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Biomedical subjects

J B Li

Publications and source records attributed to J B Li.

At least 37 records · Page 2Linked to original sources
PubMed1991

[Changes in hemorheology of traumatic optic nerve atrophy].

Whole blood viscosity (WBV), plasma viscosity (PV), hematocrit, erythrocyte sedimentation rate (ESR) and fibrinogen were assayed in 20 patients with traumatic optic nerve atrophy. The results of each item in the above examinations has been compared with that of the control group. It has been demonstrated that WBV, PV, ESR and fibrinogen in the patient group were significantly higher than that in the control group (P less than 0.01). But the ESR and fibrinogen of the treatment group were significantly lower than that in the pretreatment group (P less than 0.01). The authors suggest that the result of changes in hemorheology of traumatic optic nerve atrophy is a kind of reverse phenomenon.

Adult↗
PubMed1991

[Scanning electron microscopic observations on Clonorchis sinensis cercariae].

The surface structure of Clonorchis sinensis cercariae was observed under scanning electron microscope. The cercaria was of the parapleuro-lophocercous type. The measurements of the cercariae were as follows: body 137-240 x 62-90 microns, tail 320-470 x 21-34 microns, oral sucker 27-46 x 23-33 microns. The ventral sucker was incompletely developed and much smaller than the oral one. The whole body surface was covered with backward pointing spines. Four horizontal rows of oral spines were found around the mouth opening of the oral sucker. These spines diminished in size with the distance of the rows from the opening and their numbers were 12, 18, 19 and 18 respectively. Transverse and longitudinal plicae formed from tegument were found on the surface of the tail, being in connection with dorsal and ventral fins along posterior half of the tail. Many sensory structures or papillae were observed on the body. They were of three different types: 1) papillae with long or short cilia distributed widely on the body surface and around the mouth opening, the number of papillae with cilia on the body surface being greater than that described by Komiya et al (1940); 2) a few sensory fossa on the tail, measuring 1.0 x 0.6 microns; 3) a few ring-type papillae with knob on the body surface with pore of 0.5 micron in diameter.

Animals↗
PubMed1991

[Treatment of peptic ulcer with jian-wei yu-wang tablets].

This article reports the results of second stage clinical trial on the treatment of peptic ulcer with jian-wei yu-yang (JWYY) tablets in comparison with a control group treated with ranitidine. The results showed that the cure rate for JWYY tablet group was 62.4% and its effective rate was 93. 8% in 354 cases, whereas the cure rate of the control group was 50.7% and its effective rate was 86. 4% in 140 cases. The differences between these two groups were highly significant (P less than 0.01). Based on syndrome differentiation, optimal effect was reached in treating liver stagnation and spleen deficiency syndrome and disharmony of liver and stomach syndrome. After one year follow up studies of the therapeutic effect, the recurrence rate of the JWYY tablet group was 17.7%, while that of the ranitidine group was 54.1%. In addition, JWYY tablet had no side-effects. These data indicated that JWYY tablets were a more effective therapeutic remedy for peptic ulcer.

Adult↗
PubMed1986

Protein synthesis and degradation in skeletal muscle of chronically uremic rats.

We used the perfused hemicorpus preparation to measure individual rates of protein synthesis and degradation. Using fed animals, perfused either with or without insulin, muscle protein synthesis and hemicorpus protein degradation rates were similar, but myofibrillar protein degradation was clearly increased in the uremic preparations. When the animals were fasted, differences in the rates of skeletal muscle protein turnover were apparent. Uremic rats lost more wt at both 24 and 48 hr of fasting when compared to either ad libitum fed or pair-fed controls who started fasting at body wts equivalent to our uremic rats. The accelerated wt loss was accompanied by lower rates of protein synthesis, higher degradation rates, and greater net protein catabolism in our uremic rats. Alterations in body lipid content were present in uremia and correlated with the rate of protein degradation in both control and uremic rats. These data demonstrated that even in the fed state, uremia is associated with subtle alterations in skeletal muscle protein turnover. When stressed, these alterations become more pronounced. Insufficient stores of body lipids, either due to inadequate nutrition or altered metabolism, may contribute to the alterations in muscle protein turnover seen in chronic renal insufficiency.

Adipose Tissue↗
PubMed1984

Effects of food deprivation and refeeding on total protein and actomyosin degradation.

Total protein and actomyosin degradation rates were determined in perfused rat hemicorpus preparations. By simultaneously measuring the release of two nonmetabolizable amino acids phenylalanine and N tau-methylhistidine from the hemicorpus, the respective rates of total protein and actomyosin degradation could be calculated. When rats were deprived of food for 48 h, the rate of total protein degradation increased to 148% of the fed controls. If rats were food deprived and then refed for 24 h, the degradation rate decreased to only 79% of the rate of fed controls. Measurement of N tau-methylhistidine release indicated that food deprivation led to a dramatic increase in the rate of actomyosin degradation (427% of fed), whereas refeeding decreased the actomyosin degradation rate to that of the fed controls. Calculations of the fractional degradation rates show that actomyosin breaks down at a much slower rate than the nonactomyosin proteins (1.5 vs. 20.8%/day in preparations from fed rats, and 6.2 vs. 28.2%/day in preparations from food-deprived rats). Therefore, the contribution of actomyosin breakdown to total muscle protein breakdown is small in the fed state (11%) and increased threefold after food deprivation. The addition of insulin to the perfusion medium decreased the rate of total protein degradation by 18% in preparations from food-deprived rats with no significant effect on actomyosin degradation. Thus, in vitro, insulin's major effect may be to decrease the degradation of more rapidly turning over, nonactomyosin proteins. Protein degradation, as well as protein synthesis, contributes to the adaptation of muscle to starvation and refeeding.(ABSTRACT TRUNCATED AT 250 WORDS)

Actomyosin↗
PubMed1984

Protein synthesis versus energy state in contracting muscles of perfused rat hindlimb.

The goal of these studies was to evaluate acute changes in protein metabolism in skeletal muscle in response to contractile activity. Rates of protein synthesis were measured by following L-[U-14C]phenylalanine incorporation into protein in muscles of the perfused rat hindlimb at rest, during 10 min of maximal isometric muscle contractions, and during 10 min of recovery. Synthesis measurements were carried out under conditions that ensured that the specific radioactivity of the tRNA-bound precursor amino acid was equal to that of extracellular phenylalanine. Protein degradation was estimated by measuring the release of Nt-methylhistidine. Rates of synthesis were markedly inhibited in response to muscle contractions in tibialis anterior, gastrocnemius, and plantaris but were unaffected in soleus. Rates of synthesis returned toward those observed in the resting condition during the recovery period. Rates of degradation were also markedly inhibited in response to muscle contractions. Decreased rates of synthesis correlated with reduced tissue contents of ATP and creatine phosphate, a reduced ATP/ADP, and an elevated tissue content of lactate. The results demonstrate that isometric contractions in muscles consisting of a high proportion of fast glycolytic fibers result in a marked depression in rates of protein synthesis that may be due to an altered energy state.

Amino Acids↗
PubMed1983

Vitamin D Deficiency, hypocalcemia, and increased skeletal muscle degradation in rats.

The myopathy associated with vitamin D deficiency was examined in vitamin D-deficient and vitamin D-supplemented rats. When compared with either vitamin D-supplemented ad lib. or pair-fed rats, weight gain and muscle mass were decreased in vitamin D-deficient hypocalcemic animals. With the exception of a modest decrease in muscle creatine phosphate levels, muscle composition was unchanged by vitamin D deficiency. Muscle protein turnover rates were determined in both in vivo and in vitro studies and demonstrated that myofibrillar protein degradation was increased in vitamin D deficiency. Normal growth rates could be maintained be feeding the rats vitamin D-deficient diets containing 1.6% calcium, which maintained plasma calcium within the normal range. In addition to its role in maintaining plasma calcium, vitamin D-supplemented rats had significantly higher levels of the anabolic hormone insulin. Vitamin D supplementation may affect muscle protein turnover by preventing hypocalcemia, as well as directly stimulating insulin secretion, rather than by a direct effect within skeletal muscle.

Animals↗
PubMed1982

Prenatal diagnosis of Duchenne muscular dystrophy: failure of amniotic fluid and maternal serum N tau-methylhistidine analyses to detect affected fetuses.

N tau-Methylhistidine (MH) and creatinine levels were determined in amniotic fluid and maternal serum from 81 women undergoing midtrimester amniocentesis for reasons other than the diagnosis of neuromuscular disease. Samples were also examined in three pregnancies with male fetuses who were subsequently found to have Duchenne muscular dystrophy (DMD). Between 16 and 20 weeks' gestation, amniotic fluid and maternal serum MH levels averaged 3.22 and 1.94 mumoles/L, respectively. No significant differences were found between the control and affected fetuses for MH and creatinine levels or for MH/creatinine ratios from amniotic fluid or maternal serum. Determination of amniotic fluid MH level thus has no apparent value in the prenatal diagnosis of DMD.

Amniotic Fluid↗
PubMed1982

N tau-methylhistidine release: contributions of rat skeletal muscle, GI tract, and skin.

The relative contributions of skeletal muscle, gastrointestinal tract, and skin to urinary N tau-methylhistidine (MH) excretion were estimated during in vitro studies using the rat hemicorpus preparation. After 0.5 h of perfusion, MH release into the perfusate was linear for 3 h and averaged 29.8 nmol . h-1 . 100 g hemicorpus-1. In vivo, 24-h urinary MH excretion averaged 37.3 nmol . h-1 . 100 g body wt-1. The ratio of soft tissue to skin weight is equal (3.2:1) in the whole rat and in the hemicorpus. The gastrointestinal tract released 16.0 nmol . h-1 . 100 g body wt-1 or approximately 41% of the total urinary MH excretion. Preparations perfused with or without skin showed modest differences in the rate of MH release that were not statistically significant. Skeletal muscle contains 89.8% of total body MH content, whereas gastrointestinal tract and skin contain 3.8 and 6.4%, respectively. Gastrointestinal tract actomyosin turns over rapidly with a fractional catabolic rate of 24%/day versus 1.4%/day for skeletal muscle actomyosin.

Animals↗
PubMed1981

Muscle degradation in uremia: 3-methylhistidine release in fed and fasted rats.

The rate of myofibrillar protein degradation was measured by 3-methylhistidine (3MH) release in moderately uremic and sham-operated control rats. The rats were studied in the fed state or after 24 and 48 hours of fasting. When fed, both uremic and control rats gained weight at the same rate. During 48 hours of fasting, the uremic animals lost more weight (17.1%) than the shams (13.2%). The ratio of gastrocnemius muscle protein per gram of wet weight was not significantly different under any conditions. When fed and 48-hour fasted animals are compared, urinary excretion of 3MH rose from 0.81 to 1.32 moles per 24 hr per 100 g of initial body wt shams and from 0.90 to 1.30 moles per 24 hr per 100 g of initial body wt in the uremics. When ratio of 3MH to creatinine excretion in the urine was compared, there was no change in 3MH excretion between 0 and 24 hours, but there was an increase between 24 and 48 hours. Analysis of serum and muscle samples from fed and 48-hours fasted animals revealed that the concentrations of 3MH increased in both groups during fasting, with the uremic rats having a large increase in the total body 3MH pool. Myofibrillar degradation rates calculated from the sum of urinary excretion plus the changes in body 3MH pool size revealed that with moderate fasting, degradation rates increased in both sham and uremic rats with a larger increase being seen in the uremic group. After 48 hours of fasting, the increased amount of 3MH released from muscle of uremic rats was comparable to their larger percentage weight loss.

Animals↗
PubMed1980

Protein synthesis and degradation in skeletal muscle of normal and dystrophic hamsters.

Dystrophic hamsters (BIO 53.58) had lower body weights and gastrocnemius muscle weights than normal hamsters (BIO RB). Dystrophic muscle contained less protein than normal muscle. The proportion of collagenous to noncollagenous protein remained unchanged. Loss of protein in the dystrophic muscle was the result of an increase in the rate of protein degradation. This was accompanied by higher activities of two lysosomal proteases, cathepsins B and D. The net effect of the increase in protein degradation was blunted by an increase in the rate of synthesis of total protein and myosin. The faster rate of synthesis in dystrophic muscle was partially due to an increase in the concentration of cellular RNA. Rates of peptide-chain initiation and protein synthesis decreased in muscles of normal hamsters perfused in the absence of insulin. In the presence of insulin, these processes were maintained at higher rates. However, the rate of protein synthesis in dystrophic muscle appeared less insulin-dependent than normal muscle. Protein degradation was inhibited by insulin in both types of muscle.

Animals↗