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Results for “Protein S Deficiency”

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At least 19 recordsLinked to original sources
PubMed1989

Expression of liver-specific genes coding for plasma proteins in protein deficiency.

Protein deficiency leads to a decreased concentration of plasma proteins, although it is not clear whether this response is caused by alterations in gene transcription or in post-transcriptional events. The aim of this study was to investigate the expression of some liver-specific genes coding for plasma proteins in rats kept on a protein-free diet for 30 days. Cloned cDNA probes for the albumin, transthyretin, retinol-binding protein and prothrombin genes were used in Northern hybridizations to total liver RNA to compare their transcript levels in protein-deficient and control animals. Liver polysomes were also isolated and fractionated from the two groups of animals to examine the possible effects of protein deficiency on translation of the mRNAs. The results indicate that the albumin and transthyretin mRNAs are present in lower amounts in protein deficiency. The distribution profile along sucrose gradients shows that all mRNAs are undergoing translation, but in protein-deficient animals a small but consistent fraction of each mRNA is also present in the non-polysomal, low molecular weight fractions.

Actins↗
PubMedDate not supplied

[Nucleic acid and protein metabolism in vitamin D and dietary protein deficiency].

Protein deficiency and D-hypovitaminosis lead to marked disturbances of the RNA and protein metabolism in different organs, tissues and subcellular fractions. With a complex action of the food protein and vitamin D deficiency, changes in most organs and tissues became more intensive. The nature of the discovered shifts is largely determined by the kind of the tissue, and the degree of its metabolic activity.

Animals↗
PubMedDate not supplied

[Toxic effect of methanol under conditions of complete and deficient protein nutrition].

In experiments with albino rats receiving complete and protein-deficient nutrition the effect of different doses of methanol (10,100 and 500 mg/kg) administered daily per os for a month was studied. Methanol was shown to display toxic hepatotropic action, producing in the liver a focal proteinic degeneration of the hepatocytic cytoplasm, causing changes in the activity of some microsomal enzymes and enlarging the average size of hepatic cells (early age-specific changes). The damaging action of methanol manifested itself in a particularly distinct fashion by depressing the synthesis of DNA, when used in large doses and against the background of a protein-deficient ration.

Animals↗
PubMed1977

Effect of iron and protein deficiency on the expulsion of Nippostrongylus brasiliensis from the small intestine of the rat.

The relationship between iron deficiency and protein deficiency and infestation of the rat with the nematode Nippostrongylus brasiliensis was investigated. There was a significant delay in the expulsion of N. brasiliensis from the small intestine of both iron deficient and protein deficient animals and those with a combined deficiency of iron and protein. Iron repletion returned the time of worm expulsion to normal and this would appear to be related to iron deficiency per se rather than to anaemia. Antibody initiated damage to worms was normal in the control animals and in animals with nutritional deficiencies. This suggests that the defect in worm expulsion occurs either in the cell-mediated immune system or in one of the other mediators of expulsion. Extrapolation to the human situation has important therapeutic implications in that iron and protein deficiency may play an important role in the perpetuation of helminth infestations. Thus, to be successful antihelminth therapy should be accompanied by iron and protein supplementation.

Ancylostomatoidea↗
PubMedDate not supplied

[Amino acid composition of proteins of the membranes of rat liver sucellular structures and the effect of protein deficiency on it].

The protein amino acids composition of nuclear, mitochondrial and lysosomic membranes and those of the endoplasmatic reticulum of the liver in rats receiving for 30 days rations with normal (18.5 per cent) and low (4 per cent) protein content was investigated. The amino acid spectra of proteins forming part of various cytomembranes, in spite of their considerable resemblance, are shown to have traits of a definite specificity. Protein deficit in the ration causes not only a fall of the total amino acid content in the membranous cellular structures, but it also attended by a deranged correlation among individual amino acids.

Amino Acids↗
PubMed1985

alpha-1-Antitrypsin metabolism in the protein-deficient weanling rat.

Protein-deficient weanling rats fed on a 30 g casein/kg diet for 3 weeks lost albumin but maintained the level of serum alpha-1-antitrypsin, the most abundant protease inhibitor in blood. alpha-1-Antitrypsins from malnourished rats and control rats (given 250 g casein/kg diet) differed; the protease inhibitor from protein-deficient animals: (1) was more acidic, (2) appeared slightly larger (57 400 v. 56 000 daltons) on sodium dodecyl sulphate (SDS)-polyacrylamide gels, (3) had a more acidic Pi type and increased anodal mobility at pH 8.9, (4) bound more concanavalin-A and contained more carbohydrate, specifically two to three extra sialic acid residues. The amino sugar and neutral sugar contents of both preparations of alpha-1-antitrypsin were the same. Analysis of the products of cyanogen-bromide cleavage revealed that alpha-1-antitrypsin preparations from protein-deficient rats contain an extra glycopeptide that was not present in alpha-1-antitrypsin from control animals. In vivo studies showed that the increased sialic acid content of alpha-1-antitrypsin of protein-deficient rats did not alter the half-life of the molecule in the blood of control rats. However, the fractional catabolic rate of alpha-1-antitrypsin from either well-nourished or protein-deficient rats was significantly (P less than 0.01) lower in protein-deficient rats than in control rats (0.0247/h v. 0.0406/h). The decreased fractional catabolic rate could not be explained by changes in hepatic mannosyl-, galactosyl- or N-acetylhexosaminyl receptors since liver perfusion studies showed that bovine serum albumin, when covalently modified separately with each of these ligands, was extracted from the perfusion medium as rapidly or more rapidly by livers from malnourished animals. Perfused livers from protein-deficient rats secrete three times more alpha-1-antitrypsin than do livers from well-nourished animals. The decreased fractional catabolic rate and increased rate of biosynthesis and secretion of the glycoprotein by livers from protein-deficient animals may account for the maintenance of alpha-1-antitrypsin levels during protein malnutrition.

Albumins↗
PubMed1987

Thyroid function, energy balance, body composition and organ growth in protein-deficient chicks.

Protein-deficient diets (17, 10, 6.5 or 3% protein) and a 24% control diet were fed to growing chicks. A control group was pair-fed daily with each deficient group. Energy intake was lower in the 6.5 and 3% protein groups than in the other groups. However, weight gain, bone growth and feed conversion efficiency were lower with 10% protein or less. Relative thyroid weights were unaffected by dietary protein. Plasma T3 (3,5,3'-triiodothyronine) levels were significantly higher in all deficient groups, whereas plasma T4 (thyroxine) was lower. Plasma rT3 (reverse T3) was unaffected by the protein deficiencies, suggesting that enhanced conversion of T4 to T3 rather than to rT3 had occurred. Hepatic alpha-glycerol-3-phosphate dehydrogenase (alpha-GP) shuttle activity increased markedly in protein-deficient chicks. Efficiency of energy utilization was unaltered in chicks fed 17 or 10% protein but was higher in chicks fed 6.5 and 3% protein than in controls. All deficient chicks had more fat and less protein and water in the tissues. The lower feed conversion efficiency therefore represents almost entirely a shift in body composition toward fat and does not reflect a loss of energy as heat. We conclude that elevations in plasma T3 and in thyroid-controlled alpha-GP shuttle activity, although sensitive indicators of protein deficiencies, are not good predictors of altered thermogenic activity in protein-deficient chicks.

Animals↗
PubMed1985

Interaction of galactose and dietary protein deficiency on rat lens.

Protein deficiency, a frequently encountered nutritional disorder of developing countries is known to affect the proliferative and synthetic activities of several cell systems. But neither all the organs are affected at the same time nor at the same rate. The lens, which is an unique organ has been shown to suffer in protein malnutrition but without any clinically discernible changes. Clinical evidence suggests, early onset of senile cataract in underdeveloped countries is possibly due to protein deficiency. In the present investigation, it has been shown that addition of small concentrations of galactose to the diet readily induces cataracts in protein-deficient rats. This therefore supports the contention that protein deficiency alone may not produce morphological changes but exogenous or endogenous cataractogenic insults, may produce lenticular opacification in the protein-deficient state.

Animals↗
PubMed1978

Hair root diameter measurement as an indicator of protein deficiency in nonhospitalized alcoholics.

Protein status of alcoholics admitted to a detoxification center was investigated with a view to adapting a hair root test for use in screening for protein deficiency. Hair root volume and hair root diameter had previously been shown to correlate well with hair root protein and to be sensitive indicators of protein deficiency. Hair root volumes in this study correlated well with mean maximum hair root diameters (n = 35, r = 0.9), which were simpler to measure, so diameter measurements were used. Mean maximum hair root diameters (range 0.02 to 0.19 mm) correlated with plasma RNase concentrations (range 6000 to 14,000 units/ml; n = 17, r = -0.7). Mean hair diameters of 84 alcoholics averaged 0.0864 +/- 0.0366 mm; those of 25 nonalcoholics were significantly greater: 0.100 +/- 0.0254 mm (P less than 0.05). Frequency of occurrence of hair root diameters of 0.06 mm or less was significantly higher in 71 alcoholics (29.5%) than in 23 nonalcoholics (8.6%) matched by age. Mean hair root diameters of 0.06 mm or less therefore can be used to signify protein deficiency where more expensive or technically demanding tests are not feasible. Protein deficiency occurs extensively in non hospitalized alcoholics. This method enables staff to single out those clients most likely to be in need of nutritional counseling and therapy.

Alcoholism↗
PubMed1992

Effect of aseptic abscesses in protein-deficient rats on the relationship between interleukin-6 and the acute-phase protein, alpha 2-macroglobulin.

1. Rats established on a normal (20% protein) diet or a protein-deficient (3% protein) diet were given either a subcutaneous injection of turpentine (5 ml/kg), which induces formation of aseptic abscesses, or saline. Plasma samples were obtained at timed intervals (0-14 days) after the injection for determination of albumin, total protein, alpha 2-macroglobulin (a major acute-phase protein in the rat) and interleukin-6 concentrations. The magnitude and pattern of the acute-phase protein response was then compared with the local inflammatory reaction, assessed histologically, and with changes in the circulating concentration of interleukin-6, which is an important mediator of the acute-phase protein response. 2. After turpentine injection there was an early fall in the plasma albumin and total protein concentrations in both normal and protein-deficient rats. After 12 h the total protein concentration increased in both groups of animals reaching a peak at about 48 h, whereas the plasma albumin concentration continued to fall reaching a minimum at 48 h. The main alpha 2-macroglobulin response was delayed and attenuated in the protein-deficient rats (onset 9 versus 24 h, peak concentration 8.95 +/- 0.5 versus 5.33 +/- 0.75 g/l, P < 0.01, and area under the concentration-time curve 18.43 +/- 2.13 versus 7.96 +/- 1.48 g/l-1 days, P < 0.01, in the normal group and protein-deficient group, respectively). 3. The circulating interleukin-6 concentration showed a transient early rise at 1 h, and was followed by a larger more sustained peak at 6-48 h.(ABSTRACT TRUNCATED AT 250 WORDS)

Abscess↗