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Biomedical subjects

H Beug

Publications and source records attributed to H Beug.

193 records · Page 11Linked to original sources
PubMed1973

Quantitation of membrane sites in aggregating Dictyostelium cells by use of tritiated univalent antibody.

Cell-to-cell adhesion during aggregation of Dictyostelium discoideum cells is completely blocked by univalent antibody (Fab) directed against two classes of target sites: surface structures characteristic for aggregation-competent cells ("contact sites A") and others present also on growth-phase cells ("contact sites B"). 3 x 10(5) Fab molecules bound per cell are sufficient to block contact sites A completely, although the Fab fragments cover not more than 2% of the total cell surface. Up to 8-fold this value can be bound per cell when Fab fragments of another specificity are used, without affecting activity of contact sites A. Blockage of cell-to-cell adhesion therefore depends on the binding of Fab fragments to specific target sites, rather than on the total number of Fab molecules bound per cell. This conclusion is also valid for cell adhesion attributed to contact sites B. Contact sites therefore represent a special class of cell-surface sites which, in cell homogenates as well as in vivo, can be traced by Fab, and which are not identical with the bulk of cell-surface antigens present on aggregating cells.

Agglutination↗
PubMed1973

Dynamics of antigenic membrane sites relating to cell aggregation in Dictyostelium discoideum.

Membrane interaction in aggregating cells of Dictyostelium discoideum can be blocked by univalent antibodies directed against specific membrane sites. Using a quantitative technique for measuring cell association, two classes of target sites for blocking antibodies were distinguished and their developmental dynamics studied. One class of these sites is specific for aggregation-competent cells, their quantity rising from virtually 0-level during growth, with a steep increase shortly before cell aggregation. The serological activity of these structures is species specific; they are not detectable in a nonaggregating mutant, but present in a revertant undergoing normal morphogenesis. Patterns of cell assembly in the presence of antibodies show that selective blockage of these membrane sites abolishes the preference for end-to-end association which is typical for aggregating cells. A second class of target sites is present in comparable quantities in particle fractions from both growth-phase and aggregation-competent cells. Blockage of these sites leads to aggregation patterns in which the side-by-side contacts of aggregating cells are abolished. The target sites of aggregation-inhibiting antibodies are suggested to be identical or associated with the molecular units of the cell membrane that mediate cell-to-cell contacts during aggregation. The results indicate that in one cell, two independent classes of contact sites can be simultaneously active.

Binding Sites, Antibody↗
PubMedDate not supplied

Two-dimensional gel mapping of small GTPases reveals transformation-specific changes during oncogenesis.

Epithelial cells transformed by oncogenes in vitro change their gene expression program, thereby losing features of cell polarity and cell adhesion. Using ras-transformed mammary epithelial cells, we have investigated the expression of other small GTP-binding proteins by high-resolution two-dimensional gel electrophoresis and direct GTP ligand binding after renaturing transfer onto nitrocellulose. Ras-transformed cells lost the expression of one epithelial-specific GTP-binding protein (21-22 kDa, pI 4.5-4.8) and instead expressed a fibroblast GTP-binding protein (21-22 kDa, pI 4.8-5.0).

Animals↗
PubMedDate not supplied

Identification of a form of the avian erythroblastosis virus erb-B gene product at the cell surface.

Avian erythroblastosis virus (AEV) induces both erythroblastosis and fibrosarcoma in chickens. The viral oncogene responsible for these diseases, erb, is divided into two regions, erb-A and erb-B, although recent evidence suggests that it is primarily the erb-B gene product that is responsible for the transforming activity. The erb-B gene product has been reported previously to be a membrane glycoprotein of 68,000 molecular weight (MW), gp68erb -B. However, we show here that gp68erb -B is an intracellular precursor which is modified further to a 74,000 MW protein, gp74erb -B. By the criteria of resistance to digestion with endoglycosidase H, subcellular fractionation and inhibition of biosynthesis by the ionophore monensin, gp74erb -B appears to be located at the cell surface. Recently, a comparison of the erb-B sequence with that of the epidermal growth factor (EGF) receptor has shown that these two genes are highly homologous, and that erb-B appears to represent a truncated form of this growth factor. In light of these data the identification of gp74erb -B at the plasma membrane suggests that this may be the functionally important form of the erb-B gene product.

Alpharetrovirus↗
PubMedDate not supplied

The c-erb-A protein is a high-affinity receptor for thyroid hormone.

Hormone binding and localization of the c-erb-A protein suggest that it is a receptor for thyroid hormone, a nuclear protein that binds to DNA and activates transcription. In contrast, the product of the viral oncogene v-erb-A is defective in binding the hormone but is still located in the nucleus.

Amino Acid Sequence↗
PubMedDate not supplied

Expression of virus specific morphological cell transformation induced in enucleated cells.

Chick embryo fibroblasts infected by a temperature sensitive mutant of Rous sarcoma virus were enucleated with Cytochalasin B. The cytoplasts were still able to transform morphologically when shifted from nonpermissive to permissive temperature, and to revert ot normal morphology when shifted from permissive to nonpermissive temperature. This indicates that the viral gene product responsible for transformation acts primarily on cytoplasmic or membrane components and not on the nucleus.

Animals↗