Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011570 (depression)
 172,036 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Experiments were conducted to determine the influence of immunologic stress on methionine and lysine requirements of growing chicks. Immunologic stress was elicited by injection of either Escherichia coli lipopolysaccharide or heat-killed Staphylococcus aureus every other day for 6 d. In the first experiment, diets were formulated to provide methionine levels of 0.30, 0.50 and 0.70%. In the second experiment, diets contained 0.75, 0.90 or 1.2% lysine. In chicks fed amino acid-sufficient diets, those chicks injected with immunogens had slower growth, lower feed intake and poorer efficiency of feed utilization than those injected with saline. The decreases due to immunogens were diminished in chicks fed amino acid-deficient diets. The methionine requirements of saline- and immunogen-injected chicks were above 0.5% and between 0.3 and 0.5%, respectively; the lysine requirements were greater than 0.95% and between 0.7 and 0.95%, respectively. Thus immunogen injection decreased methionine and lysine requirements, probably because of a decreased need of amino acids for growth and tissue accretion. Immunogen-induced depression in serum zinc and increase in serum copper levels were ameliorated by lysine or methionine deficiencies. Compared with saline-injected chicks, immunogen-injected chicks had significantly higher serum interleukin-1 (IL-1) activity by 53% when fed the methionine-sufficient diet, but they did not have significantly greater IL-1 levels when fed the methionine-deficient diet. These observations indicate that the diminished expression of immunologic stress in amino acid-deficient chicks is due to an impaired immune response.
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PMID:Decreased amino acid requirements of growing chicks due to immunologic stress. 245 41

Two experiments were conducted using corn from clean or aflatoxin B1 (AFB1)-contaminated (182 ppb) sources. Weanling pigs (28 d) were fed one of eight dietary treatments arranged in a 2 x 2 x 2 factorial design. In Exp. 1 (192 pigs), treatments varied in corn source (clean or AFB1-contaminated), CP level (18 or 20%) and added fat (0 or 5%). At the end of the 28-d growth trials, plasma samples were obtained. An AFB1 x CP level interaction was detected (P less than .05) for growth rate (ADG), feed intake (FI) and feed/gain ratio (F/G). Feeding AFB1 reduced (P less than .05) ADG (.30 vs .37 kg/d) and FI (.57 vs .66 kg/d) and increased F/G (1.88 vs 1.78) of pigs fed 18% CP diets. Performance of pigs fed 20% CP diets was not altered by AFB1. Adding 5% fat to diets improved (P less than .05) F/G but did not improve ADG of pigs fed AFB1. There was an AFB1 x CP x fat interaction (P less than .05) for plasma cholesterol. Adding fat or increasing the CP level prevented the depression of plasma cholesterol in pigs fed AFB1. In Exp. 2 (96 pigs), all diets contained 18% CP and the treatments varied in corn source (clean or AFB1-contaminated), added L-lysine HCl (0 or .25%) and added DL-methionine (0 or .15%). Feeding AFB1 reduced (P less than .05) ADG of pigs fed the 18% CP diet (.44 vs .50 kg/d) but not of pigs fed diets supplemented with .25% lysine.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Influence of dietary protein, fat or amino acids on the response of weanling swine to aflatoxin B1. 249 62

Neurons with co-localized cholecystokinin (CCK) and dopamine (DA) are present predominantly in the ventral tegmental area (VTA) and project mainly to the caudal part of the medial nucleus accumbens. The activity of this dopaminergic system can be evaluated by means of the intracranial self-stimulation behaviour (ICSS) on male Wistar rats having chronic electrodes implanted into the medial forebrain bundle in the postero-lateral area of the hypothalamus. The direct injection of the CCK analogue BOC(Nle28;Nle31)CCK27-33 (BDNL-CCK7) into a lateral ventricle decreased the electrical self-stimulation of the medial forebrain bundle. Nevertheless, this decrease in self-stimulation was steeper (immediately after the injection vs a delay of +/- 5-10 min.) than the CCK8-induced ICSS depletion. The intracerebroventricular (ICV) injection of 150 pmol and 1000 pmol BC-197 (BOC-D.Asp-Tyr(SO3H)-Nle-D.Lys-Trp-Nle-Asp-Phe-NH2) was ineffective to modify the self-stimulation behaviour when administered alone while a 150 pmol BC-197 dosage was able to antagonize the decreasing effect of 150 pmol CCK-8 on ICSS. Nevertheless, a dosage 6 times as important, i.e. 1000 pmol BC-197, was needed to antagonize the depression induced by 150 pmol BDNL-CCK7 on ICSS behaviour. These results support the equipotence of BDNL-CCK7 to CCK-8 in decreasing the self-stimulation behaviour after their direct administration into the lateral ventricle. They further give evidence of the relevance of BC-197 in antagonizing the respective effects of both compounds on the ICSS.
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PMID:Similar potencies of CCK-8 and its analogue BOC(Nle28;Nle31)CCK27-33 on the self-stimulation behaviour both are antagonized by a newly synthesized cyclic CCK analogue. 273 84

Using isolated polypeptides of the F0 sector of bovine heart mitochondrial H+-ATPase, antisera were developed detecting specifically two components of F0. These two components were identified as F0I and oligomycin-sensitivity-conferring protein (OSCP) respectively. Both F0I and OSCP were digested by mild trypsin treatment of submitochondrial particles depleted of the catalytic part of H+-ATPase (USMP). Proteolysis was largely prevented by binding of F1 to F0. Proteolysis of F0I resulted in the formation of three immunoreactive, membrane-bound fragments of apparently 26 kDa, 25.5 kDa and 18 kDa, respectively, indicating that F0I contains trypsin-accessible Arg or Lys residues located close to the end and the middle part of the protein, respectively, which are in intimate contact with F1. Digestion of USMP with trypsin resulted in depression of passive H+ conduction through F0 which could be ascribed to proteolysis of F0I.
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PMID:Topological and functional characterization of the F0I subunit of the membrane moiety of the mitochondrial H+-ATP synthase. 289 6

We have examined the sites phosphorylated on acetyl-CoA carboxylase by three protein kinases which have been shown to inactivate the enzyme, i.e. cyclic-AMP-dependent protein kinase, acetyl-CoA carboxylase kinase-2 (ACK2, purified from rat mammary gland) and the AMP-activated protein kinase (formerly called acetyl-CoA carboxylase kinase-3, purified from rat liver). Each protein kinase phosphorylates two out of three sites (termed 1-3) which have been established by amino acid sequencing. The two sites phosphorylated by each kinase can be recovered on separate peptides, TC1 and TC2, derived by combined digestion of the native enzyme by trypsin and chymotrypsin: TC1 = Ser-2Ser(P)-Met-3Ser(P)-Gly-Leu; TC2 = Arg-Met-1Ser(P)-Phe- Cyclic-AMP-dependent protein kinase phosphorylates sites 1 and 2 exclusively, whereas the AMP-activated protein kinase phosphorylates sites 1 and 3, plus at least one other minor site. ACK2 phosphorylates site 1 and, more slowly, an unidentified site(s) within TC1. We have also established the structures of the single major phosphopeptides (T1 and C1 respectively) which are recovered by HPLC after acetyl-CoA carboxylase phosphorylated by cyclic-AMP-dependent protein kinase is digested with trypsin or chymotrypsin alone. T1 is related to TC1, and has the structure: Ser-Ser(P)-Met-Ser-Gly-Leu-His-Leu-Val-Lys. C1 is identical with TC2. We have carried out studies on the correlation of the activity of acetyl-CoA carboxylase with the occupancy of sites 1, 2 and 3 during phosphorylation by each of the three protein kinases. The results suggest that phosphorylation of site 3 is primarily responsible for the large decrease in Vmax produced by the AMP-activated protein kinase, while phosphorylation of site 1 may be primarily responsible for the increase in A0.5 for citrate and more modest depression of Vmax produced by cyclic-AMP-dependent protein kinase and ACK2. Our results emphasize that amino acid sequence information is essential in the unequivocal interpretation of data from phosphopeptide mapping experiments and allow a more complete interpretation of previous data on phosphorylation of acetyl-CoA carboxylase in intact cells. They also open the way to experiments which could establish the physiological roles of these protein kinases in the control of fatty acid synthesis.
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PMID:Identification by amino acid sequencing of three major regulatory phosphorylation sites on rat acetyl-CoA carboxylase. 290 Jan 38

Several animal studies have demonstrated that pain is modulated by spinal mechanisms involving prostaglandins and that acetylsalicylic acid (ASA) administered intrathecally has an analgesic effect. We report our experience of this treatment in 60 patients with proven and advanced cancer. An isobaric solution of lysine acetylsalicylate was administered by lumbar puncture in doses ranging from 120 to 720 mg of ASA. The results were evaluated using the habitual criteria: scoring system, behaviour, consumption of analgesic drugs. In this trial the method proved astonishingly effective (78% of the cases). Analgesia was strong, almost immediate and without influence on motricity. No thermic or neurovegetative changes were noted. The effect of one injection lasted from 3 weeks to 1 month on average; it was reproduced and often more prolonged after a repeat injection. Pain associated with bone metastases seems to constitute the best indication, notably in breast and lung cancer and in myeloma. Visceral (pancreas) or neural pain requires higher doses to respond. Failures (22%) were due to such factors as insufficient dosage at the very beginning of our experience or severe depressive syndrome. The perineal and sphincteral pain of rectal cancer often resists treatment. This simple, inexpensive and very effective method with no other complication than a frequent tendency to fatigue should rank among other analgesic measures in cancer. The lack of respiratory depression is a major advantage over catheter spinal opiate analgesia. We consider that its main indications are pain associated with osteolytic metastases of adenocarcinomas, and myelomas. Owing to the absence of formal toxicological data, its use must be limited to cancer pain and to patients with a life expectancy of less than 2 years.
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PMID:[Chronic refractory pain in cancer patients. Value of the spinal injection of lysine acetylsalicylate. 60 cases]. 295 75

The effect of tumor-promoting phorbol diesters to potentiate the action of epidermal growth factor (EGF) on cell proliferation is associated with phosphorylation of EGF receptors, acute depression of EGF binding, and inhibition of EGF receptor tyrosine kinase activity. In the present studies, normal human fibroblasts and A431 carcinoma cells were labeled with [32P]phosphate and treated with and without 10 nM 4 beta-phorbol 12 beta-myristate 13 alpha-acetate (PMA). The EGF receptors then were isolated by immunoprecipitation and digested with trypsin. Analysis of the labeled receptor phosphopeptides by reversed-phase HPLC revealed that PMA induces the phosphorylation of a unique phosphopeptide containing [32P]phosphothreonine. Comparison of several chemical and physical properties of the 32P-labeled phosphopeptide with the primary structure of the EGF receptor suggested the identify Lys-Arg-Thr(P)-Leu-Arg. This was confirmed by direct demonstration that a synthetic peptide of this structure comigrates during HPLC and electrophoresis with the 32P-labeled phosphopeptide isolated from the EGF receptors of normal human fibroblasts. The phosphorylated site on the peptide corresponds to threonine-654 of the EGF receptor, which is located on the cytoplasmic side of the plasma membrane nine residues distant from the transmembrane domain. These data indicate that phosphorylation of the EGF receptor in human fibroblasts and A431 cells at threonine-654 may regulate the EGF receptor tyrosine kinase activity and the binding of EGF.
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PMID:Tumor-promoting phorbol diesters cause the phosphorylation of epidermal growth factor receptors in normal human fibroblasts at threonine-654. 298 76

The cytogenetic effects of methyl acetimidate (MAI), a lysine-specific protein crosslinking reagent, were investigated using human peripheral lymphocytes in culture. Lymphocytes were treated with the chemical either prior to PHA exposure or 2-3 days following mitogenic stimulation and assessed for perturbations in cellular proliferation and induction of SCEs. Severe reductions in the mitotic index (MI) and pronounced decreases in the proportion of metaphases proceeding beyond M(1) were observed following G0 exposure to MAI concentrations of as low as 2 mM; with complete suppression of mitotic activity in all cultures exposed to levels of 3 mM MAI or greater. Concentrations resulting in severe depression in MI caused only moderate increases in SCEs. Cells exposed to less than 10 mM MAI during the late S-G2 stages of the cell cycle and harvested at the first metaphase following treatment exhibited profound mitotic delay, impaired prophase to metaphase transitions and abnormal mitotic configurations. These findings demonstrate that protein-specific crosslinking agents may induce a wide spectrum of adverse cytogenetic outcomes in both cycling and noncycling lymphocytes.
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PMID:Cytogenetic evaluations in human lymphocytes exposed to methyl acetimidate, a lysine-specific protein crosslinking agent. 311 24

1. Two experiments were conducted to determine the effects of heat on the nutritional value of lupin (Lupinus angustifolius cv. Uniharvest and Unicrop)-seed meal, relative to soya-bean meal, for growing pigs 2. In both experiments, values for carcass gain/d and food conversion ratio (FCR) on a carcass basis of pigs fed on the diets containing lupin-seed meal were inferior (P less than 0.05) to those produced by pigs fed on soya-bean meal. 3. In the first experiment, heating lupin seed at temperatures from 105 to 150 degrees for 15 min resulted in a linear depression in carcass gain/d, a quadratic increase in carcass FCR, a linear decrease in lean in the ham and a linear increase in backfat thickness. In the second experiment, autoclaving lupin seed from 5 to 45 min at 121 degrees resulted in a linear depression in carcass gain/d and a linear increase in carcass FCR. 4. The addition of L-lysine to the diets containing lupin-seed meal verified that lysine was limiting in both experiments. The additions of L-lysine did not overcome the differences in carcass gains/d of pigs fed on lupin-seed meal relative to those fed on diets containing soya-bean meal. 5. It is concluded that the low lysine availability in lupin-seed meal for pigs is not due to the presence of heat-labile anti-nutritional factors in the seed.
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PMID:Effect of heat on the nutritional value of lupin (Lupinus angustifolius)--seed meal for growing pigs. 311 97

Three chick growth assays were conducted to investigate the effects of monensin on lysine and arginine utilization in crossbred chicks (New Hampshire X Columbian). Chicks were fed either a low lysine corn-sesame meal diet containing graded increments of crystalline lysine.HCl (Assay 1) or an arginine-deficient casein-dextrose diet (Assay 2) supplemented with graded levels of L-arginine.HCl in the presence or absence of supplemental monensin (121 mg/kg). Based upon analysis by slope-ratio methodology (i.e., gain regressed on supplemental amino acid intake), the efficiency of L-lysine or L-arginine utilization was found to be the same in both monensin-fed and control chicks. In Assay 3, effects of monensin on the lysine-arginine antagonism were studied. Chicks were fed an arginine-deficient casein-dextrose diet supplemented with 1 or 2% L-lysine.acetate in the presence or absence of supplemental monensin. Growth performance was depressed by feeding both levels of supplemental L-lysine.acetate. Monensin had no effect on the magnitude of the growth depression caused by supplemental lysine. These results support the view that neither lysine nor arginine utilization is impaired by feeding monensin.
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PMID:In vivo utilization of lysine and arginine in young chicks fed monensin. 313 6


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