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Biomedical subjects

C F Baxter

Publications and source records attributed to C F Baxter.

At least 37 records · Page 2Linked to original sources
PubMed1981

L-Proline inhibition of glutamate release.

The influence of 1 mM-L-proline on electrically stimulated release of endogenous glutamate from slices of rat frontal cortex was measured. One mM-L-proline approximates the in vitro concentration that inhibits glutamate-induced spreading depression. Also, this L-proline level has been reported to be present in brain after an intraperitoneal injection that induced amnesia in chicks. L-Proline but not D-proline exhibits an inhibitory effect on glutamate release, thus supporting the suggestion that this mechanism may play a role in memory retention and/or formation.

Animals↗
PubMed1980

Role of carbon dioxide fixation, blood aspartate and glutamate in the adaptation of amphibian brain tissues to a hyperosmotic internal environment.

Mechanisms have been examined by which hyperosmotic blood plasma might elevate the levels of aspartate and glutamate in the brain of the toad Bufo boreas. CO2 fixation was assessed by two in vivo methods using [2-14 C]glucose injected intracisternally. Thirty minutes after injection, the 14C labeling of glutamate and aspartate was more than 100 times greater in brain than in liver. In brain tissues, 40 + % of 14C atoms appeared to be incorporated into aspartate via the pyruvate carboxylase pathway. Brain tissues of control toads and toads adapting or adapted to hyperosmotic plasma osmolality revealed no differences in the rate of CO2 fixation as related to glucose utilization or tissue pool sizes of glutamate and aspartate. Elevated levels of these amino acids in blood plasma preceded increases in brain tissues. Carbon atoms required during hyperosmotic adaptation for expansion of amino acid pools in brain tissues may, in part, originate from amino acids in blood but apparently not from CO2 fixation in brain.

Adaptation, Physiological↗
PubMed1979

Compartments of tubulin and tubulin-like proteins in differentiating neubroblastoma cells.

Cytoplasmic, tubular and particulate fractions of differentiating neuroblastoma cells were prepared and the tubulin together with tubulin-like proteins was measured in each cell fraction during different stages of cell differentiation. In undifferentiated cells, 73%, 5% and 22% of the tubulin and tubulin-like proteins were contained in the cytoplasmic, tubular and particulate fractions, respectively. After 5 days of differentiation, the overall content of tubulin and tubulin-like proteins had increased by 73%. This corresponded to increases of 45%, 145% and 100% in the cytoplasmic, microtubular and particulate fractions, respectively. The increase in membrane-bound (particulate) tubulin and tubulin-like proteins was significantly greater than the total increase of proteins in the particulate fraction. Polyacrylamide gel electrophoresis of the proteins in each subcellular fraction revealed the presence of protein bands corresponding to the alpha and beta subunits of tubulin. Whereas these bands indicated equal amounts of protein in the alpha and beta positions for the tubular and particulate cell fractions, an analysis of the cytoplasmic fraction revealed much more protein migrating to the alpha-tubulin position than to the beta-tubulin position, especially during cell differentiation. Furthermore, two overlapping but distinct protein bands were demonstrable in the position of the alpha-tubulin from the cytoplasmic fraction. These bands were designated alpha 1 and alpha 2. The particulate fraction contained only the alpha 1 and the tubular fraction only the alpha 2 protein band. The addition of 1 mM dibutyryl cyclic AMP to the neuroblastoma cells, at the time when the serum was withdrawn, enhanced the rate of differentiation and the redistribution of tubulin and tubulin-like proteins within the 3 cellular compartments. These results are discussed as they relate to the regulation, biosynthesis, turnover and compartmentation of tubulin and tubulin-like proteins in differentiating neuroblastoma cells.

Animals↗
PubMed1975

Gamma-aminobutric acid and glutamate decarboxylas (l-glutamate 1-carboxy-lyase e.c. 4.1.1.15) in the nervous system of the cockroach, periplaneta americana.i.regional distribution and properties of the enzyme.

Both the central and peripheral nervous system of the cockroach Periplaneta americana contain gamma-aminobutyric acid (GABA) and glutamate decarboxylase (GAD). In the central ganglia of the cockroach, an average of more that 60 mumoles of GABA are formed from glutamate (Glu) per gram wet weight of tissue per hour. This activity level of the GAD apoenzyme is considerably higher than that found in the central nervous system of crustaceans, amphibians, avians and mammals but is similar to that reported for nervous system tissues from other insect species. A comparison of properties of the crude cockroach enzyme with GAD from crustacean and mammalian origin revealed both similarities and differences: whereas crude cockroach GAD has cofactor requirements and an affinity for Glu substrate (Km 2.8 X 10-2) which are similar to GAD from lobster and mouse, it is uniquely inhibited by both Cl-and by GABA. The GAD from cockroach nervous tissues has two apparent pH optima of which the lower one is preferentially inhibited by a compound which is found in the nerve sheath and the fat body tissue adjacent to ganglia and axons.

Aminobutyrates↗
PubMed1975

Viability of some metabolic processes in the isolated toad brain adapted to two osmotic environments.

The viability of the isolated toad brain in an aerated Ringer-like medium has been evaluated by the following criteria: 1) amino acid content before and after incubation; 2) accumulation of amino acids in the incubation medium; 3) a comparison of glucose utilization and [U-14C]glucose metabolism with that occurring in vivo; 4) tissue swelling; and 5) tissue lactate contents. On the basis of these criteria, the isolated toad brain, from toads adapted to a fresh-water or a salt-water environment, retains considerable metabolic integrity for at least 2 hr of incubation at 25 degrees C. Specifically, there was no swelling of the tissue, no apparent accumulation of lactate in the tissue, glucose appeared to be utilized at a rate not too different from that calculated for the toad brain in vivo, and the distribution of label from [U-14C]glucose had an overall pattern which resembled that observed in vivo. The tissue levels of amino acids were generally stable in vitro; however, there was a marked decline in the content of aspartate. The accumulation of amino acids in the medium varied considerably from one amino acid to another. Thus, there was very little net efflux of aspartate, GABA, and glutamate from the tissue but considerable net efflux of glutamine. This efflux of amino acids was greater from brains of hyperosmotically adapted toads than from the brains of toads adapted to fresh water by amounts proportional to their initial tissue contents.

Adaptation, Physiological↗
PubMed1973

Glutamate uptake by the isolated toad brain.

The isolated toad brain accumulates L-glutamate against strong concentration gradients until a tissue-to-medium concentration ratio of about 3000 : 1 is attained. The accumulated glutamate does not equilibrate with most of the endogenous tissue glutamate but is converted rapidly to glutamine and released into the medium. This mechanism may be involved in the preservation of low extracellular levels of cerebral glutamate.

Animals↗