GLORIA

GEOMAR Library Ocean Research Information Access

X

Your email was sent successfully. Check your inbox.

An error occurred while sending the email. Please try again.

Proceed reservation?

Export
Filter
  • The Company of Biologists  (3)
Material
Publisher
  • The Company of Biologists  (3)
Person/Organisation
Language
Years
FID
  • 1
    Online Resource
    Online Resource
    Functionally polarized layers formed by epidermal cells on a permeable transparent collagen film
    The Company of Biologists ; 1988
    In:  Journal of Cell Science Vol. 91, No. 4 ( 1988-12-01), p. 491-499
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 91, No. 4 ( 1988-12-01), p. 491-499
    Abstract: Rat epidermal cells were cultured on a transparent collagen film, which was permeable to low Mr substances. Then the cells were bathed in both media (apical and basal), which were separated by the collagen membrane. The cells formed a multilayered epidermal sheet with well-developed structures of desmosomes. This sheet on a permeable support was found to be an effective permeability barrier for glucose and amino acids. The epidermal layer showed functional polarity for the uptake and excretion of nutrients, metabolites and newly synthesized proteins: glucose and amino acids were taken up exclusively from the basal medium and lactate was secreted selectively into the same medium, whereas ammonia was secreted into the apical medium. The apical media became more acidic than the basal ones, presumably due to the preferential distribution of H+ transport systems on the apical side of the epidermal layer. The epidermal cells that expressed functional polarities in vitro as described above were able to proliferate and differentiate, and remained healthy for as long as at least 40 days even using a conventional culture medium with foetal calf serum, but without any special growth factors and feeder cells.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    URL: Article
    DOI: 10.1242/jcs.91.4.491
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1988
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 2
    Online Resource
    Online Resource
    Morphological and immuno-cytochemical characterization of a hetero-spheroid composed of fibroblasts and hepatocytes
    The Company of Biologists ; 1992
    In:  Journal of Cell Science Vol. 101, No. 3 ( 1992-03-01), p. 495-501
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 101, No. 3 ( 1992-03-01), p. 495-501
    Abstract: A novel method for the preparation of spheroids containing two types of cells (hetero-spheroid) has been successfully developed by utilizing a collagen-conjugated thermo-responsive polymer, poly-N-isopropyl acrylamide (PNIPAAm), as a cell substratum. PNIPAAm solidifies above its lower critical solution temperature (LCST, about 30°C), and instantly dissolves into the culture medium below its LCST. We firstly seeded and cultured human dermal fibroblasts on the substratum up to a confluent state and then seeded rat primary hepatocytes onto the fibroblast monolayer. The hetero-spheroid was prepared by detaching the hepatocyte-attached fibroblast monolayer at a temperature below LCST and culturing it on the non-adhesive substratum. The surface area of the substratum and the seeding population ratio of each cell precisely and reproducibly regulated the size and the cell composition of the resulting hetero-spheroid, respectively. Histological and immuno-cytochemical observations of spheroids revealed characteristic organizations of fibroblasts and hepatocytes within a spheroid because the latter cells expressed albumin for up to at least 3 weeks. TEM study of the hetero-spheroid showed the presence of structures morphologically similar to the Disse’s space and the bile canaliculus, which are features characteristic of liver. These findings suggest that the method described above is useful for making a hetero-spheroid that morphologically and functionally resembles tissues or organs in vivo, i.e. an organoid.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    URL: Article
    DOI: 10.1242/jcs.101.3.495
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1992
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
  • 3
    Online Resource
    Online Resource
    Recognition of collagen by fibroblasts through cell surface glycoproteins reactive with Phaseolus vulgaris agglutinin
    The Company of Biologists ; 1992
    In:  Journal of Cell Science Vol. 101, No. 3 ( 1992-03-01), p. 625-633
    Details
    In: Journal of Cell Science, The Company of Biologists, Vol. 101, No. 3 ( 1992-03-01), p. 625-633
    Abstract: The role of glycochains of cell surface glycoproteins in the cell to collagen interaction was examined by studying the effect of lectins on the fibroblast-mediated collagen gel contraction. Lectins of Phaseolus vulgaris agglutinin (PHA), concanavalin A (ConA), lentil seed agglutinin (LCA), pea agglutinin (PSA), Ricinus communis ag-glutinin-60 (RCA), and wheat germ agglutinin (WGA) dose-dependently inhibited gel contraction, while lectins of mushroom agglutinin (ABA), peanut agglutinin (PNA), pokeweed mitogen (PWM), and soybean agglutinin (SBA) did not. Of these lectins, PHA seemed to be worthy of further analysis, because PHA, but not other lectins, inhibited spreading of fibroblasts on collagen fibrils but not on plastic or gelatin, suggesting that cell-surface glycoproteins responsive to the lectin are involved in the specific binding of fibroblasts to native collagen fibrils. The inhibitory effect of PHA-E4, an isolectin of PHA, was more intense than that of PHA-L4, another isolectin of PHA. The collagen gel contraction was also inhibited by tunicamycin and monensin in a concentration-dependent and reversible manner. These results strongly suggest that PHA-E4-reactive glycoproteins of the fibroblast surface play an important role in cell to collagen binding during the gel contraction. Five membrane proteins including β1 subunits of the integrin family were obtained by affinity chromatography with PHA-E4.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    URL: Article
    DOI: 10.1242/jcs.101.3.625
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1992
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
    Location Call Number Limitation Availability
    BibTip Others were also interested in ...
    Online Resource
Close ⊗
This website uses cookies and the analysis tool Matomo. More information can be found here...