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Biomedical subjects

M R Banyard

Publications and source records attributed to M R Banyard.

14 recordsLinked to original sources
PubMed1998

Prevalence of intercurrent disease in dogs and cats presented for vaccination at a veterinary practice.

A prospective study was undertaken to determine the prevalence of intercurrent disease in dogs and cats presented for vaccination in general practice. Fifty-two percent of animals were found to suffer from intercurrent disease and 3% had severe debilitating disease. A thorough clinical examination conducted at the time of routine vaccination appears to be an important element in maintaining companion animal health and welfare.

Age Factors↗
PubMed1990

Microfilament organization correlates with increased cellular content of gelsolin.

The relative amounts of intracellular gelsolin were determined in a number of human somatic cell hybrids and parental cell lines which greatly differ in their microfilament organizations. In contrast to the disruptive effect of gelsolin on actin filament formation in vitro, there is a correlation between the degree of microfilament organization and the amount of gelsolin within these cell lines.

Actin Cytoskeleton↗
PubMed1987

Distribution of calcium ATPase in the sarcoplasmic reticulum of fast- and slow-twitch muscles determined with monoclonal antibodies.

Four monoclonal antibodies against the calcium ATPase in sarcoplasmic reticulum (SR) of rabbit fast-twitch skeletal muscle were characterized using SDS-PAGE, Western blots and immunofluorescence. The ultrastructural distribution of the antigens was determined using post-embedding immunolabeling. The antibodies recognized the calcium ATPase in the SR but not in transverse (T-) tubule or plasma membranes. The antibody, D12, had the same binding affinity for the calcium ATPase from fast-twitch (rabbit sternomastoid) and slow-twitch (rabbit soleus) fibers and the affinity fell by 30% after fixation for electron microscopy in both types of muscle fiber. Ultrastructural studies revealed that the density of D12 antibody binding to the terminal cisternae membrane of extensor digitorum longus (edl) and sternomastoid fibers was on average seven times greater than in the slow-twitch soleus and semimembranosus fibers. Since the affinity of the ATPase for the antibody was the same in SR from fast- and slow-twitch muscles, the concentration of calcium ATPase in the terminal cisternae membrane of fast-twitch fibers was seven times greater than in slow-twitch fibers. This conclusion was supported by the fact that the concentration of calcium ATPase in light SR membranes was six times greater in SR from fast-twitch fibers than in SR from slow-twitch fibers. The results provide strong evidence that the different calcium accumulation rates in mammalian fast- and slow-twitch muscles are due to different concentrations of calcium ATPase molecules in the SR membrane.

Animals↗
PubMed1986

Increased actin nucleating activity in tumorigenic cells.

The kinetics of actin polymerization has been used to quantitate the relative levels of actin nucleating activity in extracts from a number of related tumorigenic and non-tumorigenic cells. The level of nucleating activity was significantly elevated in the tumorigenic compared with the non-tumorigenic cell extracts whether the results were expressed on the basis of per protein (2-3 fold increase) or per total endogenous cellular actin (3-4 fold increase). It is concluded that this activity is probably due to an actin filament capping/severing regulatory protein(s) and that this protein(s) may be, at least partially, responsible for the microfilament disruption observed in transformed cells.

Actin Cytoskeleton↗
PubMed1985

The free cytoplasmic calcium concentration of tumorigenic and non-tumorigenic human somatic cell hybrids.

The fluorescent indicator of Ca2+ concentration, quin-2, has been used to measure the concentration of free Ca2+ in the cytoplasm of tumorigenic and non-tumorigenic human somatic cell hybrids. The cell hybrids were derived from the fusion of a HeLa derivative (D98 AH2) and normal human fibroblasts. The calcium concentration of the tumorigenic cell lines was 180 +/- 7nM and the level in the non-tumorigenic cells was 136 +/- 6nM. This difference was statistically highly significant (P less than 0.001). Control experiments are reported which show that the level of 3a2+ measured is not influenced by cell density or by the concentration of quin-2-tetra-(acetoxymethyl)ester used in these experiments. The possible implications of this elevated level of cytoplasmic calcium in tumorigenic cells are discussed.

Aminoquinolines↗
PubMed1985

Identification of a common antigen on human erythrocyte sialoglycoproteins.

An erythrocyte sialoglycoprotein common antigen has been identified by a monoclonal antibody. The antigen recognised by the JCS-2 antibody was determined by immunoprecipitation, Western blotting and partial amino acid sequencing. Western blot analysis of human erythrocyte ghost membranes separated on sodium dodecyl sulphate polyacrylamide gel electrophoresis shows that the sialoglycoprotein common antigen occurs on the alpha, beta, gamma and delta sialoglycoproteins, either in their monomeric or dimeric form and as the heterodimer in the case of alpha and delta. The N-terminal sequence of the antigen prepared by immunoaffinity chromatography of the Triton-X100 extract of human erythrocyte ghosts shows the first 9 residues to be identical to the known sequence of the MN blood group glycoproteins. The common epitope on the sialoglycoproteins resides on the oligosaccharide and contains sialic acid.

Antibodies, Monoclonal↗
PubMed1985

Actin synthesis in tumorigenic and non-tumorigenic human hybrid cells.

We have previously shown that the total actin content of tumorigenic HeLa/fibroblast somatic cell hybrids is significantly lower than that of the non-tumorigenic hybrid cells. A measure of actin synthesis, relative to total protein synthesis, was obtained for these cells to determine whether the reduced actin content of the tumorigenic cells is due to specific suppression of actin synthesis. Actin synthesis was measured in cells labelled with [35S]methionine using DNase I affinity chromatography to isolate the actin quantitatively. The results show that actin synthesis is not specifically suppressed, since the relative amount of actin synthesized is constant for the tumorigenic and non-tumorigenic cell lines. The reduced actin content of the tumorigenic cells is therefore most likely to be the result of increased degradation of actin.

Actins↗
PubMed1984

A comparison of the expression of the DIDS-binding proteins from normal and tumorigenic human cells.

A monoclonal antibody was prepared against DIDS, an inhibitor of anion transport, and used to compare the occurrence and distribution of DIDS-binding sites of tumorigenic and non-tumorigenic human somatic-cell hybrids. The monoclonal antibody (E8) was produced by the fusion of the mouse myeloma (NS-1) with mouse spleen cells and is of the IgG1 subclass. The apparent half-saturation of DIDS for HEp-2 cells is 16 microM and the reaction is rapid. The number of binding sites on tumorigenic and non-tumorigenic hybrid cells was the same. The DIDS-binding protein occurs homogeneously on all cells, a characteristic which distinguishes it from the possible tumour antigen recognised by the M/27 monoclonal antibody.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗
PubMed1984

Association of an integral membrane protein with glucose transport and with anion transport.

A monoclonal antibody that recognizes a cell-surface glycoprotein associated with glucose transport was reported previously. Additional information about the function and intracellular distribution of the antigen recognized by this antibody is presented. The monoclonal antibody recognizes a cell-surface and a cytoplasmic determinant. The density of the cell-surface determinant is heterogeneous within the cell population. The subpopulation of cells that carry the cell-surface determinant at high density correspond with a subset of cells that incorporate 2-deoxy-D-[3H]glucose more rapidly than the population as a whole. The monoclonal antibody is used, with cell-affinity chromatography, to isolate this subset of cells. The cytoplasmic determinant, to which the antibody binds, is associated with the cytoplasmic microfilaments but the antibody is not absorbed by actin. The cell-surface and cytoplasmic components are not identical since the apparent affinity of the antibody for each site is different. The portion of the antigen in the membrane behaves as an integral membrane protein while the remainder is tightly associated with the detergent-insoluble cytoskeleton. The expression of the antigen on the cell surface is modified by covalent attachment of an inhibitor of anion transport, 4,4'-diisothiocyano-2,2'-disulphonic stilbene. The possible interaction of the anion/lactate transporter with the glucose transporter is discussed.

4,4'-Diisothiocyanostilbene-2,2'-Disulfonic Acid↗
PubMed1984

Microfilament organization and total actin content are decreased in hybrids derived from the fusion of HeLa cells with human fibroblasts.

The organization of the microfilaments and the actin content of matched pairs of tumorigenic and non-tumorigenic HeLa/fibroblast hybrid cells was compared. Each pair consisted of a hybrid cell line with suppressed tumorigenicity and a segregant tumorigenic cell line derived from it. The tumorigenic HeLa parent cell line and a non-tumorigenic human fibroblast line were also included in the comparison. Microfilament organization of the cell lines was assessed by fluorescence microscopy using NBD-phallacidin, a probe that specifically binds to actin filaments. The re-expression of tumorigenicity is associated with a loss of microfilament organization. The actin content, as measured by the DNase I inhibition assay, was significantly lower in the tumorigenic hybrids and the HeLa parent than in the non-tumorigenic cells. The comparison was significant when the actin concentration was expressed either per cell or per protein. Despite this reduced level of total actin in tumorigenic cells, the ratio of monomeric to total actin remained constant in all cell lines tested.

Actins↗
PubMed1982

The fractionation and characterization of bovine tear proteins, especially lactoferrin.

Gentle procedures are described for the fractionation of bovine tear fluid by a combination of centrifugation, salt precipitation, gel filtration and ion exchange chromatography. Fractions are examined by gel electrophoretic immunological methods. Reference patterns are compiled and compared with bovine milk and serum patterns. Properties of some of th components are determined. Lactoferrin is isolated in two separate, but closely related, fractions. An acidic protein with a molecular weight of 23 000 daltons, is also isolated. Distinct heterogeneity is observed between individual animals, suggestive of a genetic polymorphism. A method is presented for the determination of the antibacterial activity of tear fluid and its fractions.

Amino Acid Sequence↗
PubMed1980

A genetic influence on the appearance of specific antibody in serum and secretions following challenge with antigen.

The concentration of specific antibody in the tear secretion following subconjunctival inoculation with Keyhole Limpet haemocyanin was influenced by genotype. Cattle of the Bos indicus type responded more strongly to subconjunctival inoculation than did Bos taurus animals. The regression analysis of the concentration of specific antibody in tears on the concentration of specific antibody in the serum suggested a quantitative difference in the transfer of specific antibody from the serum to tears. The concentration of specific antibody in serum was different in Bos indicus and Bos taurus animals. The relative position of this difference was influenced by the route of inoculation used.

Animals↗