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Biomedical subjects

C Tagesson

Publications and source records attributed to C Tagesson.

At least 73 records · Page 4Linked to original sources
PubMed1979

The prerequisites for local lysolecithin formation in the human gallbladder. III. Demonstration of two different phospholipase A activities.

The positional specificity of the phospholipase A (EC 3.1.1.4) in human gallbladder epithelium has been studied using 14C-phosphatidylethanolamine radiolabeled either in the 1-acyl or in the 2-acyl position. After heating of homogenized epithelial cells at 70 degrees C for 2 min, their lysophospholipase activity was lost. In contrast, the ability to hydrolyze 14C-phosphatidylethanolamine in biosynthetically radiolabeled Escherichia coli was largely retained. The amounts of radioactivity found in the products of hydrolysis under different conditions suggest that there are two different phospholipase A activities in the gallbladder epithelium: one, with optimal activity at pH 7, that requires Ca2+ and is specific for the 2-acyl position, and another, with optimal activity at pH 4, that does not require Ca2+ and that, apart from the 2-acyl position, attacks the 1-acyl position as well. It is possible, therefore, that a complete deacylation of diacylphosphoglycerides in the gallbladder wall is brought about in two different ways: at neutral pH through a combined action of phospholipase A2 and lysophospholipase, the latter being able to hydrolyze the 1-acyl-lysophosphoglyceride, and, at acid pH, through the action of phospholipase A1 and A2 activity, presuming 1-acyl- and 2-acyl-lysophosphoglycerides are also attacked. Both these processes have to be considered in order to explain a turnover of diacylphosphoglycerides that physiologically would prevent the accumulation of lytic lysophosphoglycerides. The possible relevance of these findings to the pathogenesis of aseptic cholecystitis is inferred.

Calcium↗
PubMed1978

The biochemical prerequisites for preventing pathogenic lysolecithin activity in the human gallbladder. II. Studies on the subcellular localization of lysophospholipase.

The subcellular localization of lysophospholipase activity in the human gallbladder epithelium was studied by differential and density gradient centrifugation. The highest relative specific activity was found in the microsomal fraction, although the enzyme appeared in mitochondria and lysosomes as well. The cytosol did not contain any significant lysophospholipase activity, but large amounts of enzyme were solubilized during centrifugation in sucrose gradients. These findings are discussed in relation to the distribution and properties of lysophospholipase in other cells and tissues and with regard to physiological implications. The possible relevance to the pathogenesis of aseptic cholecystitis is inferred.

Centrifugation, Density Gradient↗
PubMed1978

Passage of molecules through the wall of the gastrointestinal tract. I. A simple experimental model.

We describe here a simple experimental model for studying how the structural integrity of the intestinal wall is related to the transmural passage of molecules into the circulation. The model is based on the deposition of fluorescently labeled dextran in the intestine and its eventual recovery in the portal blood and mesenteric lymph. The fluorescent compound can be determined with sensitivity and ease by using fluorescence spectrometry. As judged from chromatography on Sephadex G-100, the compound was not degraded or otherwise chemically altered on its route of passage. The rate of passage was inversely proportional to the molecular size. The model may prove useful for studying factors that influence the transmission of macromolecules across the intestinal wall. Such a transmission probably underlies the pathogenesis of a variety of diseases.

Animals↗
PubMed1978

The prerequisites for local lysolecithin formation in the human gallbladder. II. Studies on the positional specificity of the phospholipase A activity.

The positional specificity of the phospholipase A in human gallbladder epithelium was studied by using biosynthetically radioabeled diacylphosphoglycerides as substrates. Diacylphosphoglyceride in 14C-palmitic acid-labeled, autoclaved E.coli was hydrolyzed under the formation of monoacylphosphoglyceride and fatty acid that were both radiolabled. In contrast, diacylphosphoglyceride in 14C-oleate-labeled bacteria was hydrolyzed so as to give radiolabel in the fatty acid only. Since 14C-palmitate occupies predominantly the 1-acyl position and 14C oleate the 2-acyl position of the major E. coli diacylphosphoglycerides, these findings suggest that: 1) the phospholipase attacks and 2-position of diacylphosphoglycerides, and 2) a complete deacylation of diacylphosphoglycerides in the gallbladder wall is brought about by the combined action of phospholipase A2 and lysophospholipase, the latter being able to hydrolyze the 1-acyllysophosphoglyceride. It appears, therefore, that the biochemical preequisites for a local formation and degreadation of lysolecithin in the gallbladder itself are met by the positional specificity of theenzymes present. This finding further substantiates the hypothesis that lysolecithin is an adjustable mediator of aseptic cholecystitis.

Cholecystitis↗
PubMed1977

The tendency of smooth and rough Salmonella typhimurium bacteria and lipopolysaccharide to hydrophobic and ionic interaction, as studied in aqueous polymer two-phase systems.

In aqueous two-phase system, the partition of bacteria and lipopolysaccharide from a rough (R) strain (Rd-mutant) of Salmonella typhimurium is influenced by polymers with covalently linked hydrophobic groups indicating hydrophobic structures accessible at the cell surface. Furthermore, the partition of the R bacteria is influenced by a number of inorganic positive and negative ions, presumably as a consequence of interaction with negatively charged surface structures. In contrast, smooth (S) bacteria and lipopolysaccharide from the parent strain do not seem to participate in either hydrophobic or charge interaction indicating extensive hydrophilicity without charge. Thus, the S-specific polysaccharide side chain of S. typhimurium might serve the purpose of blindfolding aspecific host defence mechanisms dependent on hydrophobicity and charge. On the contrary, the R bacteria and R lipopolysaccharide have physico-chemical properties which predispose to interaction with several types of cells, organelles and molecules.

Dextrans↗
PubMed1977

Association of some enterobacteria with the intestinal mucosa of mouse in relation to their partition in aqueous polymer two-phase systems.

The association of enterobacteria with mouse intestinal mucosa has been investigated by pumping heat-killed, radioactively-labelled bacteria through the gut lumen in vitro. Approximately 20 cm of the small intestine proximal to the ileo-caecal valve was rinsed, excised and maintained in an organ bath. By using two different bacteria labelled with different radioactive isotopes, the relative association of the two bacterial pumped through the same piece of gut was determined. Cross-labelling showed that choice of isotope did not affect the association. Salmonella typhimurium 395 MR10 was used as reference and the other bacteria investigated related to it. S. typhimurium MR10 and Escherichia coli O 14 K7, which are relatively lipophilic, showed greater association than S. typhimurium 395 MS and E. coli O 111 K58, which are more hydrophilic. Prolonged incubation of bacteria with the length of intestine in vitro leading to damage of the brush border of the mucosal epithelium enhanced the association of the bacteria. These data suggest that similar physico-chemical surface properies govern the association certain enterobacteria to the intestinal mucosa as in phagocytosis with professional phagocytes.

Acetylglucosaminidase↗
PubMed1977

Surface-charge characteristics of smooth and rough Salmonella typhimurium bacteria determined by aqueous two-phase partitioning and free zones electrophoresis.

Aqueous biphasic partitioning of Salmonella typhimurium S and R bacteria in a system containing 6.2 per cent (w/w) dextran 500 and 4.4 per cent (w/w) poly(ethyleneglycol) 6000 (PEG) was similar to the partition of the corresponding surface lipopolysaccharide (LPS). Further partition analysis with charged PEG showed that S bacteria and their LPS exposed very little charge, whereas R bacteria and their LPS showed a conspicuous negative charge at neutral pH. Free zone electrophoresis also indicated that the S bacteria have a much lower surface charge density than the R bacteria and accordingly a different surface structure. Thus, the physico-chemical properties of the bacterial surface seem to be determined to a great extent by the characteristics of the cell surface LPS.

Cell Wall↗
PubMed1977

Liability to hydrophobic and charge interaction of smooth Salmonella typhimurium 395 MS sensitized with anti-MS immunoglobulin G and complement.

Sensitization of smooth Salmonella typhimurium 395 MS bacteria with hyper-immune anti-MS immunoglobulin G (IgG) antibodies increased the liability to hydrophobic interaction as assessed by the affinity for a column of Octyl-Sepharose. After sensitization, the material originally eluted with 1 M (NH4)SO4 in a 0.01 M phosphate buffer (pH 6.8) was not desorbed until the ionic strength was reduced to nil, and 0.1% (vol/vol) Triton X-100 in the 0.01 M phosphate buffer was used as eluant. Furthermore, by including positively charged bis-trimethylamino-polyethylene glycol (PEG) or negatively charged bis-sulfoamino-PEG in an aqueous two-phase system of dextran T500 and PEG 6000, the partition of the IgG-sensitized bacteria was affected by either of the polymers, whereas that of the parent bacteria was not. The hydrophobic effect of IgG binding was enhanced by complement. With heat-inactivated complement, the effect of IgG was diminished. The F(ab')2 fragment showed a much lower capacity to promote a hydrophobic interaction than the complete IgG molecule.

Antibodies, Bacterial↗
PubMed1977

Physiochemical consequences of opsonization of Salmonella typhimurium with hyperimmune IgG and complement.

Partition in an aqueous, two-polymer phase system containing dextran and polyethylene glycol was employed to investigate the physico-chemical changes inflicted upon the cell surface of a smooth strain of Salmonella typhimurium by the binding of antibody IgG and complement. The minimum antibody concentration for increased phagocytosis in vitro was approximately the same as that for a significant change in two-phase partition, ca 8000 mol/bacterium, whereas a lower concentration, less than 4000 mol/bacterium, was sufficient to increase clearance in vivo. After pepsin digestion of IgG, larger quantities, ca 35,000 mol/bacterium, was required for opsonization and to influence two-phase partition. Addition of normal rabbit or guinea-pig serum to bacteria sensitized with a low concentration of antibody IgG conspicuously enhanced phagocytosis and affinity for the dextran-rich phase. The results show that binding of 8000 IgG antibody molecules or more to smooth S. typhimurium generates physicochemical changes of the bacterial surface which from studies on S leads to R mutations are known to correlate with hydrophobicity, negative charge and phagocytosis. Such results support the view that one important function of IgG antibody and complement is to decrease the hydrophilic properties of the bacteria which is thought to be a prerequisite for phagocytosis.

Binding Sites, Antibody↗
PubMed1977

Physicochemical consequences of opsonization: perturbation of liposomal membranes by Salmonella typhimurium 395 MS opsonized with IgG antibodies.

When phagocytosis-resistant Salmonella typhimurium 395 MS bacteria sensitized with anti-MS IgG antibodies were incubated with liposomes composed of phosphatidylcholine, cholesterol, and dicetylphosphate, a previously sequestered liposomal marker (4-methylumbelliferylphosphate) was released. Unsensitized or F(ab')2-sensitized bacteria had no such effect. This perturbation was neither dependent upon negatively charged dicetylphosphate nor upon cholesterol. It was further evident that palmitoyl-poly(ethyleneglycol) caused release of the trapped marker in a similar way as sensitized bacteria. These findings demonstrate a similarity between sensitized bacteria and a hydrophobic probe and lend support to the hypothesis that the perturbation was brought about by hydrophobic interaction. The observations indicate that liposomes, like phagocytes, possess "receptor sites" for the activated part of IgG and raise the possibility that phagocytic effectors can operate in a relatively nonspecific manner.

Antibodies, Bacterial↗
PubMed1976

On the mediation inflammatory reaction in the human gallbladder epithelium.

Human gallbladder epithelium was homogenized with a view to maintaining the integrity of subcellular components. In such homogenates, N-acetyl-beta-glucosaminidase, beta-glucuronidase, beta-galactosidase, beta-glucosidase, beta-fucosidase, beta-xylosidase, and acid phosphatase were demonstrated together with phospholipase activity. All the enzymes exhibited structure-linked latency. After discarding cellular debris from the homogenate, remaining subcellular organelles were analytically separated by density gradient centrifugation. After 100,000 g for 1 hour, particles containing acid glycosidases were recovered at a sucrose density of 1.18-1.19, whereas the mitochondrial marker enzyme succinate-reductase accumulated at a density of 1.16. The bulk of sedimentable phospholipase activity was recovered with particles sedimenting at 1.18-1.19. The results are interpreted as indicating that phosphalipase is present in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, in lysosomes of the human gallbladder epithelium. Release of acid hydrolases, particularly phospholipase A, from the gallbladder epithelium is discussed as mediation of an inflammatory reaction in the gallbladder, i.e. cholecystitis.

Acetylglucosaminidase↗
PubMed1976

Rapidly progressive glomerulonephritis with antibodies against glomerular basement membranes in serum and kidneys.

Four cases of rapidly progressive glomerulonephritis with similar clinical courses are presented. Examination of kidney biopsies from these patients showed severe glomerulitis with capillary necrosis, fibrin thrombi and interstitial inflammation but no vasculitis. Electron microscopy showed wrinkled capillary basement membranes which were irregularly thickened, homogenous and had an irregular fibrillar structure. No localized deposits were observed. Immunohistological examination demonstrated linear and diffuse deposition of IgG and C3 along glomerular basement membranes. Nephrectomized kidneys from these patients were eluted and shown to contain antibodies against glomerular basement membrane. These antibodies were also present in sera of three of the patients.

Adolescent↗