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Biomedical subjects

R Soda

Publications and source records attributed to R Soda.

70 records · Page 4Linked to original sources
PubMed1985

Basophil immunoglobulin receptors in asthmatics under immunoscanning electron microscopy.

Immunolatex particles were used as markers for IgE receptors on basophils using electron-microscope scanning. These particles appeared to bind specifically to basophils. Basophils from atopic asthma patients showed greater binding to latex particles than those from intractable asthma patients or healthy subjects. Cap and patch formations on IgE receptors were frequently found in basophils of atopic asthmatics, and cap formation was observed only on basophils that were pear-shaped. The redistribution of IgE receptors, such as that by cap formation, may be a significant triggering mechanism for basophil activation. The latex density on basophils pre-treated with anti-human IgG was much greater in intractable asthmatics than in atopic asthmatics or healthy subjects, and almost all basophils with increased immunolatex particles were pear-shaped, suggesting the presence of some IgG receptors on the surface, and such receptors may play an important role in intractable asthma.

Asthma↗
PubMed1985

Receptor distribution and the endothelial uptake of transcobalamin II in liver cell suspensions.

To determine the nature of binding of transcobalamin II (TC-II) to liver cells, we covalently coupled purified holo-TC-II to submicron latex minibeads using glutaraldehyde. Incubation of the probe with liver cell suspensions at 4 degrees C led to its binding by endothelial cells but not by hepatocytes or Kupffer cells, as visualized by scanning electron microscopy. At 37 degrees C, the probe was internalized by the endothelium through a system of coated pits and vesicles as shown by transmission electron microscopy. Inhibition studies by pre-incubation with excess native TC-II demonstrated the specificity of binding. Fractionation of these cell suspensions on metrizamide gradients yielded large cell (hepatocyte-rich) and small cell (endothelium-rich) fractions. The binding of the minibead probe occurred again exclusively on endothelial cells in the small cell fraction. 125I-labeled holo-TC-II also bound to the small cell but not to the large cell fraction. Binding was saturable (Ka, 0.225 X 10(9) mol/L-1) and receptor number was calculated to be 1.33 X 10(3) per cell. Time-dependent incubation of 125I-labeled TC-II with the endothelium-rich fraction led to its uptake, reaching a steady-state plateau at 4 degrees C. At 37 degrees C, however, the initial uptake was followed by gradual release of the label into the medium. We conclude that in the liver, holo-TC-II binds initially to endothelium, where it is internalized and is subsequently released probably to the interstitial space. Thus, the endothelium may play a fundamental role in the regulation of the uptake of TC-II by the liver.

Animals↗
PubMed1984

Modulation of WGA binding sites on marrow sinus endothelium in state of stimulated erythropoiesis: a possible mechanism regulating the rate of cell egress.

To study the regulation of cellular and molecular traffic across the marrow-blood barrier, rat marrow endothelial surface was incubated with ferritin-conjugated concanavalin A, wheat germ agglutinin (WGA), recinus communis agglutinin I, and phytohemagglutinin. Normal animals were compared with those after erythropoietic stimulation (phenylhydrazine-induced hemolysis, phlebotomy). A selective and significant reduction in the density of WGA receptors, but not other lectins was noted congruent to the degree of reticulocytosis. Neuraminidase treatment also reduced WGA binding sites and the surface negative charge as detected by polycationic ferritin (PCF). Thus, the reduction in WGA binding sites, may reflect a decrease in the density of membrane sialic acid, rendering the endothelial surface charge less negative and providing an electrostatic attraction for the negatively charged surface of reticulocytes. The findings may also be explained by an increase in the frequency of WGA-excluding fenestrae in the endothelium. These areas, lacking sialic acid, may provide unstable areas in the membrane suitable for the passage of cells and molecules in both directions. It is concluded that, by modulating the density of sialic acid residues, the endothelium may regulate the traffic of cells and molecules across the marrow-blood barrier.

Animals↗
PubMed1984

Transendothelial transport (transcytosis) of iron-transferrin complex in the bone marrow.

To determine the transport pathway of iron-transferrin complex (Fe-TF) across the marrow-blood barrier, we labeled Fe-TF with colloidal gold and perfused rat femoral marrow with this probe. At 4 degrees C, the probe bound to the luminal surface of marrow sinus endothelium. The binding was inhibitable in the presence of excess native Fe-TF indicating the specificity of the binding. At 37 degrees C, the probe was internalized largely via a system of coated pits and vesicles and transported across the endothelium via a system of tubules and endosomal vesicles. It could not be ascertained if all Fe-TF was still associated with the colloidal gold probe within the endothelium, but the probe appeared to be externalized on the abluminal side into the interstitium where it subsequently bound to the surface of marrow erythroblasts and was internalized. Endothelium appeared to store part of the probe within a large vesicular system. No transport of Fe-TF was noted through diaphragmed fenestrations, diaphragmed vesicles, or interendothelial junctions. No endothelial uptake of this magnitude was noted when native gold particles or gold-labeled bovine serum albumin was used. Our findings indicate that in the bone marrow, gold-labeled Fe-TF is first taken up by sinus endothelium through a receptor-mediated mechanism and is possibly transported transendothelially via a vesicular system (transcytosis).

Animals↗
PubMed1984

Liver endothelium and not hepatocytes or Kupffer cells have transferrin receptors.

Using a visual probe, consisting of latex minibeads covalently linked to transferrin (TF), we found that, in rat liver cell suspensions, transferrin receptors were limited to endothelial cells. Neither hepatocytes nor Kupffer cells contained an appreciable number of TF receptors. Specificity of this reaction was demonstrated by preincubation with non-derivatized TF, which inhibited the binding. This was further confirmed by fractionation of liver cell suspensions on metrizamide gradients. The uptake of either the visual probe or 125I-labeled TF was again limited to the endothelium-rich fraction. Transferrin bound to endothelial membrane was internalized at 37 degrees C, but not at 4 degrees C, via a coated pit system. Again, hepatocytes and Kupffer cells did not internalize the probe. The findings suggest that iron may be first taken up by liver endothelium and then transmitted to parenchymal cells. These results emphasize the generally unappreciated role of endothelium in the transport across the tissue-blood barrier.

Acid Phosphatase↗
PubMed1983

Distribution of insulin receptors in liver cell suspensions using a minibead probe. Highest density is on endothelial cell.

The distribution of insulin receptors was studied in rat liver cell suspensions using a latex minibead covalently bound to insulin. This probe can be visualized by electron microscopy (EM). Using this visual probe, the highest density of the receptor was found on endothelial cells in the cell suspension, with hepatocytes having only few receptors and Kupffer cells having none. Fractionation of liver cell suspensions on metrizamide gradients yielded two populations of cells; large cells (hepatocytes) and small cells which consisted mostly of Kupffer cells and endothelial cells, distinguishable by their surface and cytoplasmic features. Again, by the use of an insulin-minibead probe, the highest density of receptors was found on endothelial cells. It is suggested that the endothelium has a crucial role in the uptake and transport of the hormone across the tissue-blood barrier.

Animals↗
PubMed1983

Mapping of the bone marrow sinus endothelium with lectins and glycosylated ferritins: identification of differentiated microdomains and their functional significance.

The distribution of lectin binding sites and sugar-recognizing systems (lectin-like substances) was studied on the luminal side of the bone marrow sinus endothelium in rats. Ferritin-conjugated lectins (Con A, PHA, RCA, WGA, UEA) and glycosylated ferritins (mannosyl, fucosyl, chitobiosyl) were used as probes. With the exception of UEA, all lectins bound to the endothelial surface. The binding was heavier on the plasmalemma proper of the nuclear region (PP-N) compared to that of the tapered region (PP-T). Lectin mapping also identified differentiated microdomains with less or no bindings. These domains related to the transport organelles in the endothelium: luminal vesicles (LV) and diaphragmmed fenestrae (DF). The relative density of binding for these four domains demonstrated the following spectrum PP-N greater than PP-T greater than LV greater than DF. The relation of this binding pattern to the transport function of marrow sinus endothelium for various cells and molecules has been discussed. Lectin mapping also identified heavily labeled microvilli and microprojections from the membrane. These organelles may have a function in recognizing cells and molecules for the transport. The absence of binding for UEA, also absent in liver endothelium, may differentiate sinus endothelia from other endothelia. This lectin is thought to be endothelium-specific in other systems. No binding was observed with glycosylated ferritins suggesting the absence of lectin-like substances on marrow sinus endothelium.

Affinity Labels↗
PubMed1983

New in vitro method for detecting asthma allergen. Counting reactive basophils after addition of allergen.

Changes in the morphology and number of basophils were examined after the addition in vitro of house dust extract in cells from seventy-seven patients with bronchial asthma. Morphological changes (reactive basophils) showed a close relation to the end-point titrations of antigen in skin tests, RAST score and bronchial provocation tests, but changes in number of basophils did not. With a RAST score of 2 or greater the change in reactive basophils varied from 40 to 80% (mean 58.1%), which was much greater than seen in persons with no RAST, score 0. Patients with positive bronchial inhalation tests, showed 40 to 80% (mean 57.8%) reactive basophils, whereas persons with a negative bronchial challenge test showed a range of reactive basophils from 0 to 50% (mean 28.9%). The difference in percentage of reactive basophils between the positive and negative groups of persons tested by bronchial inhalation was statistically significant.

Allergens↗