Biomedical subjects

X C Jiang

Publications and source records attributed to X C Jiang.

At least 37 records · Page 2Linked to original sources

PubMed1999

[Studies on hereditary variations of millet seed after high altitude balloon flight].

OBJECTIVE: To select high yield, high protein and fatty acid millet. METHOD: Air-dried seeds of millet were carried by high altitude balloon (HAB) for 8 h. Botany characteristics of these seeds were analyzed and studied after recovery. RESULT: Germinating potential rose 21.1%, germinating percentage reduced 5.2% as compared with the control; plant height was 6.8 cm lower than that of the control in SP1; while flag-leaf area and spike weight were 25% and 15.9% higher than those of the control respectively. Large-spike strains were stable in SP3 pregeny. In SP3(-2), the contents of seed protein and fatty acid were more than those of control; in SP3(-5), the average spike length was 5.8 cm, and the content of Fe element in seed was 61.5 mg/kg more than these of control; in SP4 superspike strains, spike character, chlorophyll content and photosynthetic rate were significantly higher than the control during growing phase and growing anaphase, photosynthetic rate in flag-leaf was over 27.9% higher than those in the control. CONCLUSION: New strains with high protein and fatty acid and high yield could be selected by HAB. The characteristics of these variations in the new strain is hereditable.

Chlorophyll↗

PubMed1999

[Development and prospect of plant mutation breeding induced by aviation and spaceflight in China].

Since 1987, about fifty species, three hundred varieties of crops have been sent in recoverable satellites or high altitude balloon (HAB). The selected lines include a high-yield, disease-resist, and hybrid-vigorous rice line, a recovered line of Japonica rice restoring sterility of Indica rice, a new green pepper strain which grows fruits over 500 g, a disease-resist, high-quality tomato line, a big-pod rape line, a big-fruit white lotus line and a big-bulb lily. The special conditions in the outer space can induce a variety of mutations in the plants and their progeny, which provides a new way for the plant breeding.

Agriculture↗

PubMed1998

Expression of plasma phospholipid transfer protein mRNA in normal and emphysematous lungs and regulation by hypoxia.

The lung is the major site expressing plasma phospholipid transfer protein (PLTP) mRNA in humans and mice, suggesting that this protein might have an important role in maintaining normal function of this organ. In the lung of human collagenase transgenic mice, an emphysematous animal model, PLTP mRNA was 3-fold higher than in control mice. However, the mRNA in other tissues was not changed. To further assess the expression and function of PLTP, we measured PLTP mRNA level in lung tissue of two emphysematous patients and found that the mRNA was 4-fold higher than in control subjects. In situ hybridization on mouse lung suggested positive staining in alveolar type II epithelial cells. In addition, immortalized rat alveolar pre-type II epithelial cells and freshly isolated mature rat alveolar type II epithelial cells both highly expressed PLTP mRNA, and the former cells actively secreted PLTP activity into the medium. To examine the possible mechanisms leading to high levels of PLTP expression in vivo, we exposed the pre-type II cells to hypoxia and demonstrated induction of PLTP mRNA and a coordinate increase in secreted PLTP activity. Thus, the PLTP gene is highly expressed in alveolar type II epithelial cells and is induced during hypoxia and in emphysema. These observations suggest that a hypoxic stimulus occurring in emphysema may be a novel mechanism that contributes to enhanced expression of PLTP.

Animals↗

PubMed1997

L-arginine prevents xanthoma development and inhibits atherosclerosis in LDL receptor knockout mice.

BACKGROUND: The potential antiatherosclerotic actions of NO were investigated in four groups of mice (n = 10 per group) lacking functional LDL receptor genes, an animal model of familial hypercholesterolemia. Group 1 was fed a regular chow diet. Groups 2 through 4 were fed a 1.25% high-cholesterol diet. In addition, group 3 received supplemental L-arginine and group 4 received L-arginine and N omega-nitro-L-arginine (L-NA), an inhibitor of NO synthase (NOS). METHODS AND RESULTS: Animals were killed at 6 months; aortas were stained with oil red O for planimetry and with antibodies against constitutive and inducible NOSs. Plasma cholesterol was markedly increased in the animals receiving the high-cholesterol diet. Xanthomas appeared in all mice fed the high-cholesterol diet alone but not in those receiving L-arginine. Aortic atherosclerosis was present in all mice on the high-cholesterol diet. The mean atherosclerotic lesion area was reduced significantly (P < .01) in the cholesterol-fed mice given L-arginine compared with those receiving the high-cholesterol diet alone. The mean atherosclerotic lesion area was significantly larger (P < .01) in cholesterol-fed mice receiving L-arginine + L-NA than in those on the high-cholesterol diet alone. Within the atherosclerotic plaques, endothelial cells immunoreacted for endothelial cell NOS; macrophages, foam cells, and smooth muscle cells immunostained strongly for inducible NOS and nitrotyrosine residues. CONCLUSIONS: The data indicate that L-arginine prevents xanthoma formation and reduces atherosclerosis in LDL receptor knockout mice fed a high-cholesterol diet. The abrogation of the beneficial effects of L-arginine by L-NA suggests that the antiatherosclerotic actions of L-arginine are mediated by NOS. The data suggest that L-arginine may be beneficial in familial hypercholesterolemia.

Animals↗

PubMed1996

Profound induction of hepatic cholesteryl ester transfer protein transgene expression in apolipoprotein E and low density lipoprotein receptor gene knockout mice. A novel mechanism signals changes in plasma cholesterol levels.

The plasma cholesteryl ester transfer protein (CETP) mediates the transfer of cholesteryl esters from HDL to other lipoproteins and is a key regulated component of reverse cholesterol transport. Dietary hypercholesterolemia results in increased hepatic CETP gene transcription and higher plasma CETP levels. To investigate the mechanisms by which the liver senses hypercholesterolemia, mice containing a natural flanking region CETP transgene (NFR-CETP transgene) were bred with apo E or LDL receptor gene knockout mice (E0 or LDLr0 mice). Compared to NFR-CETP transgenic (Tg) mice with intact apo E genes, in NFR-CETP Tg/E0 mice there was an eightfold induction of plasma CETP levels and a parallel increase in hepatic CETP mRNA levels. Other sterol-responsive genes (LDL receptor and hydroxymethyl glutaryl CoA reductase) also showed evidence of altered regulation with decreased abundance of their mRNAs in the E0 background. A similar induction of plasma CETP and hepatic CETP mRNA levels resulted from breeding the NFR-CETP transgene into the LDL receptor gene knockout background. When placed on a high cholesterol diet, there was a further increase in CETP levels in both E0 and LDLr0 backgrounds. In CETP Tg, CETP Tg/E0, and CETP Tg/LDLr0 mice on different diets, plasma CETP and CETP mRNA levels were highly correlated with plasma cholesterol levels. The results indicate that hepatic CETP gene expression is driven by a mechanism which senses changes in plasma cholesterol levels independent of apo E and LDL receptors. Hepatic sterol-sensitive genes have mechanisms to sense hypercholesterolemia that do not require classical receptor-mediated lipoprotein uptake.

Animals↗

PubMed1996

Structure-function relationships of human cholesteryl ester transfer protein: analysis using monoclonal antibodies.

Cholesteryl ester transfer protein (CETP), a 476 amino acid glycoprotein, mediates cholesteryl ester (CE), triglyceride, and phospholipid transfer among plasma lipoproteins. A monoclonal antibody (mAb), TP2, specific for an epitope within the last 26 amino acids of CETP has been shown to block all CETP-mediated lipid transfer, apparently by limiting access to lipid-binding sites in the carboxy terminal of CETP. A new panel of 16 anti-human CETP mAbs has now been used to further probe the structure-function relationships of CETP. Of the new mAbs, 9 partially inhibit CETP-mediated CE transfer (24-43%) from HDL to LDL. The corresponding epitopes were mapped within the CETP primary structure by the reactivity of the mAbs with CETP variants having deletions or amino acid substitutions. Of the 9 new, neutralizing mAbs, 6 are specific for epitopes situated between residues 410-450 and two others for epitopes between residues 184-260 and 332-366, respectively. The epitope of one neutralizing mAbs could not be mapped. Therefore, binding of mAbs to epitopes situated in four non-overlapping regions within CETP primary structure that are separated by as many as 280 residues can neutralize CETP-mediated CE transfer. Epitopes of mAbs that do not influence CE transfer activity map to the regions 184-260, 261-331, and 367-409, respectively. When pairs of mAbs were tested for their abilities to mutually compete for binding to immobilized CETP, competition was observed for mAbs specific for epitopes that are distant in CETP primary structure. The cross-competition patterns demonstrate that the carboxy terminal 60% of CETP adopts a compact structure. Together with previous mutagenesis studies, the data suggests that a carboxy terminal neutral lipid binding domain may be in close proximity to a lipoprotein binding region within native CETP.

Animals↗

PubMed1995

Regulation of murine plasma phospholipid transfer protein activity and mRNA levels by lipopolysaccharide and high cholesterol diet.

Plasma phospholipid transfer protein mediates the net movement of phospholipids between lipoproteins and between lipid bilayers and high density lipoprotein. In this study, the mouse phospholipid transfer protein cDNA was cloned by reverse transcription polymerase chain reactions based on the cDNA sequence of human phospholipid transfer protein. The predicted amino acid sequence of mouse phospholipid transfer protein shows the protein to be 476 amino acids long and to have a sequence identity of 83% with that of human phospholipid transfer protein. Mouse plasma phospholipid transfer protein activity is 1.5-2 times that of human plasma phospholipid transfer protein activity. As in humans, mouse peripheral tissues displayed a higher abundance of phospholipid transfer protein mRNA than observed in central organs. The order of phospholipid transfer protein mRNA expression was as follows: lung > adipose tissue, placenta, testis > brain > muscle, heart, liver. We examined the regulation of phospholipid transfer protein expression by dietary cholesterol and by bacterial lipopolysaccharide. A high fat, high cholesterol diet caused a significant increase (35%) in plasma phospholipid transfer protein activity and a significant increase (18%) in high density lipoprotein phospholipids. This increased activity was accompanied by approximately 100% increase in phospholipid transfer protein mRNA in lung. After lipopolysaccharide injection, plasma phospholipid transfer protein activity was decreased by approximately 66%. This decrease in activity was associated with a similar decrease in phospholipid transfer protein mRNA in lung, adipose tissue, and liver. The decrease in plasma phospholipid transfer protein activity was also associated with a significant increase (17%) in high density lipoprotein phospholipid concentration. The opposite changes in phospholipids levels with lipopolysaccharide treatment and dietary cholesterol despite similarly increased high density lipoprotein phospholipids levels indicate that high density lipoprotein phospholipids levels are likely determined both by phospholipid transfer protein levels and by gradients of phospholipids concentration between high density lipoprotein and other phospholipids sources.

Amino Acid Sequence↗

PubMed1995

Point mutagenesis of positively charged amino acids of cholesteryl ester transfer protein: conserved residues within the lipid transfer/lipopolysaccharide binding protein gene family essential for function.

The cholesteryl ester transfer protein (CETP) binds to plasma lipoproteins and transfers neutral lipids between them. Previous studies showed that lipoprotein binding involves ionic interactions between CETP and lipoproteins, with increased binding of CETP to lipoproteins carrying increased negative charge. In order to understand the molecular determinants of lipoprotein binding in CETP, site-directed mutagenesis was carried out on positively charged amino acids within and outside regions of conserved sequence in the putative family of lipid transfer/lipopolysaccharide (LPS) binding proteins (LT/LBP). Within the conserved regions, two mutant proteins, K233A and R259D, were well secreted by the transfected cells but showed markedly reduced cholesteryl ester transfer activity. Separating the bound from free CETP by gel filtration after incubation with HDL, HDL binding by K233A was found to be impaired, suggesting that the binding deficiency of the mutant may be responsible for decreased transfer activity. Kinetic analysis showed a marked increase in the apparent Km but no change in Vmax, consistent with a lipoprotein binding defect. Thus, within CETP, K233 and R259 play an essential role in cholesteryl ester transfer activity probably by mediating binding of CETP to lipoproteins. Sequence alignment of CETP, phospholipid transfer protein, LPS binding protein, and bactericidal permeability-inducing protein showed that K223 and R259 were strictly conserved as positively charged amino acids, suggesting a common function within the LT/LBP gene family.

Acute-Phase Proteins↗

PubMed1995

Decreased cholesteryl ester transfer protein (CETP) mRNA and protein and increased high density lipoprotein following lipopolysaccharide administration in human CETP transgenic mice.

The plasma cholesteryl ester transfer protein (CETP) mediates the exchange of HDL cholesteryl esters (CE) and VLDL triglycerides leading to catabolism of HDL. There is some evidence that HDL ameliorates the toxicity of LPS, and LPS is known to influence several enzymes affecting HDL metabolism. Therefore, the effects of LPS on CETP and plasma lipoproteins were examined in human CETP transgenic mice. Administration of LPS to mice expressing a CETP transgene linked to its natural flanking sequences (NFR-CETP Tg) resulted in a rapid marked decrease in hepatic CETP mRNA and plasma CETP concentration. Corticosteroid injection produced a similar decrease in hepatic CETP mRNA and adrenalectomy abolished this response to LPS. LPS caused disproportionate reductions in plasma CETP activity compared to mass, and was found to be a potent inhibitor of CETP activity when added directly to plasma. LPS was injected into mice expressing (A) a human apoA-I transgene, (B) apoA-I and NFR-CETP transgenes, or (C) apoA-I and LPS-inducible metallothionein promoter-driven CETP transgenes, producing (A) minimal changes in HDL cholesterol, (B) decreased plasma CETP and increased HDL cholesterol, and (C) increased plasma CETP and decreased HDL cholesterol. Thus, LPS administration produces a profound decrease in hepatic CETP mRNA, primarily as a result of adrenal corticosteroid release. The decrease in plasma CETP activity after LPS administration may reflect both this effect as well as a direct interaction between CETP and LPS. The decrease of CETP in response to LPS has major effects on HDL levels, and may represent an adaptive response to preserve or increase HDL and thereby modify the response to LPS.

Animals↗

PubMed1994

Genetic cholesteryl ester transfer protein deficiency caused by two prevalent mutations as a major determinant of increased levels of high density lipoprotein cholesterol.

Genetic determinants of HDL cholesterol (HDL-C) levels in the general population are poorly understood. We previously described plasma cholesteryl ester transfer protein (CETP) deficiency due to an intron 14 G(+1)-to-A mutation(Int14 A) in several families with very high HDL-C levels in Japan. Subjects with HDL-C > or = 100 mg/dl (n = 130) were screened by PCR single strand conformational polymorphism analysis of the CETP gene. Two other mutations were identified by DNA sequencing or primer-mediated restriction map modification of PCR products: a novel intron 14 splice donor site mutation caused by a T insertion at position +3 from the exon14/intron14 boundary (Int14 T) and a missense mutation (Asp442 to Gly) within exon 15 (D442G). The Int14 T mutation was only found in one family. However, the D442G and Int14 A mutations were highly prevalent in subjects with HDL-C > or = 60 mg/dl, with combined allele frequencies of 9%, 12%, 21% and 43% for HDL-C 60-79, 80-99, 100-119, and > or = 120 mg/dl, respectively. Furthermore, prevalences of the D442G and Int14 A mutations were extremely high in a general sample of Japanese men (n = 236), with heterozygote frequencies of 7% and 2%, respectively. These two mutations accounted for about 10% of the total variance of HDL-C in this population. The phenotype in a genetic compound heterozygote (Int14 T and Int14 A) was similar to that of Int14 A homozygotes (no detectable CETP and markedly increased HDL-C), indicating that the Int14 T produces a null allele. In four D442G homozygotes, mean HDL-C levels (86 +/- 26 mg/dl) were lower than in Int14 A homozygotes (158 +/- 35 mg/dl), reflecting residual CETP activity in plasma. In 47 D442G heterozygotes, mean HDL-C levels were 91 +/- 23 mg/dl, similar to the level in D442G homozygotes, and significantly greater than mean HDL-C levels in Int14 A heterozygotes (69 +/- 15 mg/dl). Thus, the D442G mutation acts differently to the null mutations with weaker effects on HDL in the homozygous state and stronger effects in the heterozygotes, suggesting dominant expression of a partially defective allele. CETP deficiency, reflecting two prevalent mutations (D442G and Int14 A), is the first example of a genetic deficiency state which is sufficiently common to explain a significant fraction of the variation in HDL-C in the general population.

Adult↗

PubMed1993

Down-regulation of mRNA for the low density lipoprotein receptor in transgenic mice containing the gene for human cholesteryl ester transfer protein. Mechanism to explain accumulation of lipoprotein B particles.

To evaluate the effects of cholesteryl ester transfer protein (CETP) on apoB-containing lipoproteins, we analyzed plasma lipoproteins from three different lines of human CETP transgenic mice, with plasma CETP concentration ranging from low (1.5 microgram/ml) to high levels (8.5 micrograms/ml). With increasing CETP concentration, very low density lipoprotein and low density lipoprotein (LDL) cholesteryl ester (CE) and apoB were progressively increased, and high density lipoprotein CE was decreased. To investigate the mechanism of accumulation of lipoproteins containing apoB (lipoprotein B), the abundance of hepatic LDL receptor mRNA was determined. LDL receptor mRNA was reduced as a result of CETP expression, with maximum repression to about 48% of the level of non-transgenic mice. Among the different lines of CETP transgenic mice there was an inverse relationship between plasma CETP concentration and hepatic LDL receptor mRNA abundance (r = -0.94, p < 0.01). CETP expression also led to increased cholesterol and cholesteryl ester content in liver and to decreased abundance of mRNAs encoding 3-hydroxy-3-methylglutaryl-coenzyme A reductase and 7-alpha-hydroxylase. Thus, CETP expression results in increased cholesteryl ester concentration in very low density lipoprotein and LDL, probably reflecting both CE transfer from high density lipoprotein and accumulation of lipoprotein B particles. The accumulation of lipoprotein B particles results from CETP-mediated down-regulation of liver LDL receptors, possibly due to enhanced return of cholesterol to the liver.

Animals↗

PubMed1993

Electrophysiological analysis of the nasal chemical senses in garter snakes.

Electroolfactogram and electrovomeronasogram recordings were made from garter snakes stimulated with vapor of amyl acetate, butanol and of earthworm wash. The olfactory epithelium was more sensitive than the vomeronasal epithelium to all three stimuli. Volatiles from prey washes were capable of stimulating the olfactory epithelium when delivered as airstreams. The vomeronasal epithelium was sensitive only to the air delivery of vapor of amyl acetate. Single unit recordings from the mitral cell layer of the accessory olfactory bulb of garter snakes were made in response to liquid delivery of a variety of chemical stimuli including classical odorants, amino acids and proteins derived from prey. All three classes of stimuli altered unit firing in the accessory olfactory bulb. Amyl acetate, earthworm wash, goldfish wash and non-volatile amino acids delivered as liquid stimuli to the vomeronasal epithelium produced responses in the accessory olfactory bulb that were more distinct and reliable than the electrovomeronasogram responses to airborne odorants recorded at the periphery. Both excitatory and inhibitory responses were observed in the accessory olfactory bulb of garter snakes. The direction of the response to a given stimulus differed for different neurons. Responses were frequently biphasic and could last longer than 50 seconds. Individual neurons responded to different classes of stimuli suggesting that they are broadly tuned.

Animals↗

PubMed1993

Chemical and immunological analysis of prey-derived vomeronasal stimulants.

We have isolated seven proteins from earthworm preparations that are chemoattractive to garter snakes. Three of these proteins have been purified to homogeneity: two from aqueous earthworm wash (EWW) and one from electric shock-induced earthworm secretion (ESS). One of the two highly purified proteins from EWW has a relative molecular mass of 20 kDa and contains free sulfhydryl groups that appear to play a functional role in its chemoattractivity. The other purified protein from EWW has a molecular mass of 3 kDa (low molecular weight protein, LMW). The highly purified chemoattractive protein (ES20) from ESS is a glycoprotein having a minimum molecular mass of 15.4 kDa calculated from its amino acid and carbohydrate contents. It consists of a single polypeptide chain. The sequence of terminal 15 amino acid residues from its amino (NH2-) terminal has been determined. It binds specifically to the membranes of vomeronasal sensory epithelium in a saturable and reversible fashion with a Kd value of about 0.3 microM and Bmax value of 0.4 nmol/mg of protein. This protein causes an increase in firing rate of individual neurons in the accessory olfactory bulb of garter snakes, the projection site for vomeronasal neurons. All the isolated chemoattractive proteins from both earthworm preparations can be divided immunologically into three groups: (i) those closely related to the ES20 snake-attractive protein, (ii) those closely related to the LMW snake-attractive protein, and (iii) those unrelated to either ES20 or the LMW protein.

Amino Acids↗

PubMed1993

A missense mutation in the cholesteryl ester transfer protein gene with possible dominant effects on plasma high density lipoproteins.

Plasma HDL are a negative risk factor for atherosclerosis. Cholesteryl ester transfer protein (CETP; 476 amino acids) transfers cholesteryl ester from HDL to other lipoproteins. Subjects with homozygous CETP deficiency caused by a gene splicing defect have markedly elevated HDL; however, heterozygotes have only mild increases in HDL. We describe two probands with a CETP missense mutation (442 D:G). Although heterozygous, they have threefold increases in HDL concentration and markedly decreased plasma CETP mass and activity, suggesting that the mutation has dominant effects on CETP and HDL in vivo. Cellular expression of mutant cDNA results in secretion of only 30% of wild type CETP activity. Moreover, coexpression of wild type and mutant cDNAs leads to inhibition of wild type secretion and activity. The dominant effects of the CETP missense mutation during cellular expression probably explains why the probands have markedly increased HDL in the heterozygous state, and suggests that the active molecular species of CETP may be multimeric.

Aged↗

PubMed1992

The CCAAT/enhancer-binding protein trans-activates the human cholesteryl ester transfer protein gene promoter.

The plasma cholesteryl ester transfer protein (CETP), primarily synthesized in the liver of several species, is expressed at very low levels in a number of transformed human liver cell lines. The human CETP gene promoter contains a sequence that closely resembles the binding site for the transcription factor CCAAT/enhancer-binding protein (C/EBP). This site is capable of binding C/EBP, as shown by electrophoretic mobility shift and DNase I footprint analyses. Transient expression of the bacterial chloramphenicol acetyltransferase gene under the control of the human CETP gene promotor gave low activities in the human hepatoma cell line, HepG2. However, in the presence of C/EBP, CAT activity was markedly elevated indicating that CETP gene promoter activity was enhanced. In primary cultures of isolated hepatocytes, CETP mRNA was lost rapidly and in parallel with the C/EBP mRNA. C/EBP may play an important role in the proper maintenance of CETP gene promoter activity, and its low levels in proliferating or cultured cells may account for the low level of the CETP gene expression in immortalized human liver cell lines or cultured hepatocytes.

Animals↗

PubMed1992

Dietary cholesterol increases transcription of the human cholesteryl ester transfer protein gene in transgenic mice. Dependence on natural flanking sequences.

To investigate the regulation of expression of the human cholesteryl ester transfer protein (CETP) gene, transgenic mice were prepared using a CETP minigene linked to the natural flanking sequences of the human CETP gene. By using a transgene containing 3.2 kb of upstream and 2.0 kb of downstream flanking sequence, five different lines of transgenic mice were generated. The abundance of CETP mRNA in various tissues was determined on standard laboratory diet or high fat, high cholesterol diets. In three lines of transgenic mice the tissues expressing the human CETP mRNA were similar to those in humans (liver, spleen, small intestine, kidney, and adipose tissue); in two lines expression was more restricted. There was a marked (4-10-fold) induction of liver CETP mRNA in response to a high fat, high cholesterol diet. The increase in hepatic CETP mRNA was accompanied by a fivefold increase in transcription rate of the CETP transgene, and a 2.5-fold increase in plasma CETP mass and activity. In contrast, CETP transgenic mice, in which the CETP minigene was linked to a metallothionein promoter rather than to its own flanking sequences, showed no change in liver CETP mRNA in response to a high cholesterol diet. Thus (a) the CETP minigene or natural flanking sequences contain elements directing authentic tissue-specific expression; (b) a high cholesterol diet induces CETP transgene transcription, causing increased hepatic CETP mRNA and plasma CETP; (c) this cholesterol response requires DNA sequences contained in the natural flanking regions of the human CETP gene.

Animals↗

PubMed1992

[Histopathological and immunopathological studies on experimental pulmonary candidiasis].

Experimental pulmonary candidiasis was produced by intratracheal inoculation of candida albicans in mice. The pathological changes could be divided into two stages, dominated by polymorphonuclear leukocyte infiltration and granuloma formation respectively. Preincubation of C. albicans with mouse anti-C. albicans antibody showed no obvious effect on pathological changes of the lungs as compared with the changes in the control mice, indicating that specific antibody did not play a crucial role in the defence mechanism of the lungs against C. albicans infection in normal mice. In the mice injected with antineoplastic drugs and hormones, abundant pseudohyphae were found in the lungs. Tissue necrosis and hemorrhage were obvious.

Animals↗

PubMed1992

[Oxygen-lactated Ringer's solution for surgical patients].

The effects of intravenous infusion of the lactated Ringer's solution inflated with oxygen (Oxygen-LR) and lactated Ringer's solution (LR) on oxygenation of blood were studied in 23 patients undergoing abdominal surgery under epidural anesthesia. LR 1000 ml was infused with inflated oxygen at 1L/min in 30 minutes in the oxygen-LR group (n = 12). The partial pressure of oxygen-LR was increased to 600.45 +/- 78.78 from 129.4 +/- 9.69 mmHg. LR 1000 ml was infused in 30 minutes in the control group (n = 11). There was no significant difference in PaO2, PaCO2, SatO2, A-aDO2 during and 30 minutes after infusion between the oxygen-LR and control groups. We believe that oxygen-LR is of no clinical value because of its low ability is of no carrying oxygen.

Adolescent↗