Surface alterations in transformed epithelial and fibroblastic cells in culture: A disturbance of membrane degradation versus biosynthesis?

Borek, Carmia; Grob, Marianne; Burger, Max M.

doi:10.1016/0014-4827(73)90569-7

Cited by 50 publications

(3 citation statements)

References 17 publications

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“…From this evidence, we would suggest that maintenance of the nonagglutinable surface architecture on these CHO subclones is dependent on the presence of protease-labile surface peptides whose association with the lectin receptors is dependent on continuous transcription and translation. Similar conclusions have been reached by Baker and Humphreys (3) as well as Borek et al (4) in work performed with other cell lines.…”

Section: Maintenance Of the Nonagglutinable Statesupporting

confidence: 90%

An analysis of lectin-initiated cell agglutination in a series of CHO subclones which respond morphologically to growth in dibutyryl cyclic AMP.

Veen¹,

Roberts²,

Noonan³

1976

The Journal of Cell Biology

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We have investigated the molecular basis of the agglutinability of CHO subclones which respond differentially in terms of morphology and surface architecture in the presence of dB-cAMP in the medium. We have demonstrated that the agglutinability of these subclones with both wheat germ agglutinin (WGA) and concanavalin A (Con A) probably depends on the free lateral mobility of the lectin receptor sites in the plane of the membrane. The nonagglutinable surface architecture seems to depend on the presence in the membrane of a proteaselabile peptide(s), which appears to be distinct from the lectin receptors, as well as on continuous protein and RNA synthesis. This dependence on continuous transcription and translation may be related to the maintenance of the protease-labile peptide(s) in such a state as to restrict mobility of the lectin receptors. The surface architecture defined as nonagglutinable also depends on the state of polymerization of the intracellular microtubules and microfilaments. It is suggested that these microskeletal elements serve to anchor the lectin receptors in such a manner as to restrict their mobility and thereby reduce the relative agglutinability of a cell line. We suggest that control of the free mobility of both the Con A and WGA receptor sites is dependent on two constraints, one applied by protease-labile ("surface") membrane components and the other by components of the intracellular microskeletal system.The role of the plasma membrane in controlling cell growth has been an actively investigated area of research over the past few years (7). In particular, many investigators have sought differences in the membrane of normal and transformed cells which might account for the different growth properties exhibited by the two cell types (24). A number of fairly consistent but not invariable types of plasma membrane modification have been reported to occur as a consequence of cell transformation. These have included (a) an increase in the average molecular weight of sialofucopeptides released from the transformed cell surface after extensive trypsin digestion (5), and (b) enhanced agglutinability of transformed ceils by plant lectins (25). It was of some interest, therefore, that the reverse of these changes (i.e. a decrease in the amount of sialic acid associated 204

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Section: Maintenance Of the Nonagglutinable Statesupporting

confidence: 90%

An analysis of lectin-initiated cell agglutination in a series of CHO subclones which respond morphologically to growth in dibutyryl cyclic AMP.

Veen¹,

Roberts²,

Noonan³

1976

The Journal of Cell Biology

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“…Moving the hydrophilic portions of these molecules through the hydrophobic interior of the membrane would require such large energies of activation (Singer, 1971) that such processes would occur only at negligible rates . These considerations are relevant to the recent proposal of Burger (1970) and Borek et al . (1973) that such transmembrane rotations or "swivels" could account for the differential agglutinability of transformed cells by the inversion of certain agglutinin sites with the simultaneous appearance of another class of agglutinin sites .…”

Section: Discussionmentioning

confidence: 68%

The Distribution and Asymmetry of Mammalian Cell Surface Saccharides Utilizing Ferritin-Conjugated Plant Agglutinins as Specific Saccharide Stains

Nicolson

Singer

1974

The Journal of Cell Biology

215

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The preparation, properties, and some applications of ferritin conjugates of two plant agglutinins, concanavalin A and Ricinus communis agglutinin, are reported . These conjugates serve as specific electron-dense stains for cell-and membrane-bound saccharide residues of the a-D-mannopyranosyl and (3-D-galactopyranosyl configurations, respectively, and as examples of a wide range of ferritin-plant agglutinin conjugates useful as high resolution saccharide stains . By using a technique for preparing flattened membrane specimens, it was found with a variety of mammalian cell plasma membranes (lymphocyte, lymphoma, and myeloma and normal, spontaneously and virally transformed fibroblasts) that the ferritin conjugates were localized exclusively to the exterior face of the membrane, with essentially none found on the cytoplasmic face . On the exterior face the topographical distribution of ferritin conjugates appeared to be random . The asymmetrical distribution of saccharide residues to the outer membrane face can be explained by an "assembly line" process whereby new plasma membrane is made from intracellular precursor membranes . It also suggests that the saccharide-containing components of the plasma membrane do not rotate at any appreciable rate from one membrane surface to the other .

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“…Grisham and coworkers clearly demonstrated that clonogenic RLEC lines are derived from the nonparenchymal cell fraction (53,77). Since some RLECs have hepatocytic characteristics (79, 82–86), these investigators reasoned that these cell lines were derived from FLSCs presumably present in the canal of Hering (53,87). In a series of elegant studies, this group has provided strong evidence to suggest that the WB‐F344 RLEC line developed in their laboratory was indeed derived from liver stem‐like cells.…”

Section: Are Normal Rat Liver Epithelial Cell Lines Derived From Bipomentioning

confidence: 99%

Liver Stem Cells: A Potential Source of Hepatocytes for the Treatment of Human Liver Disease

2001

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Severe liver injury often leads to the proliferation of oval cells, which differentiate along hepatocytic and biliary lineages. Because oval cells proliferate only when hepatocyte replication is impaired, they are considered to be the progeny of facultative liver stem cells (FLSCs). Identification and isolation of FLSCs has been hampered by the lack of markers that delineate these bipotential progenitors. We hypothesized that transition ductal cells are FLSCs because they are located in a unique anatomical niche sharing tight junctions with a neighboring hepatocyte and another terminal ductular cell. Alternatively, it has been proposed recently that bone marrow-derived stem cells are FLSCs since these cells differentiate along the hepatic lineage following colonization of the liver. The intent of this review is to provide insight into the nature and origin of liver stem cells and to explore the possibility that stem cell technology may lead to the development of clinical modalities for the treatment of human liver disease.

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Surface alterations in transformed epithelial and fibroblastic cells in culture: A disturbance of membrane degradation versus biosynthesis?

Cited by 50 publications

References 17 publications

An analysis of lectin-initiated cell agglutination in a series of CHO subclones which respond morphologically to growth in dibutyryl cyclic AMP.

An analysis of lectin-initiated cell agglutination in a series of CHO subclones which respond morphologically to growth in dibutyryl cyclic AMP.

The Distribution and Asymmetry of Mammalian Cell Surface Saccharides Utilizing Ferritin-Conjugated Plant Agglutinins as Specific Saccharide Stains

Liver Stem Cells: A Potential Source of Hepatocytes for the Treatment of Human Liver Disease

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