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  • 1995-1999  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Hepatic stellate cells (vitamin A-storing cells) change their cytoskeleton structure by extracellular matrix components through a signal transduction system (1998)
    Springer
    Histochemistry and cell biology 110 (1998), S. 121-128 
    Details
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  When cultured on a polystyrene surface or aminoalkylsilane-coated cover glasses, rat and human hepatic stellate cells exhibit a flattened, fibroblast-like shape with well-developed stress fibers. However, culturing the cells on type I collagen gel results in the elongation of long, multipolar cellular processes, whereas cells cultured on Matrigel maintain their round shapes. Dual fluorescence staining of microtubules and fibrillar actin indicated that the processes extend together with collagen fibers and contained microtubules as the core, whereas the periphery contained fibrillar actin. Immunofluorescence staining of vinculin showed that the focal adhesions were distributed mainly in lamellipodia when cultured on aminoalkylsilane-coated cover glasses, whereas in the cells cultured on type I collagen gel they were localized to the tips of the processes and along their bottom surface contacting collagen fibers. Wortmannin, as well as staurosporin and herbimycin A, inhibited the elongation process and induced the retraction of elongated processes. The wortmannin treatment also resulted in an alteration in focal adhesion distribution from the processes to cell bodies. These results indicate that the cell surface integrin binding to interstitial collagen fibers induces the elongation of processes through signaling events and the subsequent cytoskeleton assembly in hepatic stellate cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004180050273
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Translocation of pICln in a pig kidney cell line, LLC-PK1, by low osmotic stress (1999)
    Springer
    Clinical and experimental nephrology 3 (1999), S. 163-168 
    Details
    ISSN: 1437-7799
    Keywords: Key words pICln ; Chloride channel ; LLC-PK1 ; ATP ; Azide ; Dihydrocytochalasin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Background. There has been no conclusive explanation regarding the function of pICln (a 26- to 27-kDa acidic protein) on an osmo-sensitive chloride channel responsible for an outwardly rectifying anion current. We observed the effects of the hypotonic treatment of LLC-PK1 cells on the intra-cellular dynamic state of pICln. Methods. LLC-PK1 cells were cultured, and pICln in cells was observed immunohistochemically. The cells were fractionated into nuclei, mitochondrial, microsomal, and soluble fractions biochemically, and pICln was detected by an immunoblotting method after sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. Results. pICln in cells was observed on nuclei and their surroundings, but not on cell membranes. pICln was present in soluble and insoluble forms. The molecular masses of the oligomeric forms in the soluble fractions were different from those previously reported with Madin-Darby canine kidney (MDCK) cells, indicating the differences in the pICln-oligomer depending on cell type. On analysis with SDS-polyacrylamide gel electrophoresis, the exposure of cells to hypotonic media elevated the ratio of soluble to insoluble forms within 5 min. This result also conflicted with those previously reported with MDCK cells. This finding suggests that the function of pICln and the signaling mechanism differ depending on the cell species. Both extracellular ATP and NaN3 inhibited this elevation of the soluble/insoluble ratio, coinciding with previous reports that extracellular nucleotides and depletion of intracellular ATP inhibited the volume-sensitive chloride channel. Dihydrocytochalasin B, an F-actin-disrupting drug, inhibited the elevation of the soluble/insoluble ratio. Conclusions. The soluble form of pICln was increased within 5 min by exposure of LLC-PK1 cells to hypotonic media. This translocation was inhibited by extracellular ATP, NaN3, and dihydrocytochalasin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s101570050029
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    Paper (German National Licenses)
    Fulltext
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