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Biomedical subjects

M Reith

Publications and source records attributed to M Reith.

At least 19 recordsLinked to original sources
PubMed2003

Molecular characterization and quantitative analysis of superoxide dismutases in virulent and avirulent strains of Aeromonas salmonicida subsp. salmonicida.

Aeromonas salmonicida subsp. salmonicida is a facultatively intracellular gram-negative bacterium that is the etiological agent of furunculosis, a bacterial septicemia of salmonids that causes significant economic loss to the salmon farming industry. The mechanisms by which A. salmonicida evades intracellular killing may be relevant in understanding virulence and the eventual design of appropriate treatment strategies for furunculosis. We have identified two open reading frames (ORFs) and related upstream sequences that code for two putative superoxide dismutases (SODs), sodA and sodB. The sodA gene encoded a protein of 204 amino acids with a molecular mass of approximately 23.0 kDa (SodA) that had high similarity to other prokaryotic Mn-SODs. The sodB gene encoded a protein of 194 amino acids with a molecular mass of approximately 22.3 kDa that had high similarity to other prokaryotic Fe-SODs. Two enzymes with activities consistent with both these ORFs were identified by inhibition of O(2)(-)-catalyzed tetrazolium salt reduction in both gels and microtiter plate assays. The two enzymes differed in their expression patterns in in vivo- and in vitro-cultured bacteria. The regulatory sequences upstream of putative sodA were consistent with these differences. We could not identify other SOD isozymes such as sodC either functionally or through data mining. Levels of SOD were significantly higher in virulent than in avirulent strains of A. salmonicida subsp. salmonicida strain A449 when cultured in vitro and in vivo.

Aeromonas↗
PubMed2001

The highly reduced genome of an enslaved algal nucleus.

Chromophyte algae differ fundamentally from plants in possessing chloroplasts that contain chlorophyll c and that have a more complex bounding-membrane topology. Although chromophytes are known to be evolutionary chimaeras of a red alga and a non-photosynthetic host, which gave rise to their exceptional membrane complexity, their cell biology is poorly understood. Cryptomonads are the only chromophytes that still retain the enslaved red algal nucleus as a minute nucleomorph. Here we report complete sequences for all three nucleomorph chromosomes from the cryptomonad Guillardia theta. This tiny 551-kilobase eukaryotic genome is the most gene-dense known, with only 17 diminutive spliceosomal introns and 44 overlapping genes. Marked evolutionary compaction hundreds of millions of years ago eliminated nearly all the nucleomorph genes for metabolic functions, but left 30 for chloroplast-located proteins. To allow expression of these proteins, nucleomorphs retain hundreds of genetic-housekeeping genes. Nucleomorph DNA replication and periplastid protein synthesis require the import of many nuclear gene products across endoplasmic reticulum and periplastid membranes. The chromosomes have centromeres, but possibly only one loop domain, offering a means for studying eukaryotic chromosome replication, segregation and evolution.

Base Sequence↗
PubMed2001

Lipovitellins derived from two forms of vitellogenin are differentially processed during oocyte maturation in haddock (Melanogrammus aeglefinus).

In the process of cloning vitellogenin (Vtg) cDNAs from haddock (Melanogrammus aeglefinus), two related, but distinct, mRNAs were identified. Full-length cDNA sequences were determined for both Vtg types (Had1 and Had2), and the deduced amino acid sequences were found to be 54% identical to each other and 48-58% identical to other teleost Vtgs. To investigate the expression of the two Vtg mRNAs, proteins from prehydrated oocytes and fertilized eggs were separated on SDS-polyacrylamide gels. Only a single lipovitellin I band was detected in each sample, and the egg lipovitellin I was smaller (97 vs. 110 kDa) than the oocyte protein, indicative of proteolytic processing during oocyte hydration. Mass spectrometric (MALDI-TOFMS and tandem mass spectrometry) analyses of tryptic fragments from the haddock oocyte and egg lipovitellin I revealed that the lipovitellin I from prehydrated oocytes contained tryptic fragments that matched the sequences of both types of Vtg, suggesting that there were two proteins in this band, while the egg lipovitellin I contained tryptic fragments that only matched the Had1 cDNA sequence, indicating that the Had2 lipovitellin had been degraded during hydration. Physiological data from haddock oocytes and eggs demonstrate that, as in other marine fish that spawn pelagic eggs, the free amino acid content increases during oocyte hydration and apparently contributes to hydration by driving the osmotic uptake of water. The correlation of the disappearance of one lipovitellin I with the increase of free amino acids in the oocyte suggests that this protein is a major source of the free amino acids for oocyte hydration.

Amino Acid Sequence↗
PubMed2001

An intervention to increase quality of life and self-care self-efficacy and decrease symptoms in breast cancer patients.

This study tested effects of a nurse-administered self-efficacy intervention given on five monthly occasions and designed to enhance patients' self-care self-efficacy. The hypotheses were that at four months and eight months after beginning chemotherapy the efficacy-enhancing experimental group would have significantly higher scores on quality of life and self-care self-efficacy than the control group and significantly less symptom distress. Fifty-six women receiving chemotherapy for breast cancer were randomized to the experimental and control groups. Outcome variables were quality of life, measured by the Functional Assessment of Cancer Treatment-Breast (FACT-B), symptom distress, measured by the Symptom Distress Scale (SDS), and factors of self-care self-efficacy, measured by Strategies Used by Patients to Promote Health (SUPPH). The interaction effects for the FACT-B ranged from small for functional concerns (eta square = .03) to large for social concerns (eta square = .110); effects for the SDS were large (eta square = .140), and for factors on the SUPPH effect sizes ranged from small (eta square = .01) for Enjoying Life and Stress Reduction to medium (eta square = .089) for Coping, and large (eta square = .141) for Making Decisions. Interventions to promote self-efficacy may increase quality of life and decrease symptom distress for women diagnosed with breast cancer.

Adaptation, Psychological↗
PubMed1996

Genes encoding the same three subunits of respiratory complex II are present in the mitochondrial DNA of two phylogenetically distant eukaryotes.

Although mitochondrial DNA is known to encode a limited number (<20) of the polypeptide components of respiratory complexes I, III, IV, and V, genes for components of complex II [succinate dehydrogenase (ubiquinone); succinate:ubiquinone oxidoreductase, EC 1.3.5.1] are conspicuously lacking in mitochondrial genomes so far characterized. Here we show that the same three subunits of complex II are encoded in the mitochondrial DNA of two phylogenetically distant eukaryotes, Porphyra purpurea (a photosynthetic red alga) and Reclinomonas americana (a heterotrophic zooflagellate). These complex II genes, sdh2, sdh3, and sdh4, are homologs, respectively, of Escherichia coli sdhB, sdhC, and sdhD. In E. coli, sdhB encodes the iron-sulfur subunit of succinate dehydrogenase (SDH), whereas sdhC and sdhD specify, respectively, apocytochrome b558 and a hydrophobic 13-kDa polypeptide, which together anchor SDH to the inner mitochondrial membrane. Amino acid sequence similarities indicate that sdh2, sdh3, and sdh4 were originally encoded in the protomitochondrial genome and have subsequently been transferred to the nuclear genome in most eukaryotes. The data presented here are consistent with the view that mitochondria constitute a monophyletic lineage.

Amino Acid Sequence↗
PubMed1995

Evaluation of different preparation parameters for the production and cryopreservation of seed cultures with recombinant Saccharomyces cerevisae.

In this article we describe the intensive investigation of defined physicochemical parameters for their influence on the preparation, storage stability in liquid nitrogen, and the post-thaw productivity of a recombinant strain of Saccharomyces cerevisiae expressing the human factor XIIIa protein. Preparation of industrially sized seed cultures and their storage stability were monitored over more than a 1-year period. Major parameters recorded before and after thawing were number of colony-forming units on agar slant media, plasmid retention, and expression capacity of the recombinant protein. The viability of the cells after reconstitution of the frozen batches was found to improve significantly if a certain combination of prethaw growth conditions was applied and amino acids were included in the cryoprotectant media. In addition, the influence of different concentrations of glycerol as a cryoprotectant was investigated and the specific freezing conditions which improved the viability were identified. Even without complex freezing devices for the controlled freezing of cultures, viability rates of 85% and higher were obtained, enabling consistent production of the recombinant protein.

Amino Acids↗
PubMed1995

Metaphit amplifies long-term potentiation (LTP) in the mouse hippocampus.

The influence of metaphit, a phencyclidine derivative, on the amplitude of Long-Term Potentiation (LTP) in the mouse hippocampus was investigated. Mice (C57BL/6) of both sexes were injected with metaphit (80 mg/kg) and hippocampal slices were prepared at 3, 24, 48 hrs and 6 days following injection. The extracellular evoked potentials were recorded from the pyramidal cell layer following Schaffer collateral stimulation. The threshold value, defined as the minimum strength of the stimuli to evoke a 0.1 mV potential, was about 5 fold greater in metaphit slices than in control slices 3 hr following injection, and then declined to the control value within 6 days. The magnitude of LTP was also amplified by metaphit in a time-dependent fashion. The effect was visible three hours after injection, reached its maximum at 48 hr and then declined to a level slightly higher than control at 6 days following injection. These results demonstrate that metaphit, a compound known to induce audiogenic seizures, is able to modify synaptic plasticity in the hippocampus. Presented results are also in agreement with our previous data which demonstrated an interaction between the mechanisms of LTP and audiogenic seizure.

Animals↗
PubMed1995

Multiple drug classes and hyperosmolarity alter binding of muscarinic drugs to mesothelial cells in vitro.

Mesothelial cells in vitro exhibited binding sites for L-quinuclidinyl[phenyl-4-3H]-benzilate ([3H]-QNB), but not [3H]-N-methylscopolamine (NMS), a cell-impermeable ligand. [3H]-QNB binding demonstrated a biphasic pattern of binding in living cells: a maximum after 15 min at 37 degrees C was followed by a decrease out to 90 min. [3H]-QNB binding was blocked by increasing concentrations of atropine; WIN35428 and GBR12909, dopamine transport inhibitors also decreased binding. Pretreatment of cells for 18 hours with atropine, QNB, or WIN35428 resulted in enhanced [3H]-QNB binding, but coexposure to cycloheximide blocked this increase. Hyperosmolarity caused by NaCl or mannitol decreased binding of [3H]-QNB to living cells. Thus rabbit peritoneal mesothelial cells possess binding sites for [3H]-QNB that are influenced by other drugs and osmolarity.

Animals↗
PubMed1993

A beta-ketoacyl-acyl carrier protein synthase III gene (fabH) is encoded on the chloroplast genome of the red alga Porphyra umbilicalis.

DNA sequencing of a region of the chloroplast genome of the red alga Porphyra umbilicalis revealed an open reading frame of 326 amino acids. Databank searches indicated that this ORF is 34% identical to an E. coli gene (fabH) encoding beta-ketoacyl-carrier protein synthase III. In addition, a leucine tRNA gene (trnL(GAG)) was detected just downstream. Neither of these genes are encoded on the chloroplast genomes of land plants.

3-Oxoacyl-(Acyl-Carrier-Protein) Synthase↗
PubMed1993

Two amino-acid biosynthetic genes are encoded on the plastid genome of the red alga Porphyra umbilicalis.

To isolate the gene encoding the amino-acid biosynthetic enzyme acetolactate synthase (ALS) from the red alga Porphyra umbilicalis, PCR experiments were carried out using P. umbilicalis DNA as the template and degenerate oligonucleotides representing conserved regions of ALS amino-acid sequences. Interestingly, the PCR product (0.9 kb) hybridized exclusively to the plastid DNA of this red alga. DNA sequencing of two contiguous EcoRI plastid DNA clones revealed a 590 amino-acid open reading frame with 55 to 61% identity to cyanobacterial ALS sequences. A second gene (argB) encoding another amino-acid biosynthetic enzyme, N-acetylglutamate kinase, was identified upstream of, and on the opposite strand to the gene encoding ALS (ilvB). This is the first molecular characterization of a gene for an arginine biosynthetic enzyme from any plant. In addition, two tRNA genes, trnT(GGU) and trnY(GUA), were detected downstream from ilvB while four tRNA genes, trnfM(CAU), trnA(GGC), trnA(GGC), trnS(-GCU) and trnD(GUC), were found downstream from argB. trnA(GGC) is not found in the chloroplast genomes of land plants.

Acetolactate Synthase↗
PubMed1993

The ribosomal RNA repeats are non-identical and directly oriented in the chloroplast genome of the red alga Porphyra purpurea.

A detailed restriction map of the chloroplast genome of the red alga Porphyra purpurea has been constructed. Southern hybridization experiments with cloned or gel-purified restriction fragments and PCR products indicate that the P. purpurea chloroplast genome is approximately 188 kb in size. This circular molecule contains two rRNA-encoding repeats (approximately 4.9 kb) that separate the genome into single-copy regions of 34 kb and 144 kb. Interestingly, these repeats are arranged in a direct orientation. In addition, DNA sequencing of the ends of both repeats revealed that the two rRNA repeats are not identical. No intramolecular recombination between the repeats can be detected. We discuss the possibility that the chloroplast genome of P. purpurea is organized like that of the ancestral chloroplast.

Base Sequence↗
PubMed1991

An hsp70 homolog is encoded on the plastid genome of the red alga, Porphyra umbilicalis.

A PCR experiment using Porphyra umbilicalis DNA as the template and degenerate oligonucleotides representing conserved regions of hsp70 amino acid sequences generated a 1 kb product that hybridized exclusively to the plastid DNA of this red alga. DNA sequencing of two contiguous EcoRI plastid DNA clones revealed a 620 amino acid open reading frame with 71% identity to the dnaK gene of the cyanobacterium, Synechocystis 6803. Northern hybridization experiments detected a 2.3 kb transcript that is present in control (15 degrees C) cultures and increases approximately 7-fold upon heat shock (75 minutes at 30 degrees C).

Amino Acid Sequence↗
PubMed1990

Localization of beta-phycoerythrin to the thylakoid lumen of Cryptomonas phi does not involve a signal peptide.

Recent investigations have shown that, in cryptomonads, the phycobiliproteins are located within the thylakoid lumen rather than on the stromal side of this membrane as found in cyanobacteria and red algae. To examine possible mechanisms involved in targeting this protein to the thylakoid lumen, the plastid-encoded cpeB gene from Cryptomonas phi was sequenced. This gene encodes an open reading frame of 177 amino acids that is highly similar to known beta-phycoerythrin proteins. cpeB is expressed as a monocistronic transcript of approximately 680 bases. The genes for the alpha subunits of phycoerythrin are not co-transcribed with cpeB nor located anywhere near it. No evidence of amino- or carboxy-terminal extensions or interior modifications involved in directing the Cryptomonas beta-phycoerythrin into the lumen of the thylakoid could be detected. These data suggest that a novel mechanism may be involved in directing cryptomonad biliproteins to the thylakoid lumen.

Amino Acid Sequence↗
PubMed1978

[Respiratory localizations of Launois-Bensaude symmetrical lipomatosis. Apropos of 3 cases].

The authors report 3 observations of cervico-facial lipomatosis with mediastinal localization. In the 3 cases the rather unusual localization of Launois and Bensaude's disease produced respiratory troubles which worsened a chronic respiratory insufficiency due to another cause. Once a tracheotomy had to be done because of tracheo-malacia. Another time there was a pharynged localization. This disease etiology always remains obscure, usually appearing in alcoholic addicts of about 50. Mediastinal localizations have been unfrequently described but must be searched for systematically. The evolution is chronic, without specific treatment. If there is already a chronic respiratory insufficiency in relation with a chronic obstructive bronchopneumopathy or a cardiac insufficiency, then the mediastinal localization becomes an aggravating factor.

Aged↗