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Biomedical subjects

A E Vatter

Publications and source records attributed to A E Vatter.

At least 37 records · Page 2Linked to original sources
PubMed1982

Inhibitors of coaggregation between Actinomyces viscosus T14V and Streptococcus sanguis 34: beta-galactosides, related sugars, and anionic amphipathic compounds.

Coaggregation between Actinomyces viscosus T14V (T14V) and Streptococcus sanguis 34 (Ss34) depends upon specific reaction between lectin on T14V and carbohydrate on Ss34. Studies on coaggregation inhibition by sugars related to D-galactose, beta-galactosides, and amphipathic molecules revealed: (i) D-fucose, D-talose approximately equal to D-galactose, which was 0.2 potency of lactose. No other hexoses or pentoses inhibited at 0.1 M. (ii) Gal beta (1 leads to 3)GalNAc alpha OCH2C6H5 was the most potent beta-galactoside inhibitor; it had 20 times the potency of lactose. (iii) Anionic nonaromatic amphipathic compounds were good inhibitors; sodium deoxycholate (I) was equal to lactose; sodium dodecyl sulfate (II) had 15 times the potency of lactose; there was 90 to 100% irreversible inhibition when T14V was treated with 0.005 M (II). Treatment of Ss34 with II had no effect. (iv) Synergism of inhibition was observed between lactose and I or lactose and II, e.g., inhibition by 0.01 M lactose = 5%; inhibition by 0.01 M I = 9%; inhibition by 0.01 M lactose + 0.01 M I = 87%. (v) The irreversible inhibition by II was prevented when 0.25 M lactose or 0.25 M I was present during treatment of T14V with 0.005 M II. (vi) Synergism and prevention by lactose or by I of irreversible inhibition by II suggest that all three react at the same site on T14V lectin. We hypothesize that the T14V lectin combining site for Ss34 carbohydrate has specific affinity for beta-galactosides and for anionic nonaromatic amphipathic molecules. This site can be saturated by either kind of reagent to exclude the other reagent or to inhibit coaggregation.

Actinomyces↗
PubMed1982

Antibodies against the Ag2 fimbriae of Actinomyces viscosus T14V inhibit lactose-sensitive bacterial adherence.

Monospecific antisera against the Ag1 and Ag2 fimbrial components of Actinomyces viscosus T14V were produced by immunizing rabbits with immune precipitates of each antigen harvested from crossed-immunoelectrophoresis plates. The Fab fragments prepared from these sera were used as specific reagents in immunoelectron microscopy to identify each fimbrial component on the bacterial surface and also were assayed for their abilities to prevent the coaggregation of A. viscosus T14V with Streptococcus sanguis 34, an interaction that is lactose sensitive. Each Fab preparation appeared to react with different fibrillar structures present on the actinomycete, and only the Ag2-specific Fabs blocked coaggregation. These results provide strong support for the presence of distinct types of fimbriae on A. viscosus T14V and indicate the exclusive involvement of Ag2 fimbriae in lactose-sensitive adherence.

Actinomyces↗
PubMed1981

Detection and localization of a lectin on Actinomyces viscosus T14V by monoclonal antibodies.

A cell-associated lectin activity that mediates lactose-inhibitable adherence of Actinomyces viscosus T14V has been localized to a specific population of fimbriae by the use of monoclonal antibodies. Nine monoclonal antibodies were produced that reacted with only 1 of 2 immunoelectrophoretically distinct fimbrial components on T14V. The fibrillar morphology of this component was revealed by the immunoelectronmicroscopic examination of bacteria incubated with the monoclonal antibodies. The lectin activity associated with these structures was detected when isolated fimbriae were cross-linked with monoclonal antibodies to form immune complexes with agglutination activity for neuraminidase-treated human erythrocytes, a reaction that was inhibited by lactose. Although the 9 monoclonal antibodies differed in their fine specificities, they reacted only with strains of A. viscosus and A. naeslundii that exhibited lactose-inhibitable adherence. These findings indicate that the lectin activity common to these bacteria resides on fimbriae that are antigenically related to those of T14V.

Actinomyces↗
PubMed1980

Isolation of lung lamellar bodies and their conversion to tubular myelin figures in vitro.

Lamellar bodies of type II alveolar epithelial cells are the intracellular storage sites of lung surfactant, while tubular myelin figures are an extracellular surfactant form found in the alveolar fluid. A refined procedure was used to isolate intact lamellar bodies from rat lung homogenates in a fraction of high purity and yield. The stability of isolated lamellar bodies under various conditions was determined by electron microscopy. Lamellar bodies were completely disrupted after incubation at 37, 24, and 0 degrees C for 0.6, 2, and 12 hr, respectively, in 0.33 M sucrose, 0.01 M HEPES (pH 7.4). In addition, they were completely disrupted after incubation for 1 hr in 0.33 M sucrose, 1 mM EGTA at 0 degrees C or 0.154 M NaCl or 0.10 M sodium phosphate (pH 7.4) at 24 degrees C. Incubation of isolated lamellar body fractions in medium containing 5 mM Ca++ or Mg++ at 37 degrees C for 1 hr resulted in the appearance of tubular myelin figures. A procedure is also presented for the isolation of tubular myelin figures from rat lung lavage fluid.

Animals↗
PubMed1979

Surface fibrils (fimbriae) of Actinomyces viscosus T14V.

Surface antigens of Actinomyces viscosus T14V were released from cell walls by digestion with lysozyme. These were separated by ion-exchange and gel filtration chromatography into fractions rich in carbohydrate or protein. The former contained a polysaccharide high in 6-deoxytalose, along with a peptide fragment from the cell wall. In the protein-rich fractions, material of high molecular weight was present, which contained some carbohydrate and up to 14.3% nitrogen. Aspartic acid, threonine, glutamic acid, lysine, alanine, and glycine were detected in these fractions, along with smaller amounts of 10 other amino acids. Most of the alanine was present as the L isomer and thus was not from peptidoglycan. Electron microscopy of the high-molecular-weight material revealed long fibrils, 3.5 to 4.5 nm in diameter, which resembled those seen on bacterial cells. V-specific antiserum, prepared by absorbing anti-A. viscosus T14V serum with cell walls of the avirulent strain (A. viscosus T14AV), did not react with the 6-deoxytalose polysaccharide but reacted well with isolated fibrils, and this was not inhibited by 6-deoxytalose.

Actinomyces↗
PubMed1978

Fimbriae of Actinomyces viscosus t14v: their relationship to the virulence-associated antigen and to coaggregation with Streptococcus sanguis 34.

1) Fimbriae from A. viscosus T14V may be similar to those found on other bacteria. 2) The antigenic difference between virulent and avirulent A. viscosus T14 appears to be of a quantitative rather than a qualitative nature and is related to fimbriae and not to the cell wall polysaccharide. 3) Coaggregation between A. viscosus T14V and S. sanguis 34 is mediated by fimbriae on the former which have specificity for beta-linked galactosyl residues.

Actinomyces↗
PubMed1978

Identification of the virulence-associated antigen on the surface fibrils of Actinomyces viscosus T14.

Actinomyces viscosus T14V is virulent (V) for monoinfected rats, causing periodontal disease and bone loss, whereas, A. viscosus T14AV, a mutant strain, is avirulent (AV). Surface antigens from the T14V and T14AV strains were prepared by lysozyme digestion of cell walls and were compared by immunodiffusion against antisera to T14V and T14AV whole cells. The V-associated antigen (V-antigen) was detected readily in the T14V, but not readily in the T14AV cell wall extract. Antiserum specific for the V-antigen was prepared by absorbing anti-A. viscosus T14V serum with cell walls from the T14AV strain. This antiserum was used in the indirect peroxidase-labeled antibody technique to localize the V-antigen on the bacterial cell surface at the ultrastructural level. With whole bacterial cells, the V-antigen was found on fine fibrils and was detected in both the T14V and T14AV strains. The presence of V-antigen on the AV strain was supported by the demonstration of antibodies against the V-antigen in anti-A. viscosus T14AV serum. Examination of isolated bacterial cell walls revealed a greater amount of fibrils and V-antigen on the T14V cell wall than on the T14AV cell wall. The data suggest that the presence of V-antigen represents a quantitative rather than a qualitative difference between the V and the AV strains of A. viscosus T14. Samples of human plaque were examined, and the V-antigen was found to be a specific marker for the fibril-containing layer of certain plaque bacteria, which are probably strains of A. viscosus or A. naeslundii.

Actinomyces↗
PubMed1978

Mechanism of coaggregation between Actinomyces viscosus T14V and Streptococcus sanguis 34.

Actinomyces viscosus T14V and Streptococcus sanguis 34 coaggregate by a mechanism which is not inhibited by 1 M NaCl, is dextran independent, requires calcium, is pH dependent with an optimum at pH 8.0 to 8.5, and appears to require the interaction of a protein or glycoprotein on A. viscosus with a carbohydrate on S. sanguis. The coaggregation is inhibited more than 80% by 0.01 M lactose, 0.02 M beta-methyl-D-galactoside, or 0.05 M D-galactose; inhibition of coaggregation was less than 10% in 0.1 M alpha-methyl-D-galactoside, melibiose, maltose, cellobiose, sucrose, and a number of monosaccharides. At very high concentrations of enzyme, protease from S. griseus destroyed the reactive site on A. viscosus but not on S. sanguis. Both were totally resistant to dextranase. Periodate (0.01 M; pH 4) inactivated both bacteria. The ability of S. sanguis to coaggregate with A. viscosus was not destroyed by phenol-water extraction at 65 degrees C for 15 min. When the bacteria were cultured under specified conditions, the coaggregation was highly reproducible. Under the same conditions, T14AV, the avirulent mutant of A. viscosus T14V, did not coaggregate with S. sanguis 34. Electron microscopic studies of coaggregates, labeled immunochemically with antibody to A. viscosus, indicated that fibrils on A. viscosus may be involved in the coaggregation.

Actinomyces↗
PubMed1977

A mode of formation of tubular myelin from lamellar bodies in the lung.

A mechanism is suggested by which the membranes of lamellar bodies are converted to tubular myelin (TM) in the lung. It is argued that a simple corrugation of the membranous sheets can produce the TM formation. Such corrugation would occur in response to simple stresses acting on the lamellar body membranes. The intersections of the tubular figures are formed by fusion of adjacent corners in the corrugations. This results in a more stable hydrophobic bonding of phospholipid molecules. Strong supportive evidence for the mechanism is given by electron micrographs of TM formations.

Animals↗
PubMed1977

The requirement of viable thymocytes for species-specific attachment to and release from macrophages.

The role of the thymocyte in its species-specific binding to macrophages has been explored. Although formalin treatment of macrophages resulted in loss of binding to thymocytes, formalin treatment of thymocytes did not have this effect. However, two differences between living and formalin-treated thymocytes were noted. Formalin-treated thymocytes bound to macrophages of any species whereas the binding of living thymocytes was species specific. Living thymocytes attained maximum binding in approximately 1 hr and then the fraction bound gradually diminished. Formalin-treated thymocytes remained bound to the macrophage and appeared to be phagocytized. Released thymocytes did not bind to fresh macrophages, but released macrophages bound to fresh thymocytes. The results suggest that the binding of thymocytes to macrophages results in maturation of thymocytes.

Animals↗
PubMed1977

Isolation and enumeration of peripheral blood monocytes.

Monocytes were isolated by counterflow contrifugation from human peripheral mononuclear cells obtained from whole blood by the Ficoll-Hypaque technique. Examination of volume spectra of the monocytes showed a bimodal distribution with peaks at 330 and 370 micron3. The upper peak contained 61.4 +/- 3.3% of the total monocyte population, whereas the remainder were in the lower peak which overlaps the lymphocyte spectrum. The purity of the monocyte preparations from six normal adult donors, identified by peroxisomes observed by electron microscopy, was 90.4 +/- 1.6%.

Adult↗
PubMed1976

Morphological and physical basis for lung surfactant action.

An abhesive or 'anti-glue' function for lung surfactant is proposed which is reconcilable with the known unfolding of alveolar walls at low lung volumes. The theory is developed based upon the fact that the work required to part wetted surfaces is directly proportional to the surface tension. Application of the concept of the spreading coefficient from surface physical chemistry S = gammata-(gamma lla + gamma lle), where the gamma's refer to the surface (interfacial) tensions among the tissue (t), air (a) and lining layer (ll) surface, is shown to explain qualitatively physiological data in lungs subjected to maneuvers with working fluids varying widely in surface tension and spreading properties.

Animals↗
PubMed1975

Adenine nucleotides in the secretory granule fraction of rat islets.

Concomitant with glucose-induced insulin release, there occurred an increase of ATP from 4.40 plus or minus 0.21 to 23.16 plus or minus 0.52 pmol/100 islets/min (P less than 0.001) in the effluent from perifused rat islets. There is a linear relationship between circulating ATP and insulin levels both in the stimulated and basal state (r = 0.689, P less than 0.01). Islets incubated with labeled adenine for a short period of time (37.5 min) showed no release of radioactivity upon subsequent glucose-induced insulin release. Islets incubated for a prolonged interval with labeled adenine (150 min) showed an increase in acid soluble radioactivity in the effluent during glucose-induced insulin release. Following incubation of the islets with labeled adenine for 150 min, approximately 5% of the homogenate radioactivity was found in the secretory granules. Using column chromatography to separate the adenine nucleotides, the distribution of radioactivity among the various nucleotides in the secretory granule fraction was found to be: AMP 54.42 plus or minus 4.96%, ADP 14.20 plus or minus 1.63%, ATP 15.39 plus or minus 3.84%, and cAMP 16.07 plus or minus 2.11%. The distribution of radioactivity in the effluent adenine nucleotides after glucose-induced insulin release was: AMP 32.83 plus or minus 4.62%, ADP 24.52 plus or minus 2.77%, ATP 28.13 plus or minus 5.45%, and cAMP 26.01 plus or minus 3.34%. The absolute levels of adenine nucleotides in the secretory granules were ATP 4.19 plus or minus 0.88, ATP madp 7.94 plus or minus 2.20 and cAMP 4.46 plus or minus 1.74 pmol/ug prot. The levels in the islet effluent were ATP, 15.30 plus or minus 2.70, ATP qDP, 29.43 plus or minus 3.49 and cAMP 7.66 plus or minus 1.93 pmol/100 islets/min for the first ten min of glucose-stimulated insulin release. Thereafter there was a rapid decline in effluent cAMP while ATP and ADP remained in essentially equivalent amounts. The distribution of radioactivity and absolute levels of the adenine nucleotides in the effluent reflects that found in the secretory granules, confirming previous observations that insulin release is occurring by exocytosis.

Adenine Nucleotides↗