Biomedical subjects

A Miseta

Publications and source records attributed to A Miseta.

31 records · Page 2Linked to original sources

PubMed1994

Cation distribution in mammalian red blood cells: interspecies and intraspecies relationships between cellular ATP, potassium, sodium and magnesium concentrations.

The intracellular K+/Na+ ratio of erythrocytes of different mammalian species are known to differ markedly. These differences are sustained despite plasma potassium and sodium concentrations being almost identical, i.e. high [Na+] and low [K+], in all mammalian species. Conventional cell theory couples intracellular K+ and Na+ concentrations with Na+/K(+)-dependent ATPase activity. Ling's Association-Induction (AI) hypothesis couples intracellular K+ and Na+ concentrations with the concentration of ATP, by way of an inductive adsorption of both monovalent cations on the available terminal and lateral carboxyl groups of proteins. Based on the working hypothesis, different relationships are expected between the erythrocyte K+ and Na+ concentrations and ATP levels. Our results indicate that the intracellular ATP level in erythrocytes of different species corresponds with intracellular K+ and Na+ levels, K+/Na+ ratios and total K+ + Na+ levels. Similar relationships were revealed between the erythrocyte ATP and monovalent cation contents of different individual sheep.

Adenosine Triphosphate↗

PubMed1993

Effect of the immediate precursors of phenylalanine and tyrosine on growth and protein synthesis in phenylalanine- and tyrosine-deprived HeLa cells.

Although Phe is an essential amino acid in mammalian cells, its immediate precursor, beta-phenylpyruvic acid (BPP), when present in Phe-deficient medium at 10(-4) and 10(-3) M is converted at a sufficient rate to Phe to sustain growth at 60 and 100% of non-deficient control HeLa S-3 cells, respectively. In contrast, Tyr-deficient cells were unable to convert the immediate precursor of Tyr, OH-beta-phenylpyruvic acid (OHBPP), nor could BPP rescue Tyr-deficient cells. The results are considered in terms of the organization of intracellular pathways by which precursors are transaminated and made available for protein synthesis.

Cell Division↗

PubMed1993

Relationship between cellular ATP, potassium, sodium and magnesium concentrations in mammalian and avian erythrocytes.

Intracellular K+/Na+ ratios of erythrocytes of various mammalian species are known to differ markedly. We have measured ATP, K+, Na+, Mg2+, H2O contents of erythrocytes of twelve mammalian and three avian species. Our results indicate that the intracellular ATP concentration in erythrocytes of different species is in close positive correlation with the K+/Na+ ratios (linear correlation coefficient, r = 0.852). Furthermore, ATP levels in erythrocytes of individual sheep with different potassium concentrations correspond with their K+/Na+ ratios (r = 0.747). Intracellular magnesium concentrations also correlate with ATP concentrations in erythrocytes of different species (r = 0.629) and in different sheep (r = 0.549).

Adenosine Triphosphate↗

PubMed1993

Relaxometry, animal biodistribution, and magnetic resonance imaging studies of some new gadolinium (III) macrocyclic phosphinate and phosphonate monoester complexes.

The Gd3+ complexes of three new phosphorus containing tetraaza macrocycles (1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrakis (methylene ethylphosphonic acid), H4DOTEP; 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetrakis (methylene phosphonic acid monoethylester), H4DOTPME; and the corresponding n-butyl ester, H4DOTPMB) were prepared and examined for possible use as MRI contrast agents. Although thermodynamically and kinetically less stable than Gd(DOTA)- in saline and HSA solution, the stability of these new macrocyclic complexes appears to be sufficiently high for in vivo applications. NMRD relaxivity profiles of the three complexes indicate that the number of inner sphere water molecules for these chelates is < or = 1 and that the more hydrophobic chelate, Gd(DOTPMB), binds to human serum albumin (HSA). Biodistribution studies of the radioactive 153Sm or 159Gd chelates in rats, gamma imaging of the 153Sm chelates in rats, and proton MRI studies of the nonradioactive Gd3+ chelates in rabbits all indicate that the DOTPMB complexes accumulate preferentially in the liver, spleen, and small intestines while the more hydrophilic DOTEP and DOTPME complexes appear to display renal clearances similar to other low molecular weight contrast agents.

Animals↗

PubMed1993

Changes in the concentration of ions during senescence of the human erythrocyte.

Flash frozen samples of normal human blood were cryosectioned and cryodried for electron probe x-ray microanalysis of the concentration of ions and elements in individual erythrocytes (RBCs). The data (expressed in mM/kg dry weight) demonstrated a systematic pattern of variation between the concentration of ions and elements in the RBCs. Specifically as K+ and Cl- decreased in concentration, Ca2+ and sulfur increased in concentration. Phosphorous, Na+ and Mg2+ did not demonstrate a significant pattern of change. These findings are related to the dehydration and to the volume decrease that accompanies senescence of the RBC.

Calcium↗

PubMed1992

Human and dog erythrocytes: relationship between cellular ATP levels, ATP consumption and potassium concentrations.

The intracellular K+/Na+ ratio of various mammalian cell types are known to differ remarkably. Particularly noteworthy is the fact that erythrocytes of different mammalian species contain entirely different potassium and sodium concentrations. The human erythrocyte is an example of the supposedly "normal" high potassium cell, while the dog erythrocyte contains ten times more sodium than potassium ions (Table I). Furthermore, this difference is sustained despite the plasma sodium and potassium concentrations being almost identical in both species (high Na+ and low K+). In spite of these inorganic ion differences, both human and dog erythrocytes contain 33% dry material (mostly Hb) and 67% water. Conventional cell theory would couple cellular volume regulation with Na+ and K+ dependent ATPase activity which is believed to control intracellular Na+/K+ concentrations. Since the high Na+ and low K+ contents of dog erythrocytes are believed to be due to the lack of the postulated Na/K-ATPase enzyme, they must presumably have an alternative mechanism of volume regulation, otherwise current ideas of membrane ATPase activity coupled volume regulation need serious reconsideration. The object of our investigation was to explore the relationship between ATPase activity, ATP levels and the Na+/K+ concentrations in human and dog erythrocytes. Our results indicate that the intracellular ATP level in erythrocytes correspond with their K+, Na+ content. They are discussed in relation to conventional membrane transport theory and also to Ling's "association-induction hypothesis", the latter proving to be a more useful basis on which to interpret results.

Adenosine Triphosphate↗

PubMed1991

Mammalian seryl-tRNA synthetase associates with mRNA in vivo and has homology to elongation factor 1 alpha.

Previous work in our laboratories (Slobin, L. I., and Greenberg, J.R. (1988) Eur. J. Biochem. 173, 305-310) showed that messenger ribonucleoprotein (mRNP) particles possess a polypeptide component of approximately 62 kDa that appears to share a common epitope with eucaryotic elongation factor 1 alpha (EF-1 alpha). We report here that the previously unidentified mRNP constituent corresponds to seryl-tRNA synthetase (SerRS). Furthermore, we show that SerRS contains a sequence motif that is shared by both EF-1 alpha and glutaminyl-tRNA synthetase. We also find that the association of SerRS with mRNA depends on the functional state of the latter. Our data suggest that SerRS may participate directly in the initiation phase of protein synthesis.

Amino Acid Sequence↗

PubMed1991

Proportional equilibration of K, Na ions, and sucrose molecules in pig lenses incubated in the presence of the non-ionic detergent Triton X-100.

The release of sodium and potassium and the uptake of sucrose molecules was studied in pig lenses incubated in isosmotic sucrose solution in either the presence or absence of 1% Triton X-100 (a non-ionic detergent). This Triton X-100 treatment has been shown to cause severe disruptions of cell membrane integrity. If sodium and potassium were free in the lens fibers as in a dilute aqueous solution, they would be expected to diffuse three to four times faster than sucrose. However, measurements of sodium and potassium release and sucrose uptake in the Triton X-100 treated lenses show a 1:1 equilibration. When pig lenses were incubated in the same solution without detergent, the sucrose uptake was significantly less than the potassium and sodium release. It is postulated that a slow, detergent mediated collapse of protein-water-ion interactions within the lens is the rate-limiting step of the observed equilibration of monovalent cations and sucrose molecules.

Animals↗

PubMed1989

Paraproteins associated with low plasma sodium levels.

The mechanism of the maintenance of low plasma sodium levels seen in certain multiple myeloma cases has been attributed to the cationic nature of pathological immunoglobulins (paraproteins). This hypothesis was tested with equilibrium dialysis and polyacrylamide gel electrophoresis techniques. Citrated plasma samples and affinity chromatography purified paraproteins of three multiple myeloma patients with abnormally low plasma sodium levels were dialysed against 140 mmol/L NaCl solution at pH 7.4 for 24 hours. The electrophoresis of paraproteins was conducted under non-denaturing conditions. Low plasma sodium concentrations observed under the dialysis of the patients' plasma samples were in good agreement with earlier reports. However, the isolated paraproteins did not show any sodium exclusion during the dialysis experiment. The electrophoretic mobility of the paraproteins at pH 7.4 indicated that the isoelectric point of these molecules was below 7.4, so they cannot behave as cations at the pH of the blood. From these data it appears that the maintenance of low plasma sodium levels in certain IgG type myeloma cases cannot be explained by the previously postulated cationic nature of the paraproteins.

Amino Acids↗

PubMed1989

The role of protein associated amino acid precursor molecules in the organization of genetic codons.

A better understanding of the origin and organization of genetic codons is possible based on the metabolic relatedness of amino acids. Amino acids with similar codons (anticodons) usually have the same or similar precursor molecule, even if the amino acids are not related physico-chemically. These observations suggest, that amino acid precursor molecules and enzymes responsible for the synthesis of amino acids "must have seen" the protein synthesis machinery, and played a fundamental role in the codon (anticodon) organization.

Amino Acids↗

PubMed1988

Extent and properties of nonbulk "bound" water in crystalline lens cells.

Crystalline lenses provided good material to study and measure the properties of cellular water. Different methods were used to establish the extent and properties of nonbulk water in mammalian lenses. These methods include: NMR titration analysis, a test of the osmotic properties, a test of dye exclusion In lenses with intact cell membranes and in lenses with disrupted cell membranes, and the water-holding capacity of lenses subjected to 40,000 x g for 1 hour with intact cell membranes and in lenses with disrupted cell membranes. The data from these methods, as well as other data from the literature, lead to the conclusion that most, if not all, of the water in lens cells (up to 2.2 g water/g dry mass) has motional and osmotic properties that distinguish it from bulk water. These findings call into question the common and convenient assumption that all but a small proportion of cellular water is like that in dilute solution.

Animals↗

PubMed1987

Hydrogen ion dependent reversible fibrillarization and hydration of chromatin in divalent cation-depleted isolated rat liver nuclei.

Rat liver cell nuclei isolated in the presence of Ca++ and Mg++ ions were exposed to citrate buffer at different pH levels. Their morphology was studied with the electron microscope and the water content measured. At a low pH the chromatin remained compact, but at neutral pH an intense fibrillarization of the chromatin was observed; and, seemed to be reversible, because of deoxyribonucleoproteins (DNP) filaments which dispersed at a pH of 7 were repacked to their previous site at a pH of 3. The ribonucleo-proteins (RNP)-containing structures did not show the same reversible fibrillarization. In addition to the morphological changes, a large increase in the water content ("water-holding capacity") of the chromatin structures was observed.

Animals↗

PubMedDate not supplied

Ion and water distribution in pig lenses incubated at 0 degree C to disable ion transport pumps.

This study was designed to test how extended exposure of lenses to sera with different ionic strengths influences the distribution of ions and water in the lens. Pig lenses were incubated in cold sera (0 degree C), which were adjusted to variable concentrations of NaCl, and their K+, Na+, Cl-, and water contents were measured. Incubation at 0 degree C inhibits active transport processes and thereby allows equilibration of the mobile ions and water. The hypothesis was that lens water content (volume) would follow the ion-induced protein changes predicted by a model derived from previous osmotic studies on proteins. As expected, exposure of the lens to cold caused a gain of sodium and a partial loss of potassium. However, the potassium concentration in the lens remained several fold higher than that in the bathing solution (about 41 vs. 1.8-4.6 mM/kg H2O), indicating that a portion of the potassium within the cold-exposed lens was not free to diffuse. That the water content of the lens showed a negative rather than a positive relationship with the concentration of NaCl within the lens was explained by the idea that an increase in NaCl within the lens (up to at least 250 mM/kg H2O) causes a decrease in the osmotically unresponsive water volume associated with lens proteins.

Animals↗