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  • 1
    Electronic Resource
    Electronic Resource
    Genetic evidence that the steroid-regulated trafficking of cell surface glycoproteins in rat hepatoma cells is mediated by glucocorticoid-inducible cellular components (1987)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 35 (1987), S. 271-284 
    Details
    ISSN: 0730-2312
    Keywords: glycoprotein trafficking variant ; mouse mammary tumor virus ; heterokaryons ; glucocorticoid receptor deficient variant ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The biological control of posttranslational maturation and compartmentalization reactions that operate upon proteins during transport to their final cellular desti- nations is crucial for normal cellular function. Using the expression of mouse mammary tumor virus (MMTV) glycoproteins as sensitive probes in the viral- infected rat hepatoma cell line M1.54, we have discovered and documented a novel glucocorticoid-regulated trafficking pathway that controls the cell surface localization of MMTV glycoproteins. One complement-selected derivative of M1.54 cells, CR4, failed to compartmentalize cell surface MMTV glycoproteins in the presence of dexamethasone. To test genetically if this glycoprotein trafficking pathway is mediated by cellular or viral gene products, CR4 cells were fused with uninfected Fu5 rat hepatoma cells. Indirect immunofluorescence of CR4 × Fu5 heterokaryons revealed that Fu5 complemented the defect in CR4 only after exposure to 1 μM dexamethasone. The glucocorticoid inhibition of Fu5 proliferation was exploited to recover the receptor-deficient uninfected derivative EDR3 that expressed a 100-fold lower level of [3H]dexamethasone binding activity. Analysis of CR4 × EDR3 cell fusions by indirect immunofluorescence revealed that EDR3 cells complemented CR4 in a dexamethasone-dependent manner, suggesting that EDR3 supplied a functional trafficking component while CR4 provided a functional glucocorticoid receptor to the heterokaryons. Taken together, our results demonstrate that cellular-encoded glucocorticoid-inducible components mediate the regulated trafficking of cell surface MMTV glycoproteins.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240350402
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  • 2
    Electronic Resource
    Electronic Resource
    Parallel changes in amino acid transport and protein kinase C localization in LLC-PK1 cells treated with TPA or diradylglycerols (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 132 (1987), S. 104-110 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Protein kinase C is considered to be a major target for tumor promoting phorbol esters such as 12-O-tetradecanoylphorbol-13-acetate (TPA). We have analyzed the correlation between A-system amino acid transport and the distribution of protein kinase C (PKC) between a membrane-rich fraction (100,000 g pellet) and cytosol (supernatant) from homogenized LLC-PK1 cells, a pig kidney epithelial cell line grown in culture. During log growth 1 day after seeding the cells onto culture plates, PKC activity is high in the membrane fraction and low in the cytosol. As the cells become confluent the PKC distribution shifts to a cytosolic pool. Concomitantly, A-system amino acid transport, as measured by methylaminoisobutyric acid [14C]MeAIB uptake, decreases. TPA (0.01-1.0 μM) induces a shift of PKC activity from the cytosol back to the membrane-rich fraction in post-confluent cells with a concomitant 2-3 fold stimulation of MeAIB uptake. The same responses can be achieved by treating cells with certain diradylglycerols, either diacylglycerols such as 1-oleyl-2-acetyl-sn-glycerol (OAG) or alkylacylglycerols such as 1-hexadecenyl-2-oleyl-sn-glycerol. Both responses to TPA are blocked by cytochalasin B, but cycloheximide inhibits the transport response without affecting PKC redistribution. It is suggested that the redistribution may be a necessary but not sufficient concomitant to the transport activation.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041320114
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  • 3
    Electronic Resource
    Electronic Resource
    Cell cycle changes in water properties in sea urchin eggs (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 133 (1987), S. 14-24 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: This study concerned changes in the motional properties of cellular water during the first cell cycle of fertilized sea urchin eggs (Lytechinus variegatus). There was a significant decrease in proton NMR T1 relaxation time and in cytoplasmic ice crystal growth during mitosis and a significant increase in T1 time and cytoplasmic ice crystal size during cleavage. This was not caused by egg water content changes as reflected by egg volume measurements. Removal of both the fertilization membrane and the hyaline layer shortly after fertilization did not alter the pattern of T1 time changes at mitosis and cleavage as compared to whole eggs; thus, the pattern of T1 time changes was attributed to intracellular events. Treatment of fertilized eggs with cytochalasin B, an inhibitor of actin polymerization, did not block the fall in T1 time at mitosis, but did block cytokinesis and the increase in T1 time, which normally occurred at cleavage. A significant pattern of actin disassembly and reassembly at mitosis and cytokinesis was found by studies on the total amount of monomeric actin (G actin) using the DNase I assay. This led to the hypothesis that the observed changes in T1 time and ice crystal size during the first cell cycle were due to the depolymerization and polymerization of cytoplasmic actin. To test this, the effect of the in vitro polymerization of purified actin on the T1 time and on ice crystal growth was examined. It was concluded that changes in the T1 time and ice crystal growth upon polymerization of actin in vitro resembled the changes seen in vivo. These results suggest that changes in the motional properties of cytoplasmic water during the first cell cycle are due, at least in part, to the state of polymerization of cytoplasmic actin.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041330103
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  • 4
    Electronic Resource
    Electronic Resource
    Analysis of DNA double strand breakage and repair using orthogonal field alternation gel electrophoresis (1987)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 3 (1987), S. 71-76 
    Details
    ISSN: 0749-503X
    Keywords: OFAGE ; X-ray damage ; DNA repair ; Saccharomyces cerevisiae ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Orthogonal field alternation gel electrophoresis (OFAGE) allows separation of DNA molecules in the size range of 200 kb to 3000 kb. These sizes encompass the chromosome sizes of the genome of Saccharomyces cerevisiae. Using this technique, we have found that yeast cells exposed to X-rays generate a smear of DNA fragments corresponding to the products of random, independent double strand breaks, and that the bands corresponding to unbroken chromosomes decrease in intensity in direct proportion to chromosome size. If exposed wild type cells are permitted time to repair (5 h at 30°C on YEPD), the fragments partially disappear and the chromosome bands reappear, although at less than normal intensity. In certain radiation-sensitive mutants (rad51, rad52 and rad54), the fragment smear appears following X-ray exposure but no repair of broken chromosomes occurs. In fact, loss of the fragments occurs; this could appear as partial repair using other procedures.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/yea.320030203
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  • 5
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    Sequence-specific packaging of DNA in human sperm chromatin (1987)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1987-05-22
    Description: The DNA in human sperm chromatin is packaged into nucleoprotamine (approximately 85%) and nucleohistone (approximately 15%). Whether these two chromatin fractions are sequence-specific subsets of the spermatozoon genome is the question addressed in this report. Sequence-specific packaging would suggest distinct structural and functional roles for the nucleohistone and nucleoprotamine in late spermatogenesis or early development or both. After removal of histones with 0.65M NaCl, exposed DNA was cleaved with Bam HI restriction endonuclease and separated by centrifugation from insoluble nucleoprotamine. The DNA sequence distribution of nucleohistone DNA in the supernatant and nucleoprotamine DNA in the pellet was compared by cloning size-selected single-copy sequences and by using the derived clones as probes of nucleohistone DNA and nucleoprotamine DNA. Two clones derived from nucleohistone DNA preferentially hybridized to nucleohistone DNA, and two clones derived from nucleoprotamine DNA preferentially hybridized to nucleoprotamine DNA, which demonstrated the existence of sequence-specific nucleohistone and nucleoprotamine components within the human spermatozoon.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gatewood, J M -- Cook, G R -- Balhorn, R -- Bradbury, E M -- Schmid, C W -- GM-07377/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1987 May 22;236(4804):962-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3576213" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/*physiology ; Cloning, Molecular ; DNA/*genetics/isolation & purification/metabolism ; Histones/isolation & purification ; Humans ; Male ; Nucleic Acid Hybridization ; Nucleoproteins/isolation & purification ; Spermatozoa/*physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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