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Y S Cheng

Publications and source records attributed to Y S Cheng.

At least 109 records · Page 6Linked to original sources
PubMed1986

Deposition of ultrafine aggregate particles in exercising rats.

The effect of exercise on particle deposition in rats was investigated. Twenty male rats were trained to run on a treadmill and were exposed to gallium-67 oxide (67Ga2O3) particles (0.1 micron activity median diffusion diameter) for 30 min while running at 30 m min-1. Twenty resting controls were exposed in the same system while confined in wire mesh cages. Ten exercising and 10 resting rats were killed 2 h and 12 days after exposure. Tissue radioactivity levels of 67Ga2O3 were measured and normalized for differences in exposure concentration and body weight. Significantly (P less than 0.05) more 67Ga was deposited in the nasal passages (20 vs 5 nCi) and in the trachea and mainstem bronchi (0.05 vs 0.03 nCi) of exercising rats than in resting rats. There were no significant differences between the exercising and resting rats in amounts of 67Ga in the lung lobes at 2 h after exposure. Using assumed minute volumes, exercising rats had a significantly (P less than 0.05) lower lung deposition efficiency, expressed as percentage of estimated inhaled material, than did resting rats (3 vs 10%). The results suggest that exercising rats inhale more ultrafine particles, but deposit a smaller fraction of them in their lungs. The result is a similar lung burden of 0.1 micron particles in resting and exercising animals.

Aerosols↗
PubMed1986

Disposition and metabolism of 14C-solvent yellow and solvent green aerosols after inhalation.

Solvent yellow (2-(2'-quinolinyl)-1,3-indandione) and solvent green (1,4-di-p-toluidinoanthraquinone) are components of colored smoke munitions and may become airborne and be inhaled by workers during the manufacture of the munitions. Little is known about the disposition of either dye after inhalation. To obtain this information, we exposed male F344/N rats to 14C-solvent yellow aerosols (160 nmol solvent yellow/liter air) or a mixture of 14C-solvent yellow and unlabeled solvent green (340 nmol solvent yellow and 370 nmol solvent green/liter air) for 60 min. After either exposure, solvent yellow was rapidly cleared from the respiratory tract, with a t1/2 of 2-3 hr. Solvent green was retained in the lungs with a minimum estimated t1/2 for clearance of 22 days. Solvent green was not detected in other tissues during the 70-hr postexposure period. After either exposure, high-pressure liquid chromatography analysis of tissues extracts indicated that 40 to 75% of the 14C in liver and kidney consisted of solvent yellow metabolites. Greater than 90% of the 14C in the lungs was unmetabolized solvent yellow. The major pathway for excretion of solvent yellow and solvent yellow metabolites was the feces (74% of the initial body burden); the t1/2 for excretion was 14 hr. Urinary 14C accounted for 14% of the initial body burden and the t1/2 for excretion was 10 hr. Over 90% of the 14C excreted in the urine was solvent yellow metabolites. Very little solvent yellow (2%) was metabolized to 14CO2. By 72 hr after exposure, only 10% of the initial 14C deposited remained in the body.

Aerosols↗
PubMed1986

Nonidentical induction of the guanylate binding protein and the 56K protein by type I and type II interferons.

Upon the addition of interferon (IFN) to cultured human cells, the expression of genes encoding the 56K and the guanylate binding protein (GBP) is specifically induced. We have analyzed their expression at the protein and the mRNA levels and studied how their regulation differs in cells treated with different IFNs. In the type I IFN (alpha and beta)-treated cells, we detected the accumulation of the 56K protein primarily in the cytoplasm. The 56K protein was undetectable in untreated cells or in cells treated with type II IFN (IFN-gamma). In contrast, a greater amount of GBP was synthesized in cells treated with type II IFN than in cells treated with type I IFN. The differential induction of these two proteins correlates well with the relative amounts of their mRNAs in type I and type II IFN-treated cells. In addition, the IFN-induced synthesis of the 56K protein was found in certain cell lines in which the GBP synthesis was not detected. These results suggest that the regulation of these two genes requires dissimilar factors which are activated or induced to different extents by type I and type II IFNs.

Adaptor Proteins, Signal Transducing↗
PubMed1986

Disposition and metabolism of [14C]dibenzo[c,g]carbazole aerosols in rats after inhalation.

Dibenzo[c,g]carbazole (DBC) is a nitrogen-containing polycyclic aromatic hydrocarbon that has been detected in tobacco tars, industrial oils, and diesel engine exhaust fumes. DBC is carcinogenic in respiratory tract tissue of hamsters and in lungs, kidneys, and livers of mice. The purpose of this research was to determine the respiratory tract deposition, distribution in tissues, metabolism, and excretion of DBC in rats after inhalation. Rats were exposed nose-only to 1.1 or 13 micrograms [14C]DBC/liter air for 60 min. Activity median aerodynamic diameters for the two concentrations of DBC ranged from 0.7 to 0.8 micron. Urine, feces, and selected tissues were collected for various times after exposure. The fractional deposition for the 1.1 and 13 micrograms/liter exposure concentrations was similar, 13 and 16%, respectively. The dominant route of excretion of 14C following exposure to either concentration of DBC was the feces, accounting for approximately 95% of the total 14C eliminated. Half-time for fecal excretion was 20 +/- 6 hr (means +/- SE). Gastrointestinal absorption of [14C]DBC was 43%. Radioactivity was widely distributed to all tissues examined, with the respiratory tract (lung, trachea, larynx, and nasal turbinates), upper gastrointestinal tract (stomach and small intestine), the liver, and the adrenals containing the highest concentrations of [14C]DBC equivalents within 1 hr after exposure. At both concentrations of DBC tested, clearance of 14C from tissues was rapid, with approximately 60 to 98% of the initial tissue burden being cleared with half-times ranging from 1 to 16 hr. The remaining 2 to 40% in the tissues was cleared with half-times that ranged from 1.5 to 14 days. Several metabolites were detected in the urine and feces, none of which appeared to be either glucuronide or sulfate conjugates. Small quantities of [14C]DBC were detected in the urine, although quantities were less than 1% of the initial respiratory tract burden of [14C]DBC. The results from this research indicate that DBC was rapidly absorbed from the lungs and translocated to many tissues. Prior to elimination, primarily in the feces, DBC was extensively metabolized. There appeared to be no effect of exposure concentration on the toxicokinetics of inhaled DBC.

Aerosols↗
PubMed1985

Affinity purification of an interferon-induced human guanylate-binding protein and its characterization.

Among the proteins that are synthesized only in interferon-treated human cells, a Mr = 67,000 protein has been previously identified by its binding to guanylate agaroses. After a 24-h treatment of human diploid fibroblasts with 200 units/ml of interferon-gamma, about 3 X 10(5) molecules of guanylate-binding protein (GBP) accumulate in each cell. We have developed a one-step purification procedures for GBP using guanylate affinity chromatography. To further elucidate the specific binding of this protein to guanylates, we have used a photoactive probe, 8-azidoguanosine [alpha 32P] triphosphate for the labeling of the GBP. Photolysis of the 8-azido-[alpha-32P]GTP in the presence of GBP results in the covalent attachment of the 32P-guanylate to the GBP. This photolabeling reaction can be inhibited only by guanylates but cannot be inhibited by other nucleotides, suggesting a specific association of GBP to guanylates. Using the purified GBP as an immunogen, we have successfully made rabbit antiserum for GBP. Both the GBP antigen and its guanylate-binding activity are detected only in the cytoplasm of interferon-treated human fibroblasts. The synthesis of the mRNA of GBP is also found in mice exposed to endogenous interferon and in interferon-treated human lymphocytes.

Animals↗
PubMed1985

Disposition and metabolism of 2,3-[14C]dichloropropene in rats after inhalation.

2,3-Dichloropropene (2,3-DCP) is a constituent of some commercially available preplant soil fumigants for the control of plant parasitic nematodes. Human exposure potential exists during manufacture of the chemicals or during bulk handling activities. The purpose of this investigation was to determine the disposition and metabolism of 2,3-[14C]DCP in rats after inhalation. Male Fischer-344 rats were exposed nose-only to a vapor concentration of 250 nmol 2,3-[14C]DCP/liter air (7.5 ppm; 25 degrees C, 620 Torr) for 6 hr. Blood samples were taken during exposure, and urine, feces, expired air, and tissues were collected for up to 65 hr after exposure. Urinary excretion was the major route of elimination of 14C (55% of estimated absorbed 2,3-DCP). Half-time for elimination of 14C in urine was 9.8 +/- 0.05 hr (means +/- SE). Half-time for elimination of 14C feces (17% of absorbed 2,3-DCP) was 12.9 +/- 0.14 hr (means +/- SE). Approximately 1 and 3% of the estimated absorbed 2,3-[14C]DCP were exhaled as either 2,3-[14C]DCP or 14CO2, respectively. Concentrations of 14C in blood increased during 240 min of exposure, after which no further increases in blood concentration of 14C were seen. 14C was widely distributed in tissues analyzed after a 6-hr exposure of rats to 2,3-[14C]DCP. Urinary bladder (150 nmol/g), nasal turbinates (125 nmol/g), kidneys (84 nmol/g), small intestine (61 nmol/g), and liver (35 nmol/g) were tissues with the highest concentrations of 14C immediately after exposure. Over 90% of the 14C in tissues analyzed was 2,3-DCP metabolites. Half-times for elimination of 14C from tissues examined ranged from 3 to 11 hr. The data from this study indicate that after inhalation 2,3-DCP is metabolized in tissues and readily excreted.

Allyl Compounds↗
PubMed1985

Uptake and excretion of [14C]methyl bromide as influenced by exposure concentration.

Methyl bromide is a widely used soil fumigant and poses potential inhalation hazard to workers. Uptake of methyl bromide and pathways for excretion of 14C were investigated in male Fischer-344 rats after nose-only inhalation of 50, 300, 5700, or 10,400 nmol (1.6 to 310 ppm) of [14C]methyl bromide/liter of air for 6 hr. Fractional uptake of methyl bromide decreased at the highest concentrations, 5700 and 10400 nmol/liter, with 37 and 27% of the inhaled methyl bromide absorbed, respectively, compared to 48% at the lower levels. This resulted in the same total amount of methyl bromide being absorbed at the two higher exposure concentrations (650 mumol/kg body wt). Total methyl bromide adsorbed was 9 or 40 mumol/kg body wt after exposure to 50 or 300 nmol/liter, respectively. Elimination of 14C was linearly related to the amount of methyl bromide absorbed as determined from urine, feces, expired CO2, and parent compound collected for 66 hr after the end of exposure. Exhaled 14CO2 was the dominant route of excretion, with from 1.2 to 110 mumol (50% of amount absorbed) exhaled, and was described by a two-component negative exponential function; 85% was exhaled with a t 1/2 of 4 hr, and the remaining 15% was exhaled with a t 1/2 of 17 hr. The rate of exhalation of 14CO2 was not affected by the amount of [14C]methyl bromide absorbed. From 0.4 to 54 mumol was excreted in urine (20% of amount absorbed). The half-time for excretion of 14C in urine was approximately 10 hr, and the rate of excretion was not dependent on the amount of [14C]methyl bromide absorbed. Little 14C was exhaled as methyl bromide (less than 4% of the dose) or excreted in feces (less than 2%). At the end of 66 hr, 25% of the 14C absorbed remained in the rats. Liver, kidneys, adrenals, lungs, thymus, and turbinates (maxilloturbinates, ethmoturbinates, and nasal epithelial membrane) contained the highest concentrations of 14C. Results indicated that uptake of inhaled methyl bromide could be saturated. Any [14C]methyl bromide equivalents absorbed, however, would be excreted by concentration-independent mechanisms.

Air Pollutants, Occupational↗
PubMed1985

Effect of vapor concentration on the disposition of inhaled 2,3-dichloropropene in Fischer-344 rats.

2,3-Dichloropropene (DCP) is an intermediate used in the manufacture of carbamate herbicides and there is potential for human exposure during the manufacturing process. DCP is a known mutagen in bacteria systems and some structural analogs of DCP are carcinogenic. Since little is known about the disposition of DCP in animals after inhalation, studies were conducted in male Fischer-344 rats to determine the effect of vapor concentration on absorption and excretion. Uptake and elimination of 14C was studied in rats after nose-only inhalation of 17, 240, or 1650 nmol of [14C]DCP vapor/liter of air (0.4, 6, or 40 ppm, respectively, at 760 mm and 25 degrees C) for 6 hr. The percentage of inhaled DCP absorbed averaged 38% and was not statistically different at any vapor concentration, although minute volume was lower during exposure to 1650 nmol/liter. Urine, feces, and expired air were collected from rats for 65 hr after exposure. Rats were sacrificed and tissues, carcass, excreta, and expired air were analyzed for 14C. Routes of 14C excretion were independent of vapor concentration, with 50% of the 14C excreted in urine, 13% in feces, approximately 7% as CO2, and less than 1% as DCP in expired air. Rates of 14C excretion were also independent of vapor concentration, with the half-times averaging 9.9 hr (urine), 13.6 hr (feces), and 0.9 hr (14CO2). Sixty hours after inhalation, 29% of the initial body burden of 14C remained in the carcass. Most was associated with the pelt, but some 14C was found in all tissues. Respiratory tract, GI tract, liver, and kidney were tissues with the highest 14C contents. The results indicate that DCP metabolism and excretion rates are relatively constant throughout the vapor concentration range studied. This suggests that results from more detailed pharmacokinetic studies (and possibly toxicity studies) at one DCP concentration may be extrapolated to other concentrations within this range.

Absorption↗
PubMed1985

Use of a jet mill for dispersing dry powder for inhalation studies.

Compressed air-powered jet mills are used in the chemical and food industries for grinding and classifying powders. We adapted one type of these fluid energy mills as a powder generator for inhalation experiments. The generating system included a jet mill and a screw feeder, the jet mill consisting of an elongated channel, a feeding jet to deliver the material into the channel, and two high-speed air jets. High speed air circulating in the channel created turbulence and centrifugal forces to disperse powder. The jet mill used can be operated from 25 to 100 psig at flow rates of 300 to 900 L/min. Two test materials--a solvent yellow dye and a dye mixture of solvent green and solvent yellow--were used. Both dyes were soft and sticky and could not be dispersed with several other powder generators tested at the concentrations required for toxicity studies. Aerosol concentrations ranging from 10 to 1500 mg/m3 at a flow rate of 400 L/min were obtained by adjusting the feed rate to the jet mill. Stability of aerosol concentration during six-hour continuous generation was 15 to 20%. Comparisons of several generators for producing sticky organic powders are also discussed.

Aerosols↗
PubMed1984

Transcriptional induction of two genes in human cells by beta interferon.

The binding of interferons to distinct cell surface receptors leads to the induction of synthesis of several unique polypeptides and their corresponding mRNAs (1-6). We have isolated two cDNAs that are complementary to nuclear RNA whose synthesis is induced from undetectable levels to maximal rates of transcription within 30-60 min after the addition of beta interferon to human fibroblasts or to HeLa cells. These results prove that a single polypeptide can, by binding to a specific plasma membrane receptor, promptly activate the transcription of a defined set of genes.

DNA↗
PubMed1984

Characterization of diesel exhaust in a chronic inhalation study.

We describe characterization of the exposure atmosphere in a life-span study of rats and mice exposed to chronic inhalation of diluted diesel exhaust. Diesel exhaust was generated by one of two General Motors 1980 Model, 5.7-liter V8 diesel engines connected to an eddy current dynamometer/flywheel system and operated on the Federal Test Procedure urban driving cycle. Animals were exposed 7 hours/day, 5 days/week to exhaust at particle concentrations of approximately 7000, 3500, and 350 micrograms/m3 or to clean air. Throughout the 24-month study, the mean particle mass concentration remained within 5% of the target values. Measured gas concentrations of CO, CO2, NO, NO2, and hydrocarbons were roughly proportional to the dilution ratio. A combination of a Lovelace Multijet cascade impactor followed by a parallel flow diffusion battery gave mass median diameters of 0.23 to 0.26 microns averaged over complete cycles and geometric standard deviations larger than 4. The aerosol concentration profile was associated with the operating cycle. The measured diesel particle size was similar to previously reported values of particles released to the atmosphere from the same model engine.

Animals↗
PubMed1983

Interferon induction of fibroblast proteins with guanylate binding activity.

Treatment of human diploid fibroblastic cells with interferon induces the synthesis of two guanylate binding proteins (GBP) with molecular weights of 67,000 and 56,000. The Mr = 67,000 protein (67K GBP) is synthesized upon treatment with either alpha-, beta-, or gamma-interferon. Among these interferons, gamma-interferon induces a higher level of 67K GBP synthesis. The 67K GBP synthesized in either beta- or gamma-interferon-treated cells has two charge forms with isoelectric points of 6.0 and 5.8, respectively. The synthesis of the Mr = 56,000 protein is induced by the treatment using either alpha- or beta-interferon, but its synthesis in gamma-interferon-treated cells is undetectable. The amounts of the radioactive GBPs synthesized in human fibroblasts are proportional to the amounts of the purified beta-interferon used for the inductions. Syntheses of GBPs require the transcription of cellular genes because their syntheses are completely blocked by actinomycin D treatments. The mRNA for the 67K GBP is found in fibroblasts that are treated by either alpha-, beta-, or gamma-interferon, but it is not detected in untreated cells. More 67K GBP mRNA is accumulated in the gamma-interferon-treated than in alpha- or beta-interferon-treated fibroblasts. This is consistent with more 67K GBP synthesis found in gamma-interferon-treated fibroblasts.

Cell Line↗
PubMed1983

Characterization of a phosphotyrosyl protein phosphatase activity associated with a phosphoseryl protein phosphatase of Mr = 95,000 from bovine heart.

A cytosolic phosphoprotein phosphatase of Mr = 95,000 purified from bovine cardiac muscle, which contains a catalytic subunit of Mr = 35,000, is known to be associated with a Mg2+-activated p-nitrophenyl phosphatase activity. We have found that the enzyme preparation is also active toward phosphotyrosyl-IgG and -casein phosphorylated by pp60v-src, the transforming gene product of Rous sarcoma virus. The properties of this phosphotyrosyl protein phosphatase activity closely resemble those of the p-nitrophenyl phosphatase activity but sharply differ from those of the phosphorylase phosphatase activity. Comparative studies of the activities of the Mr = 95,000 phosphatase, bovine kidney alkaline phosphatase, and ATP X Mg-dependent phosphatase toward phosphoseryl, phosphothreonyl, and phosphotyrosyl proteins and p-nitrophenyl phosphate under various conditions have been carried out. The results indicate that the Mr = 95,000 enzyme exhibits higher activity toward phosphoseryl and phosphothreonyl proteins than toward phosphotyrosyl proteins, while the kidney alkaline phosphatase preferentially dephosphorylates phosphotyrosyl proteins. ATP X Mg-dependent phosphatase is inactive toward phosphotyrosyl proteins.

Animals↗