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Biomedical subjects

A Weintraub

Publications and source records attributed to A Weintraub.

At least 109 records · Page 6Linked to original sources

Real-time intracardiac two-dimensional echocardiography: an experimental study of in vivo feasibility, imaging planes, and echocardiographic anatomy.

The traditional transthoracic and transesophageal echocardiographic examination have proven to be useful imaging tools for studying cardiac morphology, pathology, and function. Recently, catheter-based ultrasound transducers have been available for intravascular ultrasonic imaging. We supposed that echocardiographic examination performed from within the heart itself can provide useful information about cardiac structure and function, especially in settings where transthoracic or transesophageal echocardiography may be technically difficult to perform or poorly tolerated by the patient. To explore this concept, we performed intracardiac echocardiography in vivo in 22 dogs using both 5-MHz and 20-MHz transducers. High-quality images were obtained in all animals. Using the higher frequency transducer, detailed images with only a limited depth of field were obtained. With the 5-MHz transducer, a comprehensive cardiac examination was feasible from within the right atrium and inferior vena cava. We were able to visualize the great vessels, all cardiac valves, and cardiac chambers in a multitude of imaging planes. Alterations in ventricular function were instantly recognized. Color Doppler capabilities allowed visualization of flow abnormalities as well. We conclude that intracardiac echocardiography is feasible and could be potentially useful in certain clinical situations. With further research and development, this technique may have an important clinical impact in cardiac therapy and diagnosis.

Animals↗

Intracardiac, intravascular, two-dimensional, high-frequency ultrasound imaging of pulmonary artery and its branches in humans and animals.

Intravascular ultrasound imaging is a promising new method for assessing vascular morphology. We evaluated the capability of intravascular ultrasound to quantify pulmonary artery (PA) morphology in vitro and explored the feasibility of in vivo PA imaging in animals and humans. In the in vitro study of 15 PA segments, we used a 20-MHz prototype ultrasound catheter. Intravascular ultrasound (y) provided crisp images of PA segments and demonstrated excellent correlations with anatomic measurements (x) in the estimation of luminal area (y = 0.89x + 2.95, r = 0.99, p less than 0.001), luminal diameter (n = 30, y = 0.79x + 0.96, r = 0.92, p less than 0.001), and vessel wall thickness (n = 60, y = 0.65x + 0.33, r = 0.85, p less than 0.001). We subsequently introduced the probe into the PA of 10 dogs and were able to obtain real-time, two-dimensional images of the main PA, its major branches, and farther smaller branches as far as the wedge level. To evaluate the in vivo feasibility of PA imaging in conscious humans, we used a commercially available, 20-MHz intravascular ultrasound (IVUS) catheter in 22 subjects through a femoral or jugular venous sheath at the end of standard diagnostic cardiac catheterization. In 20 subjects, we acquired dynamic, high-resolution, cross-sectional images of the proximal and distal PA. Changes in shape and decreasing luminal area could be clearly recognized as the IVUS catheter reached branching points and as it passed more distally. There were no complications.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗

Human endothelial cell adhesiveness for neutrophils, induced by Escherichia coli lipopolysaccharide in vitro, is inhibited by Bacteroides fragilis lipopolysaccharide.

Recent studies in vitro have demonstrated that LPS from Gram-negative bacteria are capable of inducing endothelial cells to express a cell surface property that promotes the adherence of neutrophils (polymorphonuclear cells, PMN). We have investigated the effects of LPS from Bacteroides fragilis, an organism documented to have little toxicity in vivo, on the induction of this property in human endothelial cells. Monolayers of cultured human umbilical vein endothelial cells (HUVE) exhibited no increase in adhesiveness for 51Cr-radiolabeled PMN after 4 h of exposure to B. fragilis LPS from 1 ng to 10 micrograms/ml. Escherichia coli LPS elicited a dose-dependent enhancement of HUVE adhesiveness for PMN over the same concentration range, reaching a maximum of 49.4 +/- 6.6% at 10 micrograms/ml. Like E. coli LPS, B. fragilis LPS converted chromogenic substrate in the Limulus amebocyte lysate assay, and was directly cytotoxic to bovine aortic endothelial cells. Both B. fragilis LPS activities required doses two-to-three log-fold higher than for E. coli LPS. In addition, we found that B. fragilis LPS inhibited the induction of HUVE adhesiveness for PMN by E. coli LPS. This inhibition was also dose-dependent, becoming maximal (greater than 80%) when B. fragilis LPS was in 10- to 20-fold excess. Tumor necrosis factor and IL-1, two monokines which also elicit HUVE adhesiveness for PMN, were not inhibited by B. fragilis LPS, suggesting a mechanism of HUVE activation by LPS which is signal-specific, and which recognizes specificities of LPS structure.

Bacteroides fragilis↗

Structural characterization of the lipid A component of Bacteroides fragilis strain NCTC 9343 lipopolysaccharide.

The chemical structure of Bacteroides fragilis NCTC 9343 lipid A was characterized by using conventional chemical procedures, methylation analysis, and laser desorption mass spectrometry. It was found that B. fragilis lipid A consists of a beta-D-glucosaminyl-(1-6)-D-glucosaminyl-1-O-phosphate backbone whose hydroxyl groups in positions 4, 4' and 6' are free, the latter serving as the attachment site for the polysaccharide component in lipopolysaccharide. This backbone molecule carries up to of five molecules of ester- and amide-bound long chain non-hydroxylated and (R)-3-hydroxy fatty acids. With regard to the distribution on the fatty acids on the lipid A backbone, a considerable heterogeneity was revealed by laser desorption mass spectrometry. Despite this heterogeneity, a major species of B. fragilis lipid A could be defined in which the hydroxyl group at position 3' of the distal GlcN carries (R)-3-hydroxyhexadecanoic acid and the hydroxyl group at position 3 of the reducing GlcN is acylated by (R)-3-hydroxypentadecanoic acid. The amino group of the distal GlcN residue carries (R)-3-(13-methyltetradecanoyloxy)-15-methylhexadecanoic acid and that of the reducing GlcN group (R)-3-hydroxyhexadecanoic acid. The absence of ester-bound phosphate and ester-linked 3-acyloxyacyl groups, the presence of not more than five acyl residues and the predominance of fatty acids possessing 15-17 carbon atoms are unique features of B. fragilis lipid A which differentiate it from enterobacterial and other lipids A and which are likely to be related to its low endotoxic activity.

Acylation↗

Computed tomography of lumbar apophyseal joint lipoma: report of three cases.

The authors report three cases of lumbar apophyseal joint lipoma located at the L4/L5 or L5/S1 level. CT scan makes the diagnosis easily possible; indeed erosive changes with enlargement of the upper portion of the lumbar articular joint and anterior displacement of the top of the superior facet are associated with intra-articular fatty densities. Clinical symptoms are rarely encountered and may be related to narrowing of the upper portion of the intervertebral foramen.

Adult↗

Phenytoin induces interleukin-1 production in vitro.

Human adherent mononuclear cells and subcloned cell lines established from the human histiocytic cell line U-937 were cultured with phenytoin (PHT) and/or lipopolysaccharide (LPS) purified from Bacteroides fragilis. After the cultivation period, the cell-free supernatants were tested for interleukin-1 (Il-1) activity. The results showed that PHT induces Il-1 activity and potentiates LPS-induced Il-1 production. In the monocytic cell line U-937, the induced Il-1 production was found to be clonally distributed indicating that the response to PHT may be exerted by a subpopulation of monocytes. The PHT-induced Il-1 activity may be of importance in the development of gingival overgrowth. The induced Il-1 could also contribute to other known side effects such as dermatologic reactions accompanied by transient fever seen in patients medicating the drug.

Adult↗

Characterization of the common immunodominant antigenic determinant in the lipopolysaccharide of Bacteroides fragilis by a monoclonal antibody.

The target determinant of a monoclonal antibody (MoAb) to Bacteroides fragilis lipopolysaccharide (LPS) was characterized by inhibition enzyme immunoassay (EIA), immunoblotting (IB), immunofluorescence technique (IF) and electron immunocytochemical (EIC) technique. The MoAb has been shown to react positively with 96% of B. fragilis isolates. LPS preparations from 14 different B. fragilis strains were tested by EIA and IB. Two LPS preparations did not react in any of the tests. In both preparations the D-galactose was either lacking or present in low amount compared with the other LPSs. In addition, inhibition experiments with synthetic disaccharides confirmed that the target determinant is composed of beta-1,6-linked galactose disaccharide. EIC showed that the target of the LPS-MoAb is located on the surface of the outer membrane. These results show that the galactose chain present in LPS isolated from most B. fragilis strains contains the immunodominant antigenic determinant.

Antibodies, Bacterial↗

New attachment in monkeys with experimental periodontitis with and without removal of the cementum.

Experimental periodontitis was induced in monkeys by means of elastic orthodontic ligatures. The periodontally-involved teeth were then treated with different methods. At the end of the treatment period, the monkeys were sacrificed. The premolar-molar areas were dissected out and embedded in a low-viscosity embedding medium (Spurr). The results of the treatment procedures were analyzed on ground sections. Formation of new cementum and new bone was determined by means of tetracycline labeling. Root planing with an ultrasonic device or with hand instruments almost completely removed the cementum and a portion of the peripheral dentin. The root surface was more uneven after treatment with the ultrasonic device than after using hand instruments. No new attachment could be found after root planing. Cleaning of the periodontally-involved root surfaces with two detergents (cetylpyrimidinium chloride and sodium-N-lauroyl sarcosine) without root planing resulted in a significant amount of new attachment.

Animals↗

Structural studies of the polysaccharide part of the cell wall lipopolysaccharide from Bacteroides fragilis NCTC 9343.

The structure of the polysaccharide part of the lipopolysaccharide from Bacteroides fragilis NCTC 9343 has been determined using sugar and methylation analysis as the principal tools. Phenol--water extraction followed by a phenol--chloroform--light petroleum extraction yielded a lipopolysaccharide suitable for structural analysis. Analysis of sugars using alditol acetates showed that the polysaccharide contained L-rhamnose, D-galactose and D-glucose in the approximate molar ratios of 1:5:1. After weak acid hydrolysis, two polysaccharide fractions were isolated by gel permeation chromatography: PSI and PSII with the sugar molar ratios 1:5:1 and 1:2:1 respectively. Chromium trioxide oxidation revealed that all galactosyl residues have the beta configuration, and that the rhamnosyl and glucosyl residues have the alpha configuration. From methylation analysis of lipopolysaccharide and the PS I and PS II fractions the following structures could be deduced.

Bacteroides fragilis↗

Chemical and immunochemical analyses of Bacteroides fragilis lipopolysaccharides.

Lipopolysaccharides (LPSs) from 17 different Bacteroides fragilis strains were extracted in a two-step procedure. The first step was a hot phenol-water extraction of whole bacteria, resulting in a crude aqueous phase, which after lyophilization in a second step was extracted with a phenol-chloroform-light petroleum mixture. The resulting LPSs, which were essentially free from contaminating nucleic acid, proteins, and capsular polysaccharide, were investigated for their qualitative and quantitative sugar and fatty acid composition, immunochemical specificity by enzyme-linked immunosorbent inhibition assays, and particle weight by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Of the 17 strains, 13 had LPSs which all contained L-rhamnose, D-glucose, D-galactose, and D-glucosamine in approximately the same ratio. Three of these LPSs also contained D-galactosamine. The fatty acid composition was also similar in that the same fatty acids, although in slightly varying proportions, were found in all LPSs. The 13 strains also showed the same specificity in inhibition studies by enzyme immunoassay with rabbit anti-LPS antisera and LPS antigen. The LPS particle weights were also very similar, in the range of what is found for LPSs from rough mutant strains of enterobacteria. Our results suggest that most strains of B. fragilis have similar, if not identical, LPSs with relatively short polysaccharide chains.

Antigens, Bacterial↗

Encapsulation and protection against phagocytosis by Bacteroides fragilis.

The capsular polysaccharide of Bacteroides fragilis is most probably an important virulence factor as shown by its ability to protect against phagocytosis in in vitro studies, and by its abscess-promoting ability in experimental in vivo studies. Immunity against the capsular polysaccharide, either in the form of humoral antibodies or as cell-mediated immunity, can facilitate phagocytosis or prevent abscess formation. The capsular polysaccharides in two reference strains examined so far are complex in structure, and seem to be strain specific. The B. fragilis lipopolysaccharide has a relatively low endotoxic activity when compared to lipopolysaccharides from bacteria belonging to Enterobacteriaceae. Structurally the B. fragilis lipopolysaccharide has a relatively low molecular weight, and short polysaccharide chains similar to those found in lipopolysaccharides from rough mutants of Enterobacteriaceae or from capsulated bacteria such as Neisseria meningitidis and Haemophilus influenzae.

Abscess↗

Monoclonal antibodies to Bacteroides fragilis lipopolysaccharide.

Monoclonal antibodies (MoAbs) to the lipopolysaccharide (LPS) of Bacteroides fragilis were produced by immunizing mice before hybridization with bacterial outer membranes solubilized with Triton X-100. Nineteen stabile clones were established. They all produced antibodies that reacted more strongly with purified B. fragilis LPS than with crude sonicated antigen in an enzyme immunoassay. Four MoAbs were studied by immunoblotting and enzyme immunoassay inhibition. Immunoblotting confirmed that the target of the MoAbs was LPS. Marked and homogeneous staining occurred in the immunoblotting with both purified LPS and outer membranes in the molecular weight range of 8,000 to 27,000. In enzyme immunoassay inhibition, MoAbs reacted positively with 93 to 96% of B. fragilis strains, including prototype strains ATCC 23745 and NCTC 9343. Within the B. fragilis group, the MoAbs reacted positively with two of five B. ovatus strains and two to six of nine B. thetaiotaomicron strains. No marked cross-reactivity with other bacteria was observed. These results confirm earlier findings that the B. fragilis LPS contains an immunodominant antigenic determinant common to almost all B. fragilis isolates.

Animals↗

The role of immunoglobulins in amniotic fluid growth inhibition of Bacteroides fragilis, herpes simplex, coxsackie B 5 and cytomegalovirus.

In serum and amniotic fluid (AF) from 30 pregnant women, antibodies against the anaerobe Bacteroides fragilis were determined by enzyme-linked immunosorbent assay (ELISA) and the results were compared with those of previously performed tests of B. fragilis growth inhibition by AF. The neutralizing effects of serum and AF against herpes simplex virus (HSV), cytomegalovirus (CMV) and coxsackie B 5 virus were also investigated, and antibody titres were determined by ELISA. No correlation could be demonstrated between the growth-inhibitory capacity of AF and the presence of antibodies against B. fragilis in serum or AF. Neutralizing antibodies against HSV and coxsackie B 5 virus were found in 73% and 51%, respectively, of the sera and in 36% and 13%, respectively, of both serum and corresponding AF. In no case could an AF neutralizing effect upon HSV, coxsackie B5 or CMV be demonstrated without a corresponding positive serum neutralization. It is concluded that the growth-inhibitory effect of AF on viruses in antibody-mediated, while AF inhibition of B. fragilis, and possibly other bacteria as well, seems to depend upon other antimicrobial mechanisms.

Amniotic Fluid↗

Capsular polysaccharides and lipopolysaccharides from two Bacteroides fragilis reference strains: chemical and immunochemical characterization.

Fermentor growth of Bacteroides fragilis under controlled conditions in a complex medium containing 1% glucose and 10% fetal calf serum resulted in high yields of bacteria. After hot phenol-water extraction of the organisms, capsular polysaccharide was isolated from the aqueous phase and purified by Sephacryl S-300 chromatography in a buffer with 3% sodium deoxycholate. Lipopolysaccharide was isolated by phenol-chloroform-light petroleum ether extraction. The capsular polysaccharide from B. fragilis strain NCTC 9343 contained six sugars: L-fucose, D-galactose, D- and L-quinovosamine, D-glucosamine, and galacturonic acid. The capsule of strain ATCC 23745 also contained D-glucose, L-fucosamine, L-rhamnosamine, and a 3-amino-3,6-dideoxyhexose but lacked D-quinovosamine. The latter capsule also contained alanine (4%). The capsular polysaccharides were different immunochemically by ELISA inhibition. The lipopolysaccharide of both strains contained the same sugars (L-rhamnose, D-glucose, D-galactose, and D-glucosamine) and fatty acids (13-methyl-tetradecanoic and 3-hydroxy-hexadecanoic and 3-hydroxy-15 methyl-hexadecanoic as major constituents) and were identical by ELISA inhibition.

Amino Acids↗