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S K Hong

Publications and source records attributed to S K Hong.

At least 127 records · Page 7Linked to original sources
PubMed1991

Identification of an A-factor-dependent promoter in the streptomycin biosynthetic gene cluster of Streptomyces griseus.

A-factor (2-isocapryloyl-3R-hydroxymethyl-gamma-butyrolactone) is a microbial hormone controlling streptomycin (Sm) production, Sm resistance and sporulation in Streptomyces griseus. In order to identify A-factor-dependent promoters in the Sm biosynthetic gene cluster, a new promoter-probe plasmid with a low copy number was constructed by using an extremely thermostable malate dehydrogenase gene as the reporter. Of the three promoters in the Sm production region that includes strR, aphD and strB, only the promoter of strR, which codes for a putative regulatory protein, was found to be directly controlled by A-factor. This was also confirmed by S1 nuclease mapping. The region essential for its A-factor-dependence was determined to be located 430-330 base pairs upstream of the transcriptional start point. Increase in the copy number of the strR promoter region did not lead to a corresponding increase in the total promoter activity, probably due to titration of a putative activator which binds to the enhancer-like region and controls the expression of the strR promoter. This putative activator is apparently distinct from the A-factor-receptor protein. The aphD gene, which encodes the major Sm resistance determinant, Sm-6-phosphotransferase, was transcribed mainly by read-through from the A-factor-dependent strR promoter; this accounts for the prompt induction of Sm resistance by A-factor.

4-Butyrolactone↗
PubMed1991

Phosphorylation of the AfsR product, a global regulatory protein for secondary-metabolite formation in Streptomyces coelicolor A3(2).

The AfsR protein is essential for the biosynthesis at the wild-type level of A-factor, actinorhodin, and undecylprodigiosin in Streptomyces coelicolor A3(2) and Streptomyces lividans. Because overexpression of the afsR gene caused some deleterious effect on these strains, a multicopy plasmid carrying the whole afsR gene was introduced into Streptomyces griseus, from which a crude cell lysate was prepared as a protein source. The AfsR protein was purified to homogeneity from the cytoplasmic fraction through several steps of chromatography, including affinity column chromatography with ATP-agarose and use of anti-AfsR antibody for its detection. The molecular weight of AfsR was estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by gel filtration to be 105,300, which is in good agreement with that deduced from the nucleotide sequence of afsR. The purified AfsR protein was found to be phosphorylated through the transfer of the gamma-phosphate group of ATP in the presence of the cell extracts of S. coelicolor A3(2) and S. lividans. This phosphorylation proceeded very rapidly, and no competition was observed with CTP, GTP, UTP, or cyclic AMP. In the cell extract of S. griseus, no activity phosphorylating the AfsR protein was detected, suggesting that this activity is not generally present in Streptomyces spp. but is specific to certain species. It is conceivable that the extent of phosphorylation of the AfsR protein modulates its regulatory activity which, in turn, regulates expression of some target gene(s) involved in the secondary-metabolite formation in S. coelicolor A3(2).

Adenosine Triphosphate↗
PubMed1991

Renal, hormonal, and fluid shift responses to ANP during head-out water immersion in awake dogs.

Renal responses to low doses of atrial natriuretic peptide (ANP) may be potentiated during water immersion-induced central hypervolemia. To test this hypothesis, ANP was infused in awake dogs in doses of 0, 5, and 25 ng.kg-1.min-1 either when the dogs were in air or during head-out water immersion (WI) under thermoneutral conditions (37 degrees C). In general, there were greater diuretic (V) and natriuretic responses (UNaV) at the same level of plasma ANP in WI, with the slopes (or sensitivities) of V and UNaV in relation to plasma ANP levels being significantly increased during WI. Plasma renin activity decreased only during WI and was significantly correlated with both V and UNaV only during WI. Plasma and urinary arginine vasopressin levels were unchanged during WI. Infusion of ANP prevented the usual decline of hematocrit that occurs during WI. These results support the view that the renal sensitivity to ANP is augmented during the plasma volume expansion of WI. In addition, ANP may attenuate the transcapillary fluid shift that occurs during WI.

Animals↗
PubMed1990

Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2).

The afsR gene of Streptomyces coelicolor A3(2) complements afsB mutations affecting production of pigmented antibiotics. It also directs pigment production in Streptomyces lividans when carried on a plasmid vector. Nucleotide sequencing of the afsR gene revealed that it codes for a 993-amino acid protein (Mr 105,600) with A- and B-type ATP-binding consensus sequences at its N-terminal portion and two DNA-binding consensus sequences with a helix-turn-helix motif at its C-terminal portion. Each of the N- and C-terminal halves was capable of conferring pigment production, to some extent, in S. lividans, when carried separately on a multicopy plasmid. In addition, expression in trans of the two regions on the same plasmid conferred pigment production to almost the same extent as did the intact afsR gene. Mutations at the two ATP-binding consensus sequences, that were generated by in vitro site-directed mutagenesis, revealed their functional importance. Disruption of the S. coelicolor A3(2) chromosomal afsR gene in either the N- or C-terminal half using phage phi C31 KC515 resulted in significant, but not complete, loss of pigment production. These data suggest that the AfsR protein comprises two domains, viz., an ATP-binding and a DNA-binding domain, each of which could function as a positive regulator for pigment production. These afsR mutants sporulate normally. In addition to an internal promoter, which we previously detected in the middle of the AfsR coding region, S1 nuclease mapping revealed two tandem transcriptional start points, separated by 64 bp, upstream from a putative ATG start codon of the AfsR product.

Amino Acid Sequence↗
PubMed1990

Splenic contraction during breath-hold diving in the Korean ama.

Major increases of hemoglobin concentration and hematocrit, possibly secondary to splenic contraction, have been noted during diving in the Weddell seal. We sought to learn whether this component of the diving response could be present in professional human breath-hold divers. Splenic size was measured ultrasonically before and after repetitive breath-hold dives to approximately 6-m depth in ten Korean ama (diving women) and in three Japanese male divers who did not routinely practice breath-hold diving. Venous hemoglobin concentration and hematocrit were measured in nine of the ama and all Japanese divers. In the ama, splenic length and width were reduced after diving (P = 0.0007 and 0.0005, respectively) and calculated splenic volume decreased 19.5 +/- 8.7% (mean +/- SD, P = 0.0002). Hemoglobin concentration and hematocrit increased 9.5 +/- 5.9% (P = 0.0009) and 10.5 +/- 4% (P = 0.0001), respectively. In Japanese male divers, splenic size and hematocrit were unaffected by repetitive breath-hold diving and hemoglobin concentration increased only slightly over baseline (3.0 +/- 0.6%, P = 0.0198). Splenic contraction and increased hematocrit occur during breath-hold diving in the Korean ama.

Adult↗
PubMed1990

Interaction of heptanol and pressure on sodium and chloride transport by toad skin.

We examined the interaction of heptanol and hydrostatic pressure on Na+ and Cl- transport in isolated toad skin. In the presence of Cl-, heptanol decreased short-circuit current (Isc) and total transepithelial resistance (Rt). However, in the absence of Cl- in the mucosal bath, heptanol increased Rt, although it retained the same inhibitory effect on Isc. When transepithelial active Na+ transport was blocked by amiloride, heptanol had no effect on Isc whether or not Cl- was present, whereas it decreased the shunt resistance (Rs) only in the presence of Cl- in the mucosal bath. Moreover, this effect of heptanol on Rs was significantly smaller in the presence of diphenylamine-2-carboxylate (DPC), a known Cl- channel blocker. Pressure also decreased Isc through inhibition of active Na+ transport, but it increased Rs. When heptanol and pressure were applied together, their inhibitory effects on Isc were additive, but their effects on Rs were antagonistic. Furthermore, when a transepithelial Cl- current was produced by reducing the Cl- concentration of the serosal bath, heptanol stimulated this current, which was reversibly inhibited by pressure or DPC addition to the mucosal bath. When the heptanol-stimulated Cl- current was first inhibited by pressure, subsequent DPC addition had less or no effect. These results suggest that one site of an antagonistic interaction of heptanol and pressure in toad skin is an apical membrane Cl- conductance.

Alcohols↗
PubMed1990

Hyperbaric oxygen effect on active Na+ transport across isolated toad skin.

The effect of hyperbaric oxygen (HBO) on Na+ transport across the isolated toad (Bufo marinus) skin was studied by measuring the transepithelial short-circuit current (ISC) and resistance (R) at 5, 8, and 10 ATA PO2 and 15 ATA normoxia during steady state conditions. The imposition of 5, 8, and 10 ATA PO2 for 2 h resulted in 45, 52, and 85% decrease in ISC, respectively. This decrease in ISC was always accompanied by an increase in R. When amiloride (10(-4) M) was added to the bathing medium, ISC decreased to zero within 15 min regardless of the PO2 level, indicating that the HBO-induced decrease in ISC is caused by an inhibition of amiloride-sensitive Na+ transport. Addition of both superoxide dismutase (SOD) and catalase to the medium bathing both sides of the skin markedly attenuated the HBO effect on ISC and R. Applying HBO to the serosal or mucosal surface independently produced similar effects on ISC. However, the presence of antioxidant enzymes (SOD and catalase) with 10 ATA PO2 prevented the toxic HBO effect only from the serosal side; no protection by these antioxidant enzymes was observed from the mucosal side. These findings are consistent with a view that free radicals are involved in the HBO-induced inhibition of ISC. However, further studies involving the site(s) of radical generation as well as site(s) of toxic action are needed to understand the cellular and molecular mechanism of HBO toxicity.

Amiloride↗
PubMed1990

Characteristics of increased urine flow during a dry saturation dive at 31 ATA.

Three male divers were subjected to a 7-day dry saturation dive at 31 ATA (New Seatopia). Urine samples were collected for measurements of electrolytes and creatinine for glomerular filtration rate (GFR) 5 times daily, at 3-h intervals during daytime (0700-2200 h) and once at night (2200-0700 h). Collections were taken for 2 days before (predive 1 ATA air), 7 days during 31 ATA exposure, and during 10 days of decompression and for 2 days at postdive 1 ATA air. Blood samples were taken after overnight fasting at each of the dive periods for measurements of atrial natriuretic factor (ANF), electrolytes, and other blood constituents. Compression to 31 ATA resulted in a twofold increase in urine flow accompanied by increases in excretion of osmotic substances (+40%) and sodium (+54%), and a reduction in urine osmolality (-32%). The increase in urine volume was greater (P less than 0.05) at night than day with no change in GFR between day and night, confirming the earlier findings. However, no change in plasma ANF was observed in spite of a sustained increase in daily sodium and water excretion at high pressure. These results suggest that the hyperbaric diuresis-natriuresis may not be directly mediated by the ANF release.

Adult↗
PubMed1990

Effect of hydration state on renal responses to head-out water immersion in conscious dogs.

Renal responses to head-out water immersion (WI) (37 degrees C, WI 100 min) were studied in conscious, instrumented dogs during volume repletion (R), when all blood and urine losses were replaced with 0.9% NaCl, or without volume repletion (NR), to determine the influence of hydration state. The lithium clearance method was used to estimate the locus of the renal tubular fractional sodium excretion (FENa) responses. WI in the R condition increased urine flow (V) from 0.9 (+/- 0.1 SE) to 4.2 (+/- 0.6) ml/min and FENa from 0.7 (+/- 0.1) to 3.2 (+/- 0.8)%. Fractional proximal sodium reabsorption (FPRNa) decreased from 0.82 (+/- 0.03) to 0.69 (+/- 0.1)% and fractional distal sodium reabsorption decreased from 0.96 (+/- 0.01) to 0.88 (+/- 0.04)%. By comparison, WI in the NR condition elicited smaller increments in V and FENa, no change in FPRNa and a significant decrease of FDRNa from 0.97 (+/- 0.01) to 0.93 (+/- 0.01). Although there were quantitative differences in the renal responses in the R and NR conditions, there were similar increments in both arterial and atrial pressures as well as plasma atrial natriuretic peptide concentration; plasma arginine vasopressin was unaltered in either situation, and plasma renin activity was depressed in both conditions. Since plasma protein concentration was significantly lower during the R condition, the differing renal responses are probably related to differing levels of volume expansion in the R vs. NR condition.

Animals↗
PubMed1990

Absence of diuresis during a 7-day saturation dive at 2.5 ATA N2-O2.

Three male divers were studied for 2 days during each of the predive and postdive 1 ATA air control periods and for 7 days at 2.5 ATA (2.3 ATA N2 and 0.2 ATA O2). The chamber temperature was always maintained at a comfort level. Average urine flow remained at 1500 ml.day-1 during both predive and 2.5 ATA periods; urine osmolality also remained constant at around 700 mOSM/kg. On the other hand, daily excretion of Na increased significantly from 139 mEq during the predive period to 178 mEq at 2.5 ATA (P less than 0.05) but returned to the predive level during the postdive period. In contrast, daily K excretion decreased progressively with a significant decrease during the postdive period (P less than 0.05). Plasma osmolality, Na, and K remained unchanged, whereas a 6% reduction of total protein concentration at 2.5 ATA (P less than 0.05) was observed. A quantitatively similar decrease (8%) was observed for hematocrit during the 2.5 ATA period, which did not recover at postdive. These changes were accompanied by a significant increase in urinary excretion of antidiuretic hormone (P less than 0.05) and by decreases in both plasma renin and aldosterone (P less than 0.05) level and urinary excretion of aldosterone (P less than 0.05). Plasma atrial natriuretic factor remained unchanged throughout the entire dive period.

Adult↗
PubMed1989

Interstitial and intravascular pressures in conscious dogs during head-out water immersion.

Water immersion (WI) causes an increase in plasma volume in humans and dogs. To determine the mechanism for this fluid movement, the transmission of external water hydrostatic pressure to the interstitial and vascular compartments was studied in six conscious dogs. Systemic arterial, central venous, peripheral arterial (ulnar artery) and venous (cephalic vein), pleural, intra-abdominal, and interstitial fluid hydrostatic (by Guyton's capsule and wick catheter method) pressures and external reference water pressure were measured at three different levels of WI: 1) extremities only, 2) midchest, and 3) midcervical levels at 37 degrees C. There was a significant linear relationship between interstitial fluid hydrostatic pressure (X) and external water pressure (Y): (Y = 0.86X + 1.4, r = 0.93 by Guyton's capsule; Y = 0.85X + 2.4, r = 0.93 by wick catheter. However, vascular pressures did not change when dogs were immersed at the level of the extremities. These pressures increased only during WI at the midchest and midcervical levels. Therefore the pressure gradient that develops between the interstitial and intravascular compartments is probably the major reason for the transcapillary fluid shift during WI.

Abdomen↗
PubMed1989

Size selected mRNA induces expression of P-aminohippurate transport in Xenopus oocytes.

Xenopus oocytes were injected with size-fractionated mRNA isolated from the renal cortex of rabbit kidney and after 4 days incubation, PAH uptake in oocytes injected with mRNA (0.7-1.3 kb) was 8 to 45 fold that of the water injected controls. The oocyte to medium ratio of accumulated PAH was 1.95. The Km and Vmax for transport were 333 microM and 66.6 nmoles.oocyte-1.min-1, respectively. This Km is similar to that reported for PAH transport in intact kidneys and slices. The uptake of PAH was unaffected by the absence of Na+ or the presence of probenecid. Expression of the transport represents the first step in an effort to clone and identify the gene for PAH transport.

Aminohippuric Acids↗
PubMed1989

Experimental exencephaly and myeloschisis in rats.

To elucidate the early sequential morphogenetic progress of exencephaly and myeloschisis, rat embryos whose mothers had been treated with hypervitaminosis A were studied at 1-day interval from gestation day 10.5 to 15.5. In exposed animals sequential change was found in both exencephaly and myeloschisis as the embryos grew up. The 10.5-day old exencephalic embryos had still widely open cephalic neural tubes. Exencephalic embryos older than 13.5 days of gestation showed strikingly severe eversion and overgrowth of the cephalic neuroepithelium, thus failed in forming normal primitive brain. The convex dorsal surface of the exencephaly was covered with ependyma, which was connected directly with surrounding surface eqithelium at the periphery. The earliest morphologically recognized myeloschisis was in the 13.5-day old embryos. In myeloschisis, divergence at the roof plate and eversion of the spinal neural tube, disorganized overgrowth of the neuroepithelium, malformed and misplaced spinal ganglia and nerve roots, and absence of the neural arch and dermal covering were characteristic. It is suggested that exencephaly results from failure of the cephalic neural tube closure which is followed by eversion and overgrowth of the neuroepithelium. And failure in closure of the posterior neuropore and disturbance in the development of the tail bud probably play major role in the morphogenesis of myeloschisis.

Animals↗
PubMed1989

Pathogenetic role of thyrotropin receptor antibody in the development of hyperthyroidism following primary hypothyroidism.

The authors measured thyrotropin binding inhibitory immunoglobulin (TBII), thyroid stimulating antibody (TSAb), and thyroid stimulation blocking antibody (TSBAb) sequentially in patients who developed hyperthyroidism following primary hypothyroidism, and compared changes in these various functional parameters of thyrotropin receptor antibody (TRAb) with clinical manifestations, in order to investigate the role of TRAb in the development of hyperthyroidism following primary hypothyroidism. In a patient with goitrous chronic thyroiditis, TBII, TSAb and TSBAb were not detected at the initial hypothyroid phase. But with appearance of TBII and TSAb, the patient developed hyperthyroidism. In a patient with primary nongoitrous myxedema, initially high TBII and TSBAb were detected without TSAb activity. His TSBAb disappeared and TSAb appeared with development of goiter growth and hyperthyroidism. These two mechanisms, that is, appearance of previously absent TSAb and conversion of TSBAb to TSAb, might play a causative role in the development of hyperthyroidism following primary hypothyroidism. These phenomena might be evidence that Graves' disease, chronic thyroiditis, and primary nongoitrous myxedema are on a continuing spectrum of a common syndrome sharing similar pathophysiology, at least with respect to TRAb.

Adult↗
PubMed1989

Mechanism of tolerance to renal ischemia in harbor seal: role of membranes.

Many diving animals are capable of engaging in long breath-hold dives. Investigations were undertaken to compare the active tubular transport of organic ions between kidney slices from harbor seals (Phoca vitulina) and rats (control) under anoxia or low pH or both. Para-aminohippurate (PAH) and tetraethylammonium (TEA) were used as a representative organic anion and cation, respectively. The slice-to-medium concentration ratios (S:M) of PAH (congruent to 2.5) in the harbor seal was not altered (unlike in the rat) after 60 min of incubation in a nitrogen atmosphere but was reduced to congruent to 1.0 in the presence of 10(-4) M 2,4-dinitrophenol. Subsequent studies also demonstrated that PAH uptake in the harbor seal was not influenced by pH of the incubation medium over a range of 6.0 to 7.4. In contrast, PAH uptake was very sensitive to the medium pH in the rat, decreasing significantly with reduction in pH. Although the TEA uptake decreased in anoxia in both species, it decreased considerably less in the harbor seal than in the rat (40 vs. 70%). However, TEA uptake decreased significantly at low pH in both species. The magnitudes of increase in intracellular Na and of decrease in intracellular K in anoxia were consistently less in the harbor seal than in the rat, especially at low pH. On the basis of these and other findings reported in the literature, cellular mechanisms for the remarkable ischemic tolerance of the seal kidney are discussed.

Animals↗
PubMed1988

Preparation of basolateral membranes that transport p-aminohippurate from primary cultures of rabbit kidney proximal tubule cells.

The organic anion p-aminohippurate (PAH) is specifically secreted by the renal proximal tubule. The possibility was examined that the probenecid sensitive PAH transport system (which is involved in this secretory process in renal proximal tubule cells in vivo) is retained in primary cultures of rabbit kidney proximal tubule cells. Significant 3H-PAH uptake into primary cultures of proximal tubule cells was observed. After 10 min, 150 pmole PAH/mg protein had accumulated intracellularly. Given an intracellular fluid volume of 10 microliter/mg protein, the intracellular PAH concentration was estimated to be 15 microM. The initial rate of PAH uptake (when 50 microM PAH was in the uptake buffer) was inhibited 50% by 2 mM probenecid. Intact monolayers also exhibited Na+-dependent alpha methyl-D-glucoside uptake (an apical marker). Basolateral membranes were purified from primary rabbit kidney proximal tubule cell cultures. Probenecid sensitive PAH uptake into the membrane vesicles derived from the primary cultures was observed. The rate of PAH uptake was equivalent to that obtained with vesicles obtained from the rabbit renal cortex. No significant Na+-dependent D-glucose uptake into the vesicles was observed, indicating that primarily basolateral membrane vesicles had indeed been obtained.

Aminohippuric Acids↗