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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Correlation Between the Expression of Methionine Adenosyltransferase and the Stages of Human Colorectal Carcinoma (2000)
    Springer
    Surgery today 30 (2000), S. 706-710 
    Details
    ISSN: 1436-2813
    Keywords: Key words Methionine adenosyltransferase ; Colorectal adenocarcinoma ; Colon ; Immunohistochemistry
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Methionine adenosyltransferase (MAT) catalyzes the synthesis of S-adenosylmethionine (AdoMet) from ATP and L-methionine. AdoMet is the major methyl donor in most transmethylation reactions in vivo, and it is also the propylamino donor in the biosynthesis of polyamines. In the present study, we assessed MAT activity in human colons with colorectal carcinoma and the values were compared with those of morphologically normal adjacent mucosa. Higher levels of MAT activity were observed in the colorectal carcinoma than in the normal colon. The ratio of MAT activity in tumor tissue versus normal tissue seemed to be correlated well will the stage of the colorectal tumor. Furthermore, immunoblot analysis showed that the high levels of MAT activity observed in colorectal carcinoma were due to the increased amounts of MAT protein. Immunohistochemical analysis revealed that MAT was most abundant in goblet cells, particularly in granules in the supranuclear area of these cells. In the colorectal carcinoma tissues, MAT was strongly stained in the cancerous cells and localized in granules in the supranuclear region. The results of this preliminary study suggest that determination of the relative ratio of MAT activity in both normal and tumor regions in human colorectal carcinoma could be a clinically useful tool for determining the stage of malignancy of colorectal carcinomas.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s005950070081
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  • 3
    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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  • 4
    Electronic Resource
    Electronic Resource
    The differentiation of HL-60 cells in the synthetic medium induced by GM3 ganglioside (1985)
    Springer
    Bioscience reports 5 (1985), S. 517-524 
    Details
    ISSN: 1573-4935
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract GM3 ganglioside, added exogenously to a promyelocytic leukemia cell line (HL-60 cells) in serum-free synthetic medium, induced differentiation into macrophage-like cells. Macrophagic morphology and function of differentiation-induced cells were determined by cell growth behavior, May-GriJnwald-Giemsa staining, activities of nonspecific esterase, phagocytosis and nitroblue tetrazolium (NBT) reduction. GM3 ganglioside may play a role in triggering differentiation of HL-60 cells into macrophage-like cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01116951
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  • 5
    Electronic Resource
    Electronic Resource
    Stellate cells storing retinol in the liver of adult lamprey, Lampetra japonica (1987)
    Springer
    Cell & tissue research 249 (1987), S. 289-299 
    Details
    ISSN: 1432-0878
    Keywords: Stellate cells (fat-storing cells, lipocytes) ; Vitamin A (retinol) ; Liver ; Fluorescence microscopy ; Lamprey (Lampetra japonica)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Distribution, localization and fine structure of the stellate cells in the liver of lamprey, Lampetra japonica, were studied during the spawning migration by use of Kupffer's gold-chloride method, fluorescence microscopy for vitamin A (retinol) and electron microscopy. The stellate cells in the lamprey liver differ in some of their properties from those in mammalian livers. Stellate cells which store abundant retinol in lipid droplets, occur not only in the hepatic parenchyma, but also in the dense perivascular and capsular connective tissue of the liver and in the interstitium of pancreatic tissue. In the hepatic parenchyma these cells are located perisinusoidally or along thick bundles of collagen fibrils. The stellate cells display a number of large retinol-containing lipid droplets, granular endoplasmic reticulum, tubular structures, dense bodies, Golgi complex, microtubules, and microfilaments. In the space of Disse, the stellate cells and extracellular fibrilar components such as collagen fibrils and microfibrils (11–12 nm in diameter) are intervened between the two layers of basal laminae. Differentiation and possible functions of the stellate cells in the lamprey liver are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00215511
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  • 6
    Electronic Resource
    Electronic Resource
    Two stages of the differentiation of HL-60 cells induced by 1α,25 dihydroxyvitamin D3; Commitment by 1α,25 dihydroxyvitamin D3 and promotion by DMSO (1986)
    Springer
    Bioscience reports 6 (1986), S. 95-101 
    Details
    ISSN: 1573-4935
    Keywords: differentiation ; Hl-60 cells ; 1α,25 dihydroxyvitamin D3 ; commitment ; promotion ; DMSO
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract The differentiation of HL-60 cells induced by 1α,25 dihydroxyvitamin D3 was found to be separated into two stages, i.e. commitment and promotion. Most of the HL-60 cells were committed to monocyte/macrophage lineage by pretreatment with 1α,25 dihydroxyvitamin D3 (5–50 ng/ml) for 18–24 hr. The promotion in the second stage was inducer and lineage independent; treatment with 1.25% DMSO for 2 or 3 days promoted the differentiation of the committed HL-60 cells by 1α,25 dihydroxyvitamin D3 into monocyte/macrophage lineage, but not granulocyte lineage.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01145184
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  • 7
    Electronic Resource
    Electronic Resource
    L-ascorbic acid 2-phosphate stimulates collagen accumulation, cell proliferation, and formation of a three-dimensional tissuelike substance by skin fibroblasts (1989)
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Cellular Physiology 138 (1989), S. 8-16 
    Details
    ISSN: 0021-9541
    Keywords: Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: Proliferation of human skin fibroblasts was stimulated significantly by the presence of L-ascorbic acid 2-phosphate (Asc 2-P). The presence of Asc 2-P (0.1-1.0 mM) in the culture medium for 3 weeks enhanced the relative rate of collagen synthesis to total protein synthesis 2-fold as well as cell growth 4-fold. Coexistence of L-azetidine 2-carboxylic acid (AzC), an inhibitor of collagen synthesis, attenuated both effects of Asc 2-P in a dose-dependent manner. Supplementation of the medium with Asc 2-P also accelerated procollagen processing to collagen and deposition of collagen in the cell layer. Among the acidic glycosaminoglycans (GAG), another major component of extracellular matrix (ECM), deposition of sulfated forms was increased by the additive. Electron microscopic observations showed multilayered, rough endoplasmic reticulum-rich cells surrounded by dense ECM. These results indicate that Asc 2-P is useful in culture systems as a long-acting vitamin C derivative and also that it promotes reorganization of a three-dimensional tissuelike substance from skin fibroblasts in culture by stimulating collagen accumulation in the fibroblasts.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcp.1041380103
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