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Biomedical subjects

S M Hwang

Publications and source records attributed to S M Hwang.

At least 91 records · Page 5Linked to original sources
PubMed1986

Formation of the thiol adducts of 4'-(9-acridinylamino)methanesulfon-m-anisidide and their binding to deoxyribonucleic acid.

We investigated the interactions of 4'-(9-acridinylamino)methanesulfon-m-anisidide (mAMSA) with thiol-containing compounds and the potential binding of the thiolytic adducts to DNA. All thiols tested (glutathione, cysteine, coenzyme A, 2-mercaptoethanol and lactate dehydrogenase) formed adducts with mAMSA as evidenced by changes in the absorption spectrum of mAMSA and induction of fluorescence. Spectral changes induced by the thiols were different, suggesting that each thiol induced specific changes in the electronic structure of the acridine nucleus. Treatment of glutathione with p-chloromercuribenzoate eliminated the absorption spectral changes and induction of fluorescence, indicating that the reduced-thiol group is involved. In high ionic strength buffer, addition of calf thymus DNA induced fluorescence-quenching of both the mAMSA-glutathione and mAMSA-cysteine adducts without spectral shift. Viscometric studies showed that mAMSA and mAMSA-glutathione intercalated into DNA and produced similar increases in the length of linear DNA.

Aminoacridines↗
PubMed1986

Immunohistochemical localization of keratin in the taste buds of rat vallate papillae.

Keratin detected with anti-human whole keratin serum, raised in rabbits by injection of the isolated human whole keratin, was used as a histologic marker to study the origin of the cells in taste buds. Rat vallate papillae, including surrounding tissue, were processed for indirect immunofluorescent staining of ketatin. In the taste buds, most basal cells and some of the elongated cells were immunoreactive with anti-keratin serum, showing that most taste-bud cells, if not all, originate from cells of epithelial origin.

Animals↗
PubMed1986

Phosphatidylinositol:myo-inositol exchange activity in intact nerve endings: substrate and cofactor dependence, nucleotide specificity, and effect on synaptosomal handling of myo-inositol.

Micromolar concentrations of CMP produced a large increase in Mn2+-dependent phosphatidylinositol:myo-inositol exchange activity in isolated nerve endings or synaptosomes. The apparent Km for CMP was 2 microM, and that for myo-inositol was 38 microM. Only cytidine nucleotides were capable of enhancing activity, and this effect is probably specific for CMP, because the synaptosomal preparation rapidly converted CTP or CDP to CMP. Manganese did not affect the uptake of myo-inositol into the synaptosomal cytosolic fraction or myo-inositol levels. Determinations of myo-inositol specific activity showed that the Mn2+-enhanced labeling of phosphatidylinositol was not accompanied by a decrease of label content in free myo-inositol. This lack of an effect on intrasynaptosomal myo-inositol and the dependence of exchange on cytidine nucleotides whereas cytidine itself was previously found to be without effect show that for the bulk of Mn2+-dependent exchange activity, it is the myo-inositol in the incubation medium that is being directly incorporated into membrane-bound phosphatidyl-inositol. Because CMP dependence is the hallmark of exchange catalyzed by CDP-diacylglycerol:inositol phosphatidyl transferase, this enzyme is likely to be responsible for most of the exchange activity in synaptosomes. The strong affinity of this exchange system for CMP suggests that endogenous levels of this nucleotide might support Mn2+-dependent exchange in the absence of added nucleotide.

Animals↗
PubMed1984

Inositol uptake by cultured isolated rat Schwann cells.

The uptake of radiolabeled myo-inositol by Schwann cells isolated from the sciatic nerve of 2-4 day old rats was found to occur by a saturable, sodium-dependent phlorizin-inhibited mechanism with an estimated Km of 30 microM. The system was inhibited by galactose and glucose but not by galactitol. At high concentrations of myo-inositol, a diffusion-like process appeared to be functional. The characteristics of the saturable system are very similar to those of myo-inositol uptake by the endoneural fascicle preparation of sciatic nerve.

Animals↗
PubMed1983

Uptake of L-[14C]proline by isolated rat brain capillaries.

Rat brain capillaries exhibit concentrative uptake of L-proline. The uptake is mediated by two saturable systems, one with a Km of 0.11 mM and another with a Km of 5.9 mM. Entry also occurred by diffusion, especially at high substrate concentrations. The saturable high-affinity system is sodium-dependent, with a Km for sodium of 36 mM. Proline uptake is not inhibited by lysine, but is inhibited by phenylalanine, glycine, and leucine. alpha-Methylaminoisobutyric acid (MeAIB), a model for sodium-requiring transport systems, is a competitive inhibitor of the low-Km system. b-2-Aminobicyclo-[2,2,1]-heptane-2-carboxylic acid (BCH), a model for nonsodium-dependent transport, however, also inhibited proline uptake.

Animals↗
PubMed1983

L-Proline transport by isolated renal tubules from newborn and adult rats.

Proline uptake and metabolism has been examined in newborn Sprague-Dawley rat kidney and compared to that in adult animals. [14C]-Proline uptake by renal tubule fragments from newborn rats occurs at the same initial rate as in adult tubules, but at physiologic concentrations achieves significantly higher intracellular levels after 15 min of incubation. Considerable metabolism of the proline taken up was observed in tissue of both ages. Analysis of acid soluble and insoluble tubule fractions from newborn and adults indicates similar degrees of proline incorporation into protein and oxidation to CO2 relative to the amount of radioactivity taken up. A major difference exists, however, with respect to the labeled components of the acid extract: adult tubules convert [14C]-proline to metabolites at a rate twice that of newborn. Analysis of concentration-dependent uptake data reveals two distinct entry systems for proline in both isolated newborn and adult tubules. No difference in the Km or Vmax was found between the young and mature tubules.

Age Factors↗
PubMed1982

Developmental pattern of cystine transport in isolated rat renal tubules.

Isolated renal cortical tubule fragments from rats ranging in age from less than 48 h to 15 weeks were used to examine the pattern of cystine uptake with development. Immature tubules took up cystine with a faster initial rate than mature tubules and did not reach a steady state by 60 min. By eight weeks of age, the timed uptake of cystine began to approach a steady state and between 8 and 11 weeks the uptake pattern achieved its adult form of reaching a steady state by 30 min of incubation. Analysis of the intracellular metabolism of the cystine taken up by the newborn tubules revealed that the majority had been reduced to cysteine with the formation of small amounts of reduced glutathione. Cystine entered the renal cortical tubule cell from the newborn via two saturable transport systems similar to the mature animal. The kinetic parameters of initial uptake of these two transport systems were similar in the mature and newborn animal except for a higher maximum transport velocity for the low Km, low capacity system in the newborn. Lysine inhibited cystine uptake by newborn tubules and this inhibition appeared to occur on the low Km, low capacity transport system similar to the adult. Cystine uptake was sodium dependent with an apparent affinity for sodium of 36 mequiv./l. From this data, the physiologic cystinuria of the immature animal does not appear to be refeable to a lower rate of influx as previously observed with the cortical slice. Other mechanisms should be sought to explain this phenomenon of immaturity.

Aging↗
PubMed1980

Transport interactions of cystine and dibasic amino acids in isolated rat renal tubules.

Isolated renal cortical tubules prepared from adult male Sprague-Dawley rats were used to study the nature of cystine entry into tubule cells and its transport interactions with dibastic amino acids. The uptake of cystine over time was progressive, reaching a steady-state after 60 min of incubation. Analysis of the intracellular pool after incubation revealed that a significant fraction of the transported cystine was reduced to cysteine. A kinetic analysis of uptake demonstrated that two systems for cellular entry of cystine existed with a Km1 of 0.012 mM and Km2 of 0.55 mM. Cystine uptake was sodium dependent with an apparent Km for sodium of 36 mEq/liter. Lysine inhibited cystine uptake via the low Km system, but appeared not to inhibit cystine uptake via the high Km system. Ornithine, leucine, and isoleucine each inhibited cystine uptake via the low Km system. Arginine appeared to affect both systems for cystine uptake. Cystine inhibited the uptake of lysine by isolated renal tubules. The data suggest that cystine at physiologic concentrations is transported into renal tubule cells nearly equally by two systems, of which, the low Km system is shared with the dibasic amino acids. A defective low Km system could in part explain human cystinuria.

Amino Acids, Diamino↗
PubMed1980

Uptake of L-[35S]cystine by isolated rat brain capillaries.

Adult rat brain capillaries were isolated by a simplified procedure and showed an enrichment of the marker enzyme, gamma-glutamyltranspeptidase. The uptake of [35S]cystine at 37 degrees C by this preparation can be divided into two components, a sodium- and energy-dependent transport process for the free amino acid pool, with an apparent Km of 36 microM, and a binding process, with an apparent Km of 1.13 mM. Chemical analysis of the amino acid pool indicates that cystine is the major from of intracapillary 35S. Cystine transport was not inhibited by lysine, but glycine, alpha-methylaminoisobutyric acid and beta-2-aminobicyclo-[2,2,1]-heptane-2-carboxylic acid were inhibitory to a small extent.

Amino Acids↗
PubMed1979

Developmental and other characteristics of lysine uptake by rat brain synaptosomes.

Synaptosomes isolated from adult or newborn rat cerebrum take up L-lysine by two saturable systems, one with a high affinity low capacity and the other with a low affinity high capacity. Initial rate of uptake for low lysine concentrations is mort tissue. Analysis of kinetic data indicates that synaptosomes of the newborn have a higher Vmax than those of the adult for high affinity system but adult for high affinity system but adult synaptosomes have a higher Vmax than newborn for low affinity system. At a physiological lysine concentration of 0.5 mM, the calculated contributions of two systems indicate that the adult uptake occurs for about 71% by low affinity system but the newborn utilizes both systems to the same extent. The uptake is sodium independent but pH dependent. Lysine uptake is inhibited by other dibasic amino acids, arginine and ornithine but not cystine. Kinetic analysis indicates that arginine specifically inhibits the high affinity, low Km system for lysine uptake.

Aging↗
PubMed1978

On the development of glycine transport systems by rat renal cortex.

The initial uptake of glycine by renal cortical slices from newborn Sprague-Dawley and Long-Evans rats is the same as that observed in adult tissues. Both newborn and adult tissue possess similar high and low affinity glycine transport systems which require an examination of velocity measurements over a wide range of concentration (0.02--50.0 mM) for their discernment. Initial rates of glycine uptake by isolated renal tubule fragments from newborn and adults are similar at a physiological substrate concentration but at high glycine levels there appears to be a decrease in velocity of uptake (V) associated with the high Km system in the young. Whatever preparation of renal cortex is studied, there is a consistent finding that immature tissue is able to accumulate much higher intracellular levels of glycine than the adult, a finding consistent with slower efflux from the cell. An interpretation of the etiology of physiologic aminoaciduria in young animals should take this into account.

Aging↗