Search PubMed⌕ Search

Biomedical subjects

N Garber

Publications and source records attributed to N Garber.

At least 19 recordsLinked to original sources
PubMed1994

An examination of alveolar stop retraction during pacifier use.

Employing a single subject A-B-A experimental design, a four year old female with normal articulation and a history of pacifier use was observed to demonstrate alveolar stop retraction more than fifty percent of the time while using her orthodontic device. Contextual factors appeared to have played a role in this variability. Upon confirming this phenomenon in the four year old subject, a follow-up investigation was undertaken with seven children between the ages of three and five years. All subjects had age appropriate articulation skills with no evidence of alveolar stop retraction without the pacifier in place and only rarely with the pacifier in place (.85%). Implications of these findings and the need for further research are discussed.

Articulation Disorders↗
PubMed1992

On the specificity of the D-galactose-binding lectin (PA-I) of Pseudomonas aeruginosa and its strong binding to hydrophobic derivatives of D-galactose and thiogalactose.

The D-galactose-binding lectin (PA-I) from the bacterium Pseudomonas aeruginosa, isolated by affinity chromatography on Sepharose, was examined for its relative affinities for simple sugars and their derivatives using equilibrium dialysis and hemagglutination inhibition tests. The lectin, which was found to bind 0.68 mol of D-galactose per subunit of 12.8 kDa, exhibited an association constant (Ka) of 3.4 x 10(4) M-1 for D-galactose and higher affinities for hydrophobic and thio derivatives of D-galactose (with highest affinity for the hydrophobic thio derivatives). alpha-Methyl-galactoside was a stronger inhibitor than the beta-methyl derivative and alpha-lactose was a weak inhibitor but the hydrophobic phenylated derivatives of the beta-configuration of D-galactose were more potent inhibitors than the respective alpha-galactosides.

Galactose↗
PubMed1990

Rett syndrome: a longitudinal developmental case report.

Rett syndrome is a recently described progressive neurological disorder of unknown etiology occurring only in females, causing severe to profound mental retardation and characterized by loss of purposeful hand use and stereotypic hand movements. The present study examined development in five areas: gross motor skills, fine motor skills, self-help skills, communication, and cognition. Results indicated a general stagnation in all developmental areas beginning at approximately 15 months. No skills progressed beyond the 2-year level; this, despite several years of intensive, interdisciplinary intervention. Cognitive and communication skills regressed, then stabilized for several years, and subsequently began further regression. Gross motor and self-help skills appear to be areas of relative strength.

Activities of Daily Living↗
PubMed1989

Microbial lectin cofunction with lytic activities as a model for a general basic lectin role.

Lectins are ubiquitous proteins, which exhibit a specific and reversible sugar-binding activity. They react with glycosylated macromolecules and cells and may coaggragate them and lead to their lysis or alterations. Various lectin biological effects are well known, but their basic biological function is considered as yet unknown. In the present review, an experimental evidence and theoretical considerations are forwarded for supporting our suggestion that the general basic lectin or lectinoid (lectin-like protein) function in microorganisms, plants and animals is a cofunction enabling the activities of key lytic enzymes (lysins: glycosidases, proteases, esterases, phosphatases, hemolysin, etc.). The lectin service is: homing onto glycosylated receptors, anchoring to them and induction of cooperative conformational effects which enable their counterpart lysin activity on exogenous or endogenous target molecules and cells. The 'lectin-lysin' pair may reside in the same molecule, or in linked subunits. It may also be formed by cofunction of two separate entities originating from one or two (homogenous or heterogenous) cell sources. The lectin and lysin may be free or cell-bound components located intra or extracellularly. The final result of their cofunction is practically irreversible; either cell and macro-molecule lysis for nutrition, homeostasis and protection or cell alteration, reorganization and new productivity. Our suggestion emphasizes the prominent analogy of lectins to lytic enzyme positioning sites (LEPS), immunoglobulins and polypeptide hormones. The lectin analogy to LEPS and immunoglobulins is exhibited in the lectin-dependent cell and macromolecule lysis for nutritional and homeostatic purposes or for protection, respectively. The hormone-like lectin activity is exhibited in the lectin-dependent cell alterations. In addition to similar functions and effects, the analogy also includes the properties and behavior of these proteins. The suggested hypothesis is based on experimental evidence from microorganisms, plants and animals. It envisions the lectin and lectinoid function in cell attacks on glycosylated molecules or cells, cell-substratum and cell-cell interactions (fusion, invasion, etc.), cell transformation and formation of special structures. All of them according to a developmental program, or special (especially unfavourable) environmental conditions. The lectin resistance to proteolysis and unfavourable pH or temperature is in accord with the suggested hypothesis.

Animals↗
PubMed1987

Surface haemagglutinating activity of Pseudomonas aeruginosa.

Intact cells of several strains of Pseudomonas aeruginosa agglutinate papain-treated human erythrocytes. The agglutinating activity appears to reside in the surface layers of the bacterium-Pseudomonas surface haemagglutinin. This activity does not correlate with the existence of the internal PA-I and PA-II lectins, the presence of fimbriae or adherence to human buccal epithelial cells. Disruption of the bacterial cells by sonication abolishes their haemagglutinating activity. The intact cells of P. aeruginosa are also able to agglutinate rabbit, chicken, dog, guinea pig and sheep erythrocytes. This activity is generally higher with papain-treated erythrocytes, except those of rabbit in which lower haemagglutinating activity is observed after papain treatment. Optimal conditions for the haemagglutination are 37 degrees C and pH 6-7. Simple sugars do not inhibit, while fetuin and hydrophobic amino acids inhibit this activity. Exposure of the bacterial cells to proteolytic enzymes, EDTA or denaturating conditions abolish the haemagglutinating activity. These results indicate that the surface haemagglutinin is a protein which agglutinates red blood cells via hydrophobic interactions.

Amino Acids↗
PubMed1985

Intractable postphlebitic ulceration of the leg.

A new regimen for the successful treatment of intractable postphlebitic ulceration of the leg is described. It is based on preliminary culture of organisms in the ulcers followed by sensitivity tests to ascertain the appropriate antibiotics or antibacterials to be used. Patients with Pseudomonas infection are hospitalized and receive: intramuscular injections of amikacin sulphate 500 mg twice daily for 7 days; a once-daily spraying of antibiotic powder on the ulcer for 7 days; and a topical gentian violet regimen once daily for a further 2 days to encourage adhesion of a dressing to the ulcer bed. After discharge the patients are treated in the consulting rooms. Ulcers without Pseudomonas infection but from which organisms have been cultured are treated in the consulting rooms with drugs indicated by the results of sensitivity tests, and topical gentian violet. Patients from whom organisms have not been cultured are treated with co-trimoxazole and topical gentian violet. Patients are taught correct bandaging of the calf with a 150 mm wide crêpe bandage and a Rowden Foote elastic bandage. Firm bandaging prevents calf oedema, the factor predisposing to ulceration. Patients are initially seen daily and then, as the dressing becomes adherent, at decreasing intervals until it is shed. Both bandages are worn until the affected tissues heal. The patient is then fitted with a below-knee heavy-duty elastic stocking.

Adult↗
PubMed1985

Effects of growth phase and boiling of enteropathogenic Escherichia coli strains on their interaction with Pseudomonas aeruginosa lectins.

Escherichia coli strains from' serotypes O86, 0128 and O111 varied in their reactivity with Pseudomonas aeruginose lectins (PA-I with D-galactose specificity and PA-II which binds L-fucose, D-mannose, L-galactose and D-fructose). Generally, cells of O86 strains were agglutinated by PA-I, but not by PA-II, and those of O128 serotype were agglutinated by PA-II, and not by PA-I. Adsorption tests showed that cells of E. coli O86 strains adsorb PA-I to a greater extent than PA-II, while most E. coli O128 strains adsorbed higher amounts of PA-II. Cells of E. coli O111B4 which were not agglutinated by either Pseudomonas lectin could still adsorb both. Boiling of O86 and O128 cells frequently enhanced their agglutinability as well as their lectin adsorption capacity. The agglutinability enhancement was somewhat more prominent in boiled stationary phase cells than in log phase cells probably due to late synthesis of the O antigen components concomitantly with the heat-sensitive components (K antigens) which masked them. PA-I agglutinating activity was inhibited by the lipopolysaccharide (LPS) extracted from E. coli O86 cells, while PA-II was inhibited by the LPS extracted from E. coli O128 cells. These findings indicate that the receptors to the Pseudomonas lectins probably reside in the terminal part of the O-specific-polysaccharide of the LPSs of these bacteria.

Carbohydrate Conformation↗
PubMed1983

The intracellular localization of Pseudomonas aeruginosa lectins.

The localization of the Pseudomonas aeruginosa lectins (PA-I and PA-II) was studied using methods of osmotic shock, freezing and thawing and spheroplast formation. Very slight release of the two lectins occurred when P. aeruginosa was exposed to magnesium-osmotic shock or was frozen and thawed. Under these conditions, release of the periplasmic 5'-nucleotidase occurred, whereas no release of cytoplasmic glucose-6-phosphate dehydrogenase activity was detected. Formation of spheroplasts from P. aeruginosa by gradual removal of the bacterial envelopes revealed low lectin activity in the treatment fluids. Osmotic shock treatment of the lysozyme treated mureinoplasts resulted in low release of glucose-6-phosphate dehydrogenase and the two lectins (10-13%) and a considerable activity (38.4%) of 5'-nucleotidase. The presence of the lectins on the outer and the cytoplasmic membranes enabled intact cells and spheroplasts of P. aeruginosa to agglutinate papain-treated human erythrocytes. These results indicate that the two lectins are located mainly in the cytoplasm with small fractions on the cytoplasmic and outer membranes and in the periplasmic space.

5'-Nucleotidase↗
PubMed1981

A therapeutic approach to postphlebitic ulceration.

In recent years I have used a conservative regimen as an office procedure for healing postphlebitic ulceration. The regimen--oral antibiotics, oral zinc sulphate, topical gentian violet solution, sterile Telfa dressings, a synthetic sponge pressure pad, support of the lower leg by a Rowden Foote elastic bandage--led to complete resolution of the lesions except where infection with Pseudomonas was present. Even then healing was achieved, although it entailed repeated and prolonged intravenous administration of sodium carbenicillin and admission to hospital. Of 28 patients treated all were healed, 2 after Pseudomonas had been eradicated.

Diagnosis, Differential↗
PubMed1981

Interactions of Pseudomonas aeruginosa lectins with Escherichia coli strains bearing blood group determinants.

Pseudomonas aeruginosa lectins interact with Escherichia coli strains O86B7 and O128B12, which possess B and H (O) blood group determinants, respectively. The interaction could be demonstrated by specific agglutination of the bacteria, by haemagglutination inhibition tests and by lectin-mediated peroxidase binding to the bacteria. The agglutination of E. coli O86B7 by the Pseudomonas galactose-binding lectin was inhibited by D-galactose and by the lipopolysaccharide extracted from E. coli O86B7. Similarly, the specific agglutination of E. coli O128B12 by the Pseudomonas mannose-binding lectin (which also binds L-fucose, L-galactose and D-fructose) was inhibited by D-mannose, L-fucose, L-galactose and D-fructose, as well as by athe lipopolysaccharide extracted from E. coli O128B12. The interaction between E. coli O128B12 and the Pseudomonas mannose-binding lectin was also demonstrated by lectin-mediated peroxidase binding to the bacterial surface. Peroxidase binding was also inhibited by the above-mentioned sugars and E. coli O128B12 lipopolysaccharide. Treatment of cells of the two E. coli strains with protein-denaturing agents did not reduce their agglutination by the Pseudomonas lectins. On the other hand, oxidation of the cell surface sugars by sodium metaperiodate or boiling the cells in the presence of 1% acetic acid for 1 h abolished their agglutination by the two lectins. It is, therefore, suggested that the Pseudomonas lectins interact with the B and H (O) blood group determinant sugars (D-galactose in E. coli O86B7 and L-fucose in E. coli O128B12) residing in the lipopolysaccharides of these E. coli strains.

ABO Blood-Group System↗
PubMed1981

Lectin-bearing protoplasts of Pseudomonas aeruginosa induce capping in human peripheral blood lymphocytes.

The redistribution of surface membrane receptors and cap formation by pseudomonas aeruginosa lectins (Ps-GAL, which binds D-galactose, and Ps-MAN, which binds D-mannose and L-fucose) was studied in human peripheral blood lymphocytes by scanning electron microscopy. When Ps-GAL and Ps-MAN-bearing protoplasts of Pseudomonas aeruginosa were incubated with lymphocytes, cap formation was revealed by the accumulation of protoplasts at one pole of the lymphocyte. No adherence or capping was observed when intact Pseudomonas aeruginosa cells were used. Pretreatment of the lymphocytes by papain or neuraminidase did not enhance the capping. No capping or adherence of protoplasts to lymphocytes was observed in the presence of D-galactose, while addition of D-mannose had no effect. The inhibitory effect of D-galactose on the adherence and capping in human peripheral lymphocytes by Pseudomonas aeruginosa protoplasts suggests that the Ps-GAL lectin is responsible for both phenomena.

Galectins↗
PubMed1980

Localization of cholinesterase in Pseudomonas aeruginosa strain K.

The inducible cholinesterase of Pseudomonas aeruginosa strain K (ATCC 25102) degraded propionylcholine, acetylthiocholine, acetylcholine and acetyl-beta-methylcholine at a high rate and butyrylcholine and succinylcholine at very low rates. The localization of the enzyme in the periplasmic space was indicated by a similar rate of acetylcholine degradation by intact cells or their extracts, by release of cholinesterase together with alkaline phosphatase into the culture medium during cell growth in a low phosphate-containing medium, by liberation of cholinesterase and alkaline phosphatase during lysozyme-induced conversion of cells to spheroplasts and by freezing and thawing. Threatment of cells with diazo-7-amino-1,3-naphthalenedisulphonic acid, which inactivates surface-located enzymes, abolished most of the cholinesterase and 5'-nucleotidase activities.

Alkaline Phosphatase↗
PubMed1977

Mannose-binding hemagglutinins in extracts of Pseudomonas aeruginosa.

Mannose-binding hemagglutinins were found in the extracts of a pyocyanin-forming Pseudomonas aeruginosa, which contain galactose-specific hemagglutinins. They were purified simultaneously with the latter proteins by heating to 70 degrees C, precipitating with ammonium sulfate, application to a Sepharose 4B column, and elution from it by 0.05 M mannose. The mannose-specific hemagglutinins were shown to be similar to the galactophilic ones in (a) being glycoproteins of very low molecular weight (about 11 000 by SDS gel electrophoresis), (b) their tendency to aggregate, and (c) their ability to effect stronger agglutination of erythrocytes treated with papain than of untreated ones. They were found to resemble them also in their reaction with simple sugars and interactions with divalent cations, which are essential for their activity. In these properties, as well as in their relative resistance to heat and to proteolytic enzymes, these two types of bacterial hemagglutinins are like most of the plant, contrasted with the animal, hemagglutinins. The reactions with mannose and mannose-bearing compounds (yeast mannan, horseradish peroxidase (EC 1.11.1.7), and serum globulins), which are not shared with the galactophilic Pseudomonas hemagglutinins, indicate a relationship of the mannose-binding protein of Pseudomonas to the plant lectin concanavalin A. The mannose-binding hemagglutinins do not exhibit identical cell-agglutinating spectra owing to difference in profiles of sugar specificity and relative affinity to mannose derivatives compared with free mannose.

Agglutinins↗