Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.6.1.3 (ATPase)
65,361 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Myosin has been purified from the following cultured cell lines: normal rat kidney fibroblast (NRK), HeLa-Rhino (HeLa), human choriocarcinoma, human acute lymphoblastic leukemia, rat hepatoma (HTC), monkey kidney (VERO), pigmented mouse melanoma, Y-1 rat adrenal cortex, and growth hormone-secreting GH-1. Myosin constitutes 0.5-5.4% of the protein of these cells. It was not detected in washed human erythrocytes or in two types of mouse plasmacytoma cells. Two methods for the purification of myosin from cultured cells have been employed. With Method I highly purified myosin was prepared by Sepharose 4B and DEAE-cellulose chromatography from 10(10) L-929 cells as well as from mouse uterus. Those myosins have similar molecular and subunit weights as well as ATPase activity but are immunologically distinct. Method II involving ultracentrifugation and Sepharose 4B chromatography, is suitable for the production of moderately pure myosin in good yield from as few as 5-10(7) cells (five 100-mm Petrie dishes).
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PMID:The purification and quantitation of myosin from cultured cells. 13 88

Indian River male broiler chickens growing from 7 to 28 d of age were fed on diets containing energy:protein values varying from 43 to 106 MJ/kg protein and containing 0 or 1 mg triiodothyronine (T3)/kg diet to study effects on growth, metabolic hormone concentrations and in vitro lipogenesis. In vitro lipid synthesis was determined in liver explants in the presence and absence of ouabain (Na+, K(+)-transporting ATPase (EC 3.6.1.37) inhibitor) to estimate the role of enzyme activity in explants synthesizing lipid. Growth and feed consumption increased (P < 0.01) when the energy:protein value decreased from 106 to 71 MJ/kg protein; however, both variables decreased as the value was further decreased from 53 to 43 MJ/kg protein. Triiodothyronine depressed (P < 0.01) growth, but not food intake. Large energy:protein diets (> 53 MJ/kg protein) and dietary T3 lowered (P < 0.01) plasma growth hormone. Large energy:protein diets (> 53 MJ/kg protein) increased (P < 0.01) lipogenesis, plasma growth hormone (GH) and decreased plasma insulin-like growth factor 1 (IGF-1). Also, T3 decreased plasma GH, IGF-1 in vitro lipogenesis. Ouabain inhibited a greater proportion of in vitro lipogenesis in those explants synthesizing fat at a high rate. Both dietary T3 and in vitro ouabain decrease lipogenesis, but, when combined, the effects are not cumulative.
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PMID:In vitro lipid metabolism, growth and metabolic hormone concentrations in hyperthyroid chickens. 133 68

1. The involvement of gill (Na+ +K+)-ATPase in salmonid adaptation to salt water (SW) is discussed. 2. Gill (Na+ +K+)-ATPase increase during SW adaptation is mainly related to the increased number and complexity of chloride cells deputed to salt extrusion. 3. The temporal relationships between serum peaks of thyroid hormones, cortisol, growth hormone, prolactin and gill (Na+ +K+)-ATPase rise during salmonid smoltification, suggest a hormonal involvement in the enzyme stimulation and thus in the acquirement of SW tolerance. 4. Literature on gill (Na+ +K+)-ATPase response to hormonal treatment is reviewed. The effects produced on gill (Na+ +K+)-ATPase and chloride cells by exogenous hormones point out a complex inter-relationship between the hormones considered. The mechanisms involved in hormonal regulation of the enzyme remain a matter of debate.
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PMID:Gill (Na+ +K+)-ATPase involvement and regulation during salmonid adaptation to salt water. 135 28

The effects of chronic growth hormone (GH) hypersecretion on intrinsic contractile properties of the myocardium were studied in rats bearing a GH-secreting tumour. Body weight and heart weight increased, but no true cardiac hypertrophy was observed. The maximum active force of left ventricular papillary muscle was increased, and the maximum shortening velocity of the unloaded muscle was unaltered. This was despite a marked shift of the myosin isoforms towards the low ATPase activity V3 form, which was associated with a similar shift of myosin mRNAs. Total ATPase activity, measured on frozen sections, was unaltered suggesting, together with the results of the mechanical study, an increase in the number of active enzymatic sites. Studies performed on skinned fibres confirmed the increased myocardial contractility, thus suggesting that myocardial adaptation to chronic GH excess occurred, at least in part, at the level of the myofibrillar contractile apparatus.
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PMID:Effects of chronic growth hormone excess on cardiac contractility and myosin phenotype in the rat. 145 14

The regulation of energy metabolism in obesity may differ from normal condition in several respects. The synthesis of lipids may be enhanced due to a greater production of insulin, estrogens and cortisol and to a lack of dehydroepiandrosterone. Lipolysis is reduced in obese subjects by a decreased secretion of catecholamines, growth hormone, adipsin and cachectin. Inadequate intake of food and stress modify the T3/rT3 ratio. Oxidative phosphorylation and the production of ATP is modified, thermogenesis decreases due to a reduced synthesis of thermogenin. A decreased activity of substrate cycles and of the Na-K ATPase, is expected. Most of these disorders are normalized in post-obese patients. Many common drugs interfere with energy metabolism, namely those used in psychiatry and all hormones and their antagonists mentioned above and used for a long time. Obesity should not be considered as a simple result of overeating and lack of physical activity.
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PMID:[Energy metabolism in obesity]. 158 28

To determine whether growth hormone (GH) directly affects ammoniagenesis in the renal proximal tubule, ammonia production was measured in suspensions of isolated canine renal proximal tubule segments (IPTs) incubated with 2.5 mM L-glutamine and varying concentrations of human growth hormone (hGH). Ammonia production from IPTs significantly increased by nearly threefold in the presence of hGH (10(-6) M) at 60 min. This increase was dose dependent, with as little as 10(-9) M hGH significantly stimulating ammonia production. In addition, hGH enhanced glucose production when lactate, alanine, and succinate replaced L-glutamine as substrate. hGH significantly stimulated ammonia production when IPTs were incubated at alkalotic and neutral pH. The effect of hGH was lost at acidic pH. When hGH was added to IPTs incubated under Na(+)-equilibrated conditions, ammonia production was not different from control. hGH stimulated ouabain-sensitive Na(+)-K(+)-adenosinetriphosphatase (ATPase) activity by 8.1 +/- 1.1% in basolateral membranes isolated from IPTs. hGH stimulation of proximal tubule ammonia production from L-glutamine occurs at physiological concentrations of hGH and when the extracellular-to-intracellular Na+ gradient favors L-glutamine transport. This effect is associated with an increase in basolateral Na(+)-K(+)-ATPase activity. The data suggest a role for hGH in the regulation of renal acid-base metabolism under physiological conditions in which increased net acid excretion is important.
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PMID:Growth hormone regulates ammoniagenesis in canine renal proximal tubule segments. 159 Apr 30

In March, sexually immature sea trout presmolts (Salmo trutta trutta) were injected every second day with saline, 2 micrograms 17 beta-estradiol (E2)/g, 2 micrograms ovine growth hormone (GH) + 6 micrograms cortisol (F)/g, or all three hormones (E2-GH-F) simultaneously. A SW-challenge test was performed after six injections. At the time of SW-transfer, high total plasma calcium levels in E2- and E2-GH-F-treated fish indicated activated vitellogenesis in these groups. All control, GH-F, and E2-GH-F-treated fish survived SW-transfer, whereas 43% of the E2-treated fish died after transfer. On Day 2 after transfer, there were marked differences among groups in their osmoregulatory response. Changes in ion-osmotic parameters (plasma Na+, Cl-, Mg2+, and total calcium and muscle water) indicated the following degree of osmotic stress: E2 greater than control greater than E2-GH-F greater than GH-F, which was inversely correlated with pretransfer gill Na+/K(+)-ATPase activity: GH-F greater than E2-GH-F greater than control greater than E2. On Day 7 after transfer there were no major differences among the groups with regard to plasma ions and muscle water content. The detrimental influence of elevated plasma E2 levels on hypo-osmo-regulatory physiology may indicate an important role of E2 during development.
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PMID:Opposite effects of 17 beta-estradiol and combined growth hormone-cortisol treatment on hypo-osmoregulatory performance in sea trout presmolts, Salmo trutta. 165 56

In the present study, we demonstrate the localization of Ca(++)-ATPase in the anterior pituitary of the male rat. Ca(++)-ATPase was mainly distributed on the membrane system of the granular cells, which included the plasma membrane, the outer mitochondrial membrane, the enveloping membrane of secretory granules, the smooth endoplasmic reticulum and some components of the Golgi complex. No reaction product was detected on the membrane of the rough endoplasmic reticulum or that surrounding the lysosomes. A positive reaction was clearly observed on the membranes surrounding 'large' secretory granules, while that present on the membranes of the 'small' granules was comparatively weak. The cells which contained the 'large' granules were interpreted as growth hormone-secreting cells and those in which the 'small' granules were located as gonadotrophs. There were either no reaction or one that was barely detectable on the plasma membrane of the folliculo-stellate cells. These data along with our previous findings (Soji, 1982, 1984) suggest that the membranous enzymes are not uniformly distributed over all pituitary cells but rather are specific for a given cell population(s).
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PMID:Cytochemistry of Ca(++)-dependent adenosine triphosphatase (Ca-ATPase) in rat anterior pituitary cells. 182 79

The effect of chronic high plasma corticosteroids' concentration upon renal function was studied in rats bearing a transplantable pituitary mammotropic tumor which produces large quantities of ACTH and prolactin (MtTF4S). Kidney splanchnomegaly and degenerative changes of renal cortex, particularly in proximal tubules, as well as cytolysis and appearance of vacuoles were noticed in tumor bearing rats. (Na+ + K+)-ATPase activity in renal plasma membranes decreased 67% in rats with a tumor secreting ACTH and prolactin, and 64% in rats with a tumor secreting growth hormone and prolactin when compared with controls. After adrenalectomy of MtTF4S rats, kidney weight as well as plasma concentrations of urea, sodium, chloride and phosphate ions were normalized indicating the involvement of adrenal glands in the development of disturbances in renal function.
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PMID:Kidney damage in rats bearing an adrenocorticotropin and prolactin secreting tumor. 196 5

Somatic mutations in a subset of growth hormone (GH)-secreting pituitary tumors convert the gene for the alpha polypeptide chain (alpha s) of Gs into a putative oncogene, termed gsp. These mutations, which activate alpha s by inhibiting its guanosine triphosphatase (GTPase) activity, are found in codons for either of two amino acids, each of which is completely conserved in all known G protein alpha chains. The likelihood that similar mutations would activate other G proteins prompted a survey of human tumors for mutations that replace either of these two amino acids in other G protein alpha chain genes. The first gene so far tested, which encodes the alpha chain of Gi2, showed mutations that replaced arginine-179 with either cysteine or histidine in 3 of 11 tumors of the adrenal cortex and 3 of 10 endocrine tumors of the ovary. The mutant alpha i2 gene is a putative oncogene, referred to as gip2. In addition, gsp mutations were found in 18 of 42 GH-secreting pituitary tumors and in an autonomously functioning thyroid adenoma. These findings suggest that human tumors may harbor oncogenic mutations in various G protein alpha chain genes.
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PMID:Two G protein oncogenes in human endocrine tumors. 211 65


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