Search PubMed⌕ Search

SEARCH · Search PubMed

Results for “Protein Deficiency”

Search indexed PubMed citations on genomics, clinical trials, systematic reviews and public health. Explore titles, authors and supplied subject terms, then open the PubMed record.

Quote a phrase for an exact phrase match. Source license links do not imply unrestricted reuse.

At least 325 records · Page 18Linked to original sources
PubMed1986

Mental deficiency in pseudohypoparathyroidism type I is associated with Ns-protein deficiency.

Pseudohypoparathyroidism type I is a hereditary disorder characterized by resistance to parathyroid hormone and other hormones that work via cyclic adenosine 3', 5'-monophosphate (cAMP). Most patients with this disorder have generalized deficient activity of Ns-protein (type Ia), which couples stimulatory hormone receptors to catalytic adenylate cyclase. In patients with normal Ns-protein activity (type Ib), a decreased incidence of resistance to hormones other than parathyroid hormone exists. Mental deficiency of unknown cause occurs in 47% to 75% of all patients with pseudohypoparathyroidism type I. Because mutations in the adenylate cyclase-cAMP system may affect the learning ability of Drosophila flies, we assessed mental deficiency in 25 patients whose Ns-protein activity we had determined: 9 of 14 patients with type Ia disorder and 0 of 11 patients with type Ib disorder had mental deficiency. We suggest that Ns-protein deficiency, reduced cAMP levels, or both, are involved in the mental deficiency in these patients and probably in mental function in humans.

Adolescent↗
PubMed1983

[Supplementary tube feeding in protein deficiency in children with surgical diseases].

The development of protein insufficiency in children with surgical diseases is considered by the authors to be an important problem. Even good appetite does not always meet the protein requirements of the organism. An additional probe feeding is indicated for the reestalishment of passage along the intestine if the natural supply by food products fails to meet the needs of the organism.

Adolescent↗
PubMed1983

Calorie-protein deficiencies and the immune response of the chicken. II. Cell-mediated immunity.

Calorie-protein deficiency affects humoral immunity in the chicken. Secondary responses to sheep-red blood cells, a T-dependent antigen, were lower in birds fed diets two-thirds deficient in calories (C), amino acids (AA), or both (C/AA). These results led us to question what effects might be found in cell-mediated immunity after nutritional deficiency. Birds fed the same diets as in our previous study showed no reduction in total white blood cells, absolute lymphocytes, or absolute heterophils. Splenic lymphocytes from 3- or 7-week-old nutritionally deficient chickens with the exception of the AA group at 7 weeks, produced a nonsignificant increase in graft-versus-host (GvH) response of 12-day-old embryos. Thymic cells from 3-week-old nutritionally deficient birds were not deficient in the GvH potential. Thymic histology revealed reduced cellularity in AA-deficient birds. The reduced cellularity may not have been in response to stress since the mean corticosterone levels were not significantly different. Birds fed the deficient diets for 10 weeks had a significantly reduced delayed hypersensitivity response to human gamma globulin. The results indicate that the chickens' ability to produce a GvH response was not compromised and that T-cell subpopulations may have differential sensitivities to nutritional deficiencies.

Amino Acids↗
PubMed1979

Influence of prenatal and continuous postnatal protein-deficient diets on the development of rats.

The influence of prenatal and continuous postnatal protein-restricted diet on the development of rats was investigated. Virgin female rats were maintained for 35 days on isocaloric diets containing 8 or 25% casein, and then mated. The animals were supplied their respective diets during gestation and nursing. It was observed that the offspring of mothers kept on the 8% casein diet had 50% less body weight, and 10-15% less brain weight than the corresponding controls. The peak of rapid brain growth for both groups of animals occurred at age 6 days. The rate of de novo biosynthesis of sterols, following the injection of (2-14C)-mevalonic acid into the midline thalamic area and the cerebellum, was also investigated. A significant shift of the age of peaking of 14C-incorporation into sterols in the cerebellum was noted. Our results indicate that although unlimited amounts of food were supplied to the mothers on the 8% casein diet, this could not offset the detrimental effect of the protein deficiency on the offspring.

Animals↗
PubMed1990

Two ELISA's for measurement of protein S, and their use in the laboratory diagnosis of protein S deficiency.

Protein S is a vitamin K-dependent coagulation factor involved in the regulation of the anticoagulant activity of activated protein C (APC). Heterozygosity for hereditary protein S deficiency is considered as a risk factor for the development of thrombotic disease. To measure the plasma concentration of protein S, two enzyme-linked immunosorbent assays (ELISA) have been developed: the ELISA-p (using polyclonal antibodies both as catching and tagging antibodies) and the ELISA-m (using polyclonal antibodies as catching antibodies and a monoclonal antibody as tagging antibody). The performance of these assays has been compared with that of an immunoradiometric assay (IRMA) for total protein S. Results obtained with both ELISA's in plasma's of healthy volunteers, patients with hereditary protein S deficiency type I and patients using oral anticoagulant treatment correlate very well with those of the IRMA: r = 0.974 (n = 57) for ELISA-p and r = 0.966 (n = 57) for ELISA-m. The intra- and inter-assay variation (n = 6) were calculated to be 5% and 11% for the ELISA-p and 4% and 10% for the ELISA-m. Both ELISA's can be used for the measurement of total protein S, but also for the measurement of free protein S and C4b-BP-PS complexes, after PEG precipitation. The ELISA-m was further used to measure free protein S in healthy volunteers (n = 40), patients with a protein S deficiency type I (n = 20) and patients with unexplained familial thrombosis (n = 76). In the first two groups measured and calculated free protein S levels were very similar. In the third group 7 patients were identified with total protein S in the normal range, but with measured free protein S and the ratio between the measured free protein S and calculated free protein S below the lower limits of the normal range.

Blood Coagulation Disorders↗
PubMed1985

Effect of a steroidal oral contraceptive on intestinal absorptive functions in proteins deficient rat.

The effects of steroidal oral contraceptive norethynodrel plus ethinylestradiol-3-methyl ether (SOC) at a daily dose of 5 mg: 0.06 mg per kg body weight for 28 days on intestinal absorptive functions have been investigated in protein-deficient female albino rats. The administration of this contraceptive caused significant increase in glucose and amino acids uptake but had no effect on calcium and zinc uptake in pair-fed as well as in protein-deficient rat. Further studies carried out on glucose transport system showed that the transport of sodium-dependent glucose was significantly enhanced while that of sodium-independent glucose remained unaltered in drug-treated animals. Kinetic studies of glucose transport in the presence of sodium ions revealed that SOC treatment affected the rate of uptake of glucose by elevating Vmax, but the apparent Kt value remained the same in treated and untreated animals.

Amino Acids↗
PubMed1997

Effects of cow's milk supplementation on milk output of protein deficient lactating mothers and on their infants' energy and protein status.

A cow's milk supplement providing 500 kcal (2093 kJ) and 18 g of protein a day was given during 2 months to 83 lactating Zairian mothers suffering from protein malnutrition. The mothers' nutritional status improved significantly after 2 months. The initial 24-hour mother's milk output was on average 607 ml (s.d.: 182) and did not change significantly after 2 months (604 ml; s.d.: 178). Initial milk output and change in milk output did not differ according to mothers' nutritional status at inclusion. Breast-fed infants showed a significant improvement of their mean serum albumin concentration while their growth was similar to the mean growth of children of the same age.

Animals↗
PubMed1993

Effect of protein deficiency on luteinizing hormone releasing hormone (LHRH), gonadotropin releasing hormone associated peptide (GAP) and luteinizing hormone (LH) immunocytochemistry in the hypothalamus and pituitary gland of prepubertal ewes.

Growing female lambs were fed diets containing 14.2% (standard) or 8.1% (protein restricted) of proteins to determine their effects on puberty and luteinizing hormone releasing hormone (LHRH), gonadotropin hormone associated peptide (GAP), luteinizing hormone (LH) hormonal system. At the end of the experiment (30-34 weeks of age), hypothalamic LHRH, GAP and pituitary LH were analysed by immunocytochemical methods using specific antibodies. Plasma LH were determined by radioimmunoassay at 21 weeks of age. It was found that lowering of the dietary proteins content decreased the concentration of basal plasma LH significantly in lambs of 21 weeks of age. None of the sheep of this group reached sexual maturity at the same time as the animals of the standard group. However, immunoreactive (ir) LHRH neuronal system of protein restricted lambs was normally developed: Numerous irLHRH perikarya, dense network of axons and abundant material stored in the nerve terminals were well visualized in the typical sites of the preoptico-septal area, hypothalamus and the median eminence (ME). Gonadotropin associated peptide (GAP) of the LHRH precursor was present in the same populations of neurons that contained LHRH in the sheep brain. The proportion of pituitary LH-cells was three fold higher in pituitaries of the nutritionally restricted group. They displayed hypertrophy and very strong immunoreaction. These results show that protein deficiency in diets of growing female sheep delays their puberty but does not impair the synthesis and processing of LHRH in the brain neurons and synthesis of LH in pituitary cells.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1968

Organ weights and water content of rats fed protein-deficient diets.

To provide the basic information needed for studies of drug toxicity in rats suffering from protein deficiency, weanling male albino rats were fed for 28 days on either laboratory chow or a synthetic diet containing 27% or 8% of casein. The low-protein diet produced a kwashiorkoric cachexia characterized by stunting, alopecia, tail dermatitis, apathy, augmented calorie intake per kg body-weight and a 20% death rate. Autopsies at weekly intervals disclosed that the synthetic normal-protein diet produced a slight loss of total body-weight, due to loss of weight in the adrenal glands and gastrointestinal tissues, and a more-or-less generalized dehydration of body organs. The body-weight of the kwashiorkoric rats was half that of the control groups, due especially to loss of weight in caecum, kidneys, liver, muscle, skin, spleen, salivary glands and thymus gland; loss of weight was less marked in other organs, particularly the stomach, heart and testes and, especially, the brain. There was further dehydration of adrenals and brain but the liver and gastrointestinal tissues tended to be hydrated. The kwashiorkoric diet had not entirely suppressed growth-stimulated relative increase in weight of muscle, skin and testes. The histology of organs was essentially normal in the survivors. Absence of oedema in organs distinguished the kwashiorkoric rats from rats with total calorie depletion.

Animal Nutritional Physiological Phenomena↗
PubMed1992

Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle.

When rats are fed a protein deficient (PD) diet for 7 days, rates of proteolysis in skeletal muscle decrease by 40-50% (N. E. Tawa, Jr., and A. L. Goldberg. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E317-325, 1992). To identify the underlying biochemical adaptations, we measured different proteolytic processes in incubated muscles. The capacity for intralysosomal proteolysis, as shown by sensitivity to methylamine or lysosomal protease inhibitors, fell 55-75% in muscles from PD rats. Furthermore, extracts of muscles of PD rats showed 30-70% lower activity of many lysosomal proteases, including cathepsins B, H, and C, and carboxypeptidases A and C, as well as other lysosomal hydrolases. The fall in cathepsin B and proteolysis was evident by 3 days on the PD diet, and both returned to control levels 3 days after refeeding of the normal diet. In muscles maintained under optimal conditions, 80-90% of protein breakdown occurs by nonlysosomal pathways. In muscles of PD rats, this ATP-dependent process was also 40-60% slower. Even though overall proteolysis decreased in muscles of PD rats, their capacity for Ca(2+)-dependent proteolysis increased (by 66%), as did the activity of the calpains (+150-250%). Thus the lysosomal and the ATP-dependent processes decrease coordinately and contribute to the fall in muscle proteolysis in PD animals.

Adenosine Triphosphate↗
PubMed1985

Rat pancreatic beta-cells in protein deficiency: a study involving morphometric analysis and alloxan effect.

The possible cause(s) of impaired glucose tolerance in protein-calorie malnutrition was studied. The beta-cell mass was morphometrically determined and the sensitivity to alloxan was characterized in rats fed ad libitum a 4% protein diet, pair-fed or fed ad libitum a 20% protein diet. The percentage of beta-cells in the pancreas was neither affected by protein deficiency nor influenced by caloric intake. However, the diabetogenicity of alloxan was greatly reduced in protein-malnourished rats. This reduction in diabetogenicity by alloxan was partially reversed by feeding animals with sulfhydryl compound. These results suggest that decreased insulin secretion in protein malnutrition is not due to a reduction in beta-cell number.

Alloxan↗