyclic AMP system of C6V-1 cells. The results indicate taht a set of changes in the receptors and in teh cyclic AMP system of C6V-1 is one of the specific alteations by transformation, even though those may not be the cause of cell transformation.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041100202
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  • 9
    Electronic Resource
    Electronic Resource
    Forskolin induction of S-100 protein in glioma and hybrid cells (1985)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 122 (1985), S. 39-44 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: The S-100 protein level in mouse neuroblastoma (N18TG-2 and NIE-115), rat glioma (C6, C6BU-1, and C6V-1), and hybrid (NG108-15, 140-3, 141-B, NBr10A, NBr20A, NCB20, and NX3IT) cells was determined with a sensitive enzyme immunoassay system that uses a rabbit antibody to bovine brain S-100 protein. S-100 protein was detected in glioma but not in neuroblastoma cells. All seven hybrid cells derived from neuroblastoma and glioma or other types of cells were found to possess a very little or undetectable S-100 protein. The induction of S-100 protein level in prestationary phase cultures of glioma C6BU-1 cells was examined by forskolin, which was a highly specific activator of adenylate cyclase of the cells and produced morphological differentiation. After incubation with 10 μM forskolin for 48 hr, the S-100 protein level increased 2-2.5-fold in C6BU-1 glioma cells whose mean control level was 60 ± 26 ng/mg protein (± SD). The forskolin induction of S-100 protein in the cells was dose dependent, and the concentration of forskolin required for 50% activation of S-100 protein was about 0.6 μM. The increase by forskolin was initiated from 10-15 hr after incubation with it and was inhibited with cycloheximide and actinomycin D. In NG108-15 hybrid cells the induction of S-100 protein was also observed by forskolin as well as prostaglandin (PG) E1 plus theophylline which are known to activate adenylate cyclase of the cells. The results indicate that S-100 protein biosynthesis is genetically controlled in these clonal cells, and that S-100 protein can be regulated in a cAMP-dependent fashion in prestationary cultures.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041220107
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  • 10
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    Ontogeny of alpha-crystallin subunits in the lens of human and rat embryos (1994)
    Springer
    Details
    Publication Date: 1994-04-01
    Print ISSN: 0302-766X
    Electronic ISSN: 1432-0878
    Topics: Biology , Medicine
    Published by Springer
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