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Results for “Protein Deficiency”

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At least 19 recordsLinked to original sources
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↗
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↗
PubMed1975

1. The effect of dietary fat on the host-parasite relations in cotton rat filariasis. 2. Host-parasite relations in the progeny of cotton rats fed protein deficient diets and infected with filariasis-a preliminary report. 3. Immunoglobulin levels in the early stages of infection with filariasis in cotton rats with and without dietary protein deficiency. 4. Action of aliphatic alcohols on aquatic stages of mosquitoes.

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Alcohols↗
PubMed1992

Meningococcaemia in an adult with hereditary C4b-binding protein deficiency: study of the variations of the protein S system.

Serial studies of the plasma protein C-protein S system were performed during the clinical course of a pregnant woman with meningococcaemia who recovered under therapy. The patient had limited purpura fulminans skin lesions and hereditary C4b-binding protein deficiency was suspected. This diagnosis was confirmed in the patient 1 year after delivery and also by family studies. During the meningococcaemia, an initial mild and transient acquired protein C deficiency was seen but no protein S deficiency was observed despite consumption of the latter protein. As C4b-binding protein partial deficiency is associated with high free protein S and protein S activity, this may have protected against acquired protein S deficiency during meningococcaemia.

Adult↗
PubMed1992

The magnitude of the acute phase protein response is attenuated by protein deficiency in rats.

We assessed the growth rate and changes in plasma albumin, total protein and alpha 2-macroglobulin concentrations (a major acute phase protein in rats) before and after a subcutaneous injection of turpentine (0.5 mg/kg body wt) in groups of rats receiving one of a series of protein-deficient diets (protein concentrations of 0.5, 1.5, 3.0, 4.5 or 6.0 g/100 g) or a diet containing an adequate level of protein (20 g/100 g) for maximal growth. Increasing protein deficiency in the different groups of animals reduced the basal albumin and total protein concentrations and attenuated the total protein and alpha 2-macroglobulin responses to turpentine. Increasing protein deficiency delayed the time taken for alpha 2-macroglobulin to reach peak concentrations post-injection and its return to basal concentrations. The turpentine-induced hypoalbuminemia was similar in all groups of animals (approximately 10 g/L depression) but restoration to values that were present before turpentine injection was increasingly delayed with increasing protein deficiency. The magnitude of the acute phase response (peak alpha 2-macroglobulin concentration) was found to be directly related to growth rate (r = 0.70, P less than 0.001). We concluded that protein deficiency can alter the pattern and magnitude of the acute phase responses in circulating protein concentrations to an extent that is dependent on the severity of protein deficiency.

Acute-Phase Proteins↗
PubMed1977

Effects of protein deficiency, pair-feeding, or diet supplementation on maternal, fetal and placental growth in rats.

The effects of feeding, throughout gestation, a diet deficient in protein, of pair-feeding, and of supplementing the deficient diet late in gestation on maternal body weight and weights of the products of conception were investigated in the rat. Protein deprivation resulted in net loss of maternal body weight, smaller and thinner placentas with decreased DNA content and placental labyrinth size, reduced uterine tissue weight, and smaller fetuses with retarded bone development. Pair-feeding caused a less severe reduction in maternal, uterine, placental, and fetal weights. Placentas from pair-fed dams had normal cell numbers with reduced cell size. Diet supplementation late in gestation resulted in increased net and total maternal body weight and uterine, placental, and fetal fetal weights, and an apparent partial recovery in fetal bone development. Placental cell size also increased significantly. The results suggest that placental and uterine development in protein-deficient dams is not the limiting factor in fetal development. Availability of protein may be the primary limiting factor, and energy deficit may play a secondary role.

Animals↗
PubMed1979

Effect of protein deficiency on suppressor cells.

The effects of moderate protein deficiency on the in vitro response of spleen cells to phytohemagglutinin in A/Jax mice were studied. The response of spleen cells from protein-deficient mice to phytohemagglutinin was found to be enhanced as compared with that of cells from control animals. Since inadequate development or function of suppressor cells in the protein-deficient mice offered a possible explanation for the enhanced lymphoproliferative activity, cocultures of spleen cells from protein-deficient and control animals were tested for their responses to phytohemagglutinin. Suppression of [3H]thymidine incorporation was detected in coculture of 25% mitomycin-treated spleen cells from control animals and 75% spleen cells from protein-deficient mice. The suppressor (regulator) elements in control spleens were found to reside in the adherent cell population.

Animals↗
PubMed1978

The role of mucosal iron binding proteins in adaptation of iron absorption during protein deficiency and rehabilitation.

1. A state of protein deficiency has been produced in rats by feeding a low protein diet, thereafter a period of rehabilitation with a normal protein but a low iron supply followed. 2. For characterization of the iron metabolism during both periods haemoglobin, total iron binding capacity, liver non-haemin iron, intestinal iron absorption and the uptake of 59Fe in the liver was determined. 3. Under these conditions the amount of 59Fe incorporated into the mucosal transferrin and the ferritin fractions has been measured. Both fractions were obtained from the supernatant of a mucosal homogenate after chromatography on sepharose 6B. 4. In anemia due to protein deficiency the typical increase of 59Fe incorporation into the fraction of mucosal transferrin--usually occuring in iron deficiency--could not be observed. This coincides with the absence of an increased iron absorption. Moreover a decrease of iron absorption is observed, which is associated with a decreased 59Fe ratio of transferrin/ferritin-fraction. 5. After normalization of the protein supply the ratio of 59Fe incorporated into the mucosal transferrin and ferritin fractions was changed remarkably in favor to transferrin together with a several fold increase of the intestinal iron absorption. 6. The conclusion is drawn that mucosal transferrin and ferritin enable the body not only to adapt the absorption to a higher but also to a lower requirement as it is the case in protein deficiency.

Adaptation, Physiological↗
PubMed1977

Effects of protein deficiency on the biosynthesis and degradation of ribosomal RNA in rat liver.

Employing livers from rats fed on a protein-free diet for two weeks, the effects of protein deficiency on both biosynthesis and degradation of rRNA were investigated and the following results were obtained. 1. Protein deficiency led to a decrease of total liver RNA content per DNA to about 80% of that in normal rat liver. 2. From the kinetics of rRNA labelling with [14C]orotic acid in vivo, the half-lives of cytoplasmic rRNA's of normal and protein-deficient rat livers were determined to be 6.2 and 5.1 days, respectively. Furthermore, considering the pool size of rRNA in rat liver, the turnover rate of cytoplasmic rRNA was calculated to be 0.212 pmole/min/mg of nuclear DNA in normal rats and 0.240 pmole/min/mg of nuclear DNA in protein-deficient rats. 3. From the electrophoretic patterns of nucleolar RNA's of both groups of rat livers labeled with [14C]orotic acid, the time courses of the specific activities of nucleolar 45S, 32S, and 28S rRNA's were analysed and the half-life of each nucleolar RNA in both groups of rat livers was determined. Nucleolar 45S, 32S, and 28S RNA's had half-lives of 6.0, 15.9, and 26.5 min in normal rats, respectively, and 5.5, 19.4, and 22.9 min in protein-deficient rats, respectively Considering the pool size of each nucleolar RNA obtained from the leectrophoretic pattern, the turnover rates of 45S, 32S, and 28S RNA's were calculated to be the same, i.e., o.189 pmoles/min/mg of nuclear DNA, in normal rat liver and 0.372, 0.372, and 0.358 pmoles/min/mg of nuclear DNA in protein-deficient rat liver, respectively. 4. These results indicate that protein deficiency increased both the rate of degradation of cytoplasmic rRNA and that of nucleolar rRNA synthesis in rat liver. While in normal rat liver the rates of rRNA synthesis and degradation were rather similar, the rate of rRNA synthesis in protein-deficient rats was about 1.5 times higher than that of its degradation. Therefore, the decrease of total liver RNA content in protein deficiency might be accounted for by stimulated degradation of rRNA in the nucleus. 5. The activities of RNase in nuclear fractions of both groups of rat livers were compared. Both activities of nuclear acid RNase and especially that of the free form of alkaline RNase in protein-deficient rat liver were higher than those in normal rat liver.

Animals↗
PubMed1978

Suppression of rejection of Nippostrongylus brasiliensis in iron and protein deficient rats: effect of syngeneic lymphocyte transfer.

Rejection of Nippostrongylus brasiliensis is impaired in iron and protein deficient rats and this suggests that iron and protein deficiency directly or indirectly suppresses the immune response. The site of the immunological defect in deficient rats was investigated using the technique of cellular transfer of resistance. The functional activity of immune mesenteric lymph node cells obtained from iron and protein deficient donors was not depressed as measured by their capacity to cause parasite rejection in nutritionally sufficient recipients. In contrast, immune lymph node cells obtained from either sufficient or deficient donors did not result in parasite rejection in iron and protein deficient recipients. These results indicate that there is no permanent defect of lymphocyte function in iron and protein deficient rats and suggest that either some other component of the rejection mechanism is defective, or that lymphocyte function is blocked in an iron and protein deficient environment.

Animals↗
PubMed1975

Effects of severe energy and protein deficiencies on the fibres and nuclei in skeletal muscle of pigs.

1. Measurements have been made of the size and number of muscle fibres and number of nuclei in a small indicator muscle (m. flexor digiti V brevis) in the fore-foot of the pig. Well-nourished, 10-d-old and 1-year-old animals were studied, as well as 1- and 2-year-old animals that were severely energy-deficient and protein-deficient. 2. The normal 1-year-old animals had much larger muscle fibres, with more nuclei, than the pigs in any of the other groups. 3. There were no significant differences between the numbers of fibres in the muscles of pigs in any of the four groups. 4. There was a significant difference between the number of fibres in the muscles of pigs coming from different litters, irrespective of their dietary history after birth. This suggests that the number of fibres is determined genetically before birth, and all that can take place after birth is an alteration in size.

Age Factors↗
PubMed1975

Protein deficiency in carbon tetrachloride-induced hepatic lesions.

The influence of protein deficiency on the hepatotoxicity of carbon tetrachloride (CCl4) was investigated in a group of rhesus monkeys. Animals fed a protein-rich diet served as controls. The results indicate that protein-deficiency protects the liver against acute hepatotoxicity of this drug. The protective effect is abolished if the animals are administered phenobarbital prior to the administration of CCl4. The protective action is due to a reduction, in protein deficiency, of the endoplasmic reticulum associated enzymes involved in hepatotoxicity of CCl4. Repeated administration of CCl4, which induces hepatic regeneration, resulted in disappearance of fat from periportal cells in protein-deficient animals. The regenerating cells (because of their better enzyme system) acquire "nutritional autonomy" and are thus able to synthesize adequate amounts of lipoproteins for mobilization of liver triglycerides.

Animals↗