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  • 1
    Electronic Resource
    Electronic Resource
    Coordinated expression of five tropomyosin isoforms and β-actin in astrocytes treated with dibutyryl cAMP and cytochalasin D (1994)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 28 (1994), S. 303-316 
    Details
    ISSN: 0886-1544
    Keywords: cytoskeleton ; cell culture ; gene expression ; Northern blot ; serum-induction ; rat ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Cytochalasin D and dBcAMP cause cultured astrocytes to change from flat cells to retrated process-bearing cells. F-actin was present throughout cells stimulated with dBcAMP for 16 h, whereas cytochalasin D caused F-actin to form massive aggregates at the tips of the cell processes. The two drugs differently regulated the expression of both β-actin and tropomyosin genes in astrocytes cultured in the presence or absence of serum: dBcAMP caused down-regulation and cytochalasin D caused up-regulation. Northern blot analyses indicated that: (1) serum deprivation halved the concentration of all tropomyosin transcripts (TM-1, TM-2, TM-4, TMBr-1, TMBr-2). Serum induced TM-4 via transcriptional activation, independent of protein synthesis, (2) dBcAMP induced down-regulation of β-actin (-50%) and tropomyosin transcripts (-35 to 52%) even in the presence of serum. The concentration of profilin mRNA decreased in dBcAMP-reactive astrocytes (-46%). The decrease in β-actin mRNA concentration was not blocked by cycloheximide, whereas down-regulation of tropomyosin transcripts was completely reversed when protein synthesis was inhibited, and (3) cytochalasin D induced an increase in the concentration of tropomyosin transcripts (+ 69 to 185%) which was cumulative with serum stimulation. Cytochalasin D induction of both β-actin and TM-4 operated through transcriptional activation, independent of protein synthesis.The production of all tropomyosin transcripts examined here were strictly coordinated with β-actin expression in serum-, dBcAMP- and cytochalasin D-treated astrocytes. This indicates that the differential expression of tropomyosin isoforms occurring during astrocyte maturation is due to more complex regulation than that involved in serum- or cAMP-stimulated astrocytes. © 1994 Wiley-Liss, Inc.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970280404
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  • 2
    Electronic Resource
    Electronic Resource
    Distribution of gelsolin in the retina of the developing rabbit (1991)
    Springer
    Cell & tissue research 264 (1991), S. 335-338 
    Details
    ISSN: 1432-0878
    Keywords: Gelsolin ; Retina ; Müller cell ; Photoreceptors ; Development, ontogenetic ; Rabbit
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The distribution of gelsolin, a calcium-dependent actin-severing and capping protein, in the retina of the developing and adult rabbit was studied. Gelsolin immunoreactivity was found in the photoreceptors and ganglion cells, where it may have a role in neuronal morphogenesis. Only the inner segment of the photoreceptors retained a high gelsolin content in the adult retina, perhaps because the attached outer segment is continuously renewed throughout life. Gelsolin, which is a major component of the rabbit brain oligodendrocytes, was also found in the myelin of the medullary ray region of the rabbit retina. Müller cells in all regions of the rabbit retina also contain gelsolin from early in development to adulthood. Since one of the functions of these cells is to ensheath neuronal elements in the inner plexiform and optic fiber layers, we suggest that gelsolin may play the same role in Müller cells as it does in oligodendrocytes, i.e., sheath formation via its calcium-dependent action on the actin microfilament networks.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00313971
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  • 3
    Electronic Resource
    Electronic Resource
    Gelsolin immunoreactivity and development of the tectorial membrane in the cochlea of normal and hypothyroid rats (1988)
    Springer
    Cell & tissue research 254 (1988), S. 241-245 
    Details
    ISSN: 1432-0878
    Keywords: Gelsolin ; Cochlea ; Kölliker's organ ; Thyroid deficiency ; Development, ontogenetic ; Rat (Wistar)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Gelsolin was localized by immunocytochemistry in the developing cochlea of the rat. In normal animals, the protein appeared at 18 th day in utero in cells of the Kölliker's organ, which are involved in the secretion of the tectorial membrane. The Kölliker's organ cells were not immunoreactive after the first postnatal week, which is when they cease their secretory activity. Gelsolin immunoreactivity was similar in thyroid-deficient rats until the second postnatal week but, at this age, Kölliker's organ did not transform and its gelsolin immunoreactivity persisted, together with its secretory activity. As a result, the tectorial membrane was greatly distorted and out of contact with the hair cells, which dramatically impaired the mechanical properties of the organ of Corti. The developing cochlea thus provides an example of the involvement of gelsolin in a secretory process that is of importance in the development of hearing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00220040
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  • 4
    Electronic Resource
    Electronic Resource
    Solid-phase synthesis of peptide nucleic acid (PNA) monomers and their oligomerization using disulphide anchoring linkers (1998)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Peptide Science 4 (1998), S. 266-281 
    Details
    ISSN: 1075-2617
    Keywords: Peptide nucleic acid monomers ; PNA synthesis ; disulphide linkers ; solid-phase synthesis ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: A new simple solid-phase method has been developed for synthesizing Boc-protected peptide nucleic acid (PNA) monomers. An immobilized backbone 3 was built on Expansin® resin using an ester disulphide handle: 2-hydroxypropyl-dithio-2′-isobutyric acid (HPDI). The base acetic acids of thymine 5, Z-cytosine 9, Z-adenine 12, and 6-O-benzyl guanine 17 were prepared and coupled to the immoblized backbone. The HPDI handle was cleaved under mild conditions by cyanolysis or assisted hydrolysis with tris(2-carboxyethyl)phosphine (TCEP) to give undamaged PNA monomers. These monomers were coupled to form oligomers by solid-phase method with another disulphide linkage: aminoethyldithio-2-isobutyric acid (AEDI) grafted on an amino-functionalized TentaGel® resin, using in situ neutralization and TBTU as activating reagent. Final cleavage of the AEDI linker gave PNA bearing a cysteamide residue that could be useful for optimizing PNA properties. Oligomers of up to 16 residues long were assembled. © 1998 European Peptide Society and John Wiley & Sons, Ltd.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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