Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The effects of chronic alcohol ingestion on the rat small intestinal epithelium have been measured using two different experimental models, viz. either a solid diet plus alcohol or a liquid diet plus alcohol. All experimental animals consumed adequate quantities of food and exhibited a normal growth rate; thus the recorded effects were unlikely to be associated with malnutrition. After a period of 24 days, there were significant decreases in the jejunal villus cell population in both groups of experimental animals and corresponding increases in the crypt cell populations; no such changes were found in the ileum. Alcohol had no significant effect on the crypt cell production rate and the growth fraction at either of these two sites in the intestine, and thus the major effect of alcohol was to cause a lengthening of the cell cycle time in the jejunal crypts.
Virchows Arch B Cell Pathol Incl Mol Pathol 1985
PMID:Chronic effects of alcohol on the epithelium of the small intestine using two experimental models. 286 35

Dietary manipulations involving high carbohydrate feeding increase V1 cardiac myosin isoform expression in hormonally deficient rats. The purpose of this study was to determine if extremes in dietary carbohydrate availability could alter cardiac myosin isoform patterns in normal weanling and adult rats. Three and six weeks of dietary manipulations (either high or low carbohydrate diets) failed to change calcium-activated myofibril ATPase activity, calcium regulated myofibril ATPase activity, or the myosin isoform distribution in the adult. In contrast, a four week, high carbohydrate diet reduced calcium activated myosin ATPase activity by 33%, calcium regulated myofibril ATPase activity by 10%, and V1 isoform expression by 66% in weanling rats. Although the low carbohydrate diet caused no change in the myosin ATPase properties, it decreased V1 isoform expression by 17%. These results show that carbohydrate availability can alter cardiac myosin isoform expression in normal rats, but only at weanling age. The reason for this age-related contrast in response to dietary manipulations is unknown at this stage. The dietary manipulations may have acted directly on the heart by creating a state of malnutrition, or indirectly, by altering some developmental process which links maturation of the sympathetic nervous system with myosin isoform expression.
Mol Cell Biochem 1987 Dec
PMID:Differential effects of carbohydrate intake on cardiac myosin isoform expression in normal weanling and adult rats. 296 58

Normal function of the GAL11 gene is required for maximum production of the enzymes encoded by GAL1, GAL7, and GAL10 (collectively termed GAL1,7,10) in Saccharomyces cerevisiae. Strains bearing a gal11 mutation synthesize these enzymes at 10 to 30% of the wild-type level in the induced state. In a DNA-RNA hybridization experiment, the gal11 effect was shown to be exerted at the transcription level. Yeast cells bearing the gal11 mutation were shown to grow on glycerol plus lactate more slowly than the wild type. We isolated recombinant plasmids carrying the GAL11 gene by complementation of the gal11 mutation. When the GAL11 locus was disrupted by insertion of the URA3 gene, the resulting yeast cells (gal11::URA3) exhibited phenotypes almost identical to those of the gal11 strains, with respect to both galactose utilization and growth on nonfermentable carbon sources. Deficiency of Gal4, the major transcription activator for GAL1,7,10, was epistatic over the gal11 defect. The Gal11 deficiency lowered the expression of GAL2 but not that of MEL1 or GAL80; expression of these genes is also known to be dependent on GAL4 function. We determined the nucleotide sequence of GAL11, which is predicted to encode a 107-kilodalton protein with stretches of polyglutamine and poly(glutamine-alanine). An alpha-helix-beta-turn-alpha-helix structure was found in a distal part of the predicted amino acid sequence. A possible role of the GAL11 product in the regulation of galactose-inducible genes is discussed.
Mol Cell Biol 1988 Nov
PMID:GAL11 protein, an auxiliary transcription activator for genes encoding galactose-metabolizing enzymes in Saccharomyces cerevisiae. 140 62

The volume of epithelium in the cortex and in the medulla of the thymus was compared in four groups of weanling male and female CBA/J mice. Well-nourished controls (C), food intake restricted (R), and animals given a low-protein diet ad libitum (LP) were fed from 23 to 37 days of age. Baseline controls (B) were studied at 23 days of age. Epithelial volume fraction was estimated for each group by point-counting morphometry on electron micrographs. Other mice were used to obtain group mean estimates of thymic index (mg/g live weight) and volume fraction of cortex and medulla (light microscope-level point-counting morphometry). Cortical and medullary epithelial volumes were calculated for each animal examined by electron microscopy by obtaining the live weight and applying, in sequence, the group mean thymic index, an assumed thymic density of 1.0 mm3/mg, the group mean cortical or medullary volume fraction, and the measured cortical or medullary volume fraction for that animal. Serum thymulin bioactivity was also measured in C, R, and LP mice. The results reveal thymic epithelial involution in the two most common rodent models of malnutrition, and suggest that this may contribute to the low serum thymulin levels found in malnourished experimental animals and humans.
Exp Mol Pathol 1988 Apr
PMID:Involution of thymic epithelium and low serum thymulin bioactivity in weanling mice subjected to severe food intake restriction or severe protein deficiency. 335 Jan 44

Marked differences in cardiac associated morbidity and mortality have been reported between patients with and without malnutrition. Tumor-associated cachexia may impair heart function, which further aggravate host wasting and thereby create a vicious circle. The aim of this study was to evaluate to what extent a malignant tumor may influence heart function under well-defined experimental conditions. The perfused working rat heart was used as a model. Study groups of freely-fed sarcoma-bearing rats, starved and protein-calorie malnourished (PCM) non-tumor rats were compared to freely-fed control animals. All groups of malnourished animals (tumor-bearing, starved and PCM) lost significant amounts of body and heart mass compared to freely-fed controls. Loss of heart contractile mass in tumor-bearing rats and malnourished animals did not lead to impaired heart function in any respect. The rate of oxygen uptake was significantly higher under all experimental conditions in perfused hearts from tumor-bearing rats compared with hearts from starved, PCM and freely-fed control rats. Oxygen uptake per left ventricular work was significantly higher in tumor-bearing rats but significantly lower in starved and PCM rats compared with control animals. Norepinephrine at various concentrations (10(-9)-10(-5) mol/l) in the perfusate stimulated the contractility and the left ventricular peak pressure significantly more in hearts from malnourished animals compared with that of freely-fed controls. The results show that adaptive functional changes can be recorded in the isolated perfused rat heart from sarcoma-bearing rats and after a period of comparatively acute undernutrition in non-tumor rats. A malignant tumor or the associated malnutrition does not induce impaired pumping performance despite a reduction in contractile heart mass. Increased oxygen consumption in hearts from tumor-bearing animals may contribute to elevated energy expenditure in a cancer-bearing host.
J Mol Cell Cardiol 1986 Nov
PMID:Effects of tumor-load and malnutrition on myocardial function in the isolated working rat heart. 379 77

We have investigated whether the low serum levels of somatomedin-C (SM-C) observed in protein malnutrition could be related to changes in liver growth hormone and prolactin binding. Growing female rats were fasted for 3 days and subsequently refed for 14 days with isocaloric diets containing 5% (low) or 25% (normal) protein. Control rats were fed a normal protein diet during the entire study. The numbers and affinity constants of somatogenic (GH) and lactogenic (PRL) binding sites were determined by analysis of saturation curves using liver homogenates incubated with 125I-labelled bovine growth hormone and 125I-labelled ovine prolactin. Serum SM-C and growth hormone concentrations were measured by radioimmunoassay. After fasting for 3 days body weight dropped by 21% (P less than 0.01 vs. controls) and serum SM-C by 53% (P less than 0.01), while GH and PRL binding capacities decreased respectively by 63% (P less than 0.01) and 62% (P less than 0.01). On refeeding with a normal protein diet, body weight, serum SM-C, GH and PRL binding capacities returned to control values. In contrast, with low protein intake, body weight, SM-C, GH and PRL binding capacities remained respectively 16%, 55%, 49% and 81% lower than controls (P less than 0.01). No significant changes in serum growth hormone concentrations occurred with fasting or refeeding.(ABSTRACT TRUNCATED AT 250 WORDS)
Mol Cell Endocrinol 1984 Oct
PMID:Low serum somatomedin-C in protein deficiency: relationship with changes in liver somatogenic and lactogenic binding sites. 609 85

Deficiency of a granulocyte surface glycoprotein of 150,000-D had been associated with defective C3- and IgG-dependent phagocytosis in a patient with recurrent bacterial infections. By using monoclonal antibodies, we found that this patient's granulocytes, monocytes, and null cells were deficient in Mo1 (equivalent to OKM1 and Mac-1), a cell surface molecule consisting of two noncovalently linked glycoproteins of 155,000 and 94,000 D. The 155,000-D subunit is closely associated with the human complement receptor that recognizes C3bi and/or a further degradation product termed C3dg (C3bi receptor); the 94,000-D subunit has been shown to be shared, on normal cells, by two other surface membrane glycoproteins: lymphocyte function-associated antigen-1 (LFA-1) and P-150, 95. Both subunits of Mo1 were deficient on the patient's granulocytes as determined by immunoprecipitation with subunit-specific monoclonal antibodies as well as fluorescence analysis. Mol-deficient monocytes, like granulocytes, had defective C3-and IgG-dependent phagocytosis. Natural killing activity by the patient's peripheral blood leukocytes was normal. Mo1-deficient granulocytes and monocytes rosetted normally with sheep erythrocytes coated with C3bi. This rosetting was totally inhibited by a mixture of anti-Mo1 and anti-C3b (the major fragment of C3) receptor antibodies but not by either antibody alone. Since monoclonal antibodies to the 155,000-D subunit of Mo1 can inhibit C3bi receptor binding, immune phagocytosis, opsonized zymosan-induced degranulation, and superoxide generation by normal phagocytes (functions which are defective in Mo1-deficient cells), it appears likely that Mo1 deficiency may in part underlie the functional aberrations leading to recurrent bacterial infections in man.
 ...
PMID:Deficiency of a surface membrane glycoprotein (Mo1) in man. 636 Oct 68

The review considers the results of both genetical and biochemical studies of translation termination in pro- and eukaryotes. The available information on the components of the protein synthesis machinery, participating in the termination process is summarized. Special attention is paid to the problem of nonsense codon recognition. The possibility of modulation of the process of termination in vivo and in vitro is discussed. All the data considered allow us to propose the hypothesis about the role of the small ribosomal subunit RNA (SrRNA) in translation of natural messengers. Deficiency of AGG and related codone in prokaryotes suggests the possibility of scanning of mRNA's in the coding frame by the 3'-terminus of SrRNA. The context of natural terminators in mRNA's in pro-and eukaryotes reveals that the sequences between 6th and 20th positions both up- and down stream from the nonsense codons are complementary to the 3'-end of SrRNA. Interaction between 3'-terminus of SrRNA and the sequences under consideration is postulated to be important for high efficiency termination of translation.
Mol Biol (Mosk)
PMID:[Mechanisms of translation termination]. 701 69

It has been shown in the previous paper that if one Drosophila chromosome lacks histone genes, the intact homologous chromosome has an increased number of histone genes. The present study shows that the extent of compensatory multiplication of histone genes depends on the nature of the deficient chromosome. An extra Y chromosome in the genome of flies without the deficiency does not affect their histone gene content. In heterozygotes with a deficiency of histone genes the number of these genes grows gradually and reaches 90% of the norm in the eight generation (magnification). After the deficient chromosome is eliminated the increased number of histone genes is not stably inherited and reverts to the normal level in the course of 5--7 generations. Deficiency-heterozygous males of the first generation contain extrachromosomal histone DNA and have a changed ratio of the two types of histone gene blocks. The multiplication of histone genes is compared with the compensation and magnification of rDNA.
Mol Biol (Mosk)
PMID:[Changing number of histone structural genes in Drosophila]. 709 58

Senile plaques, a hallmark of Alzheimer's disease (AD), contain amyloid beta-peptide (A beta), which is generated from the larger amyloid beta protein precursor (APP). In addition to APP, several APP-related proteins have been recently identified in different organisms, including Drosophila amyloid precursor protein-like protein (APPL). Deficiency of APPL causes behavioral deficits in Drosophila, implicating a role in brain function. Moreover, mouse and human cDNA clones encoding amyloid precursor-like proteins (APLP1 and APLP2) have been identified and exhibit extensive sequence similarity to the APPL and APP genes. To define the potential role of APLP in the mammalian brain, we sought to directly localize APLP1 within the complex cortical synaptic structure. We focused on the postsynaptic density (PSD), which appears to be central to synaptic function. We now report that the 90 kDa APLP1, the first known APLP, is localized to the PSD from rat and human cerebral cortex. APLP1 increased during cortical synaptic development, suggesting a role in synaptogenesis or synaptic maturation. In contrast, APP was predominantly expressed in the synaptic membrane fraction, but was barely detectable in the PSD, including different subcellular distributions of APP and APLP1. Our observations raise the possibility that APLP1, a homologue of APPL, which appears to be necessary for normal behavior in Drosophila, participates in brain synaptic function in mammals.
Brain Res Mol Brain Res 1995 Aug
PMID:Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density. 749 61


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>