Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0009443 (cold)
 92,137 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The hepatocellular metabolic change after liver transplantation following 2 hr cold ischemia was investigated. Of 55 orthotopic liver transplantation in male Wistar rats, 47 animals were sacrificed at 3 hr, and 1, 2, 7 and 30 days to determine hepatic metabolite levels, in the form of adenine nucleotides, lactate and glycogen. Using the other 8 recipients, biochemical examinations were done at 1, 3, 5, 7, 30 and 60 days and metabolic levels estimated at 60 days. The SGOT and SGPT levels decreased gradually after a remarkable increase on the first postoperative day, while the alkaline phosphatase level revealed a peak value at 30 days. All levels recovered to within the normal range in 60 days. The total adenine nucleotide level reached the normal range within 3 hr following the blood reflow and remained at a normal level thereafter. However, all the metabolic levels apart from total adenine nucleotides deteriorated to reach their worst level at 7 days. The results of this investigation indicate that the posttransplanted deterioration of metabolic levels were possibly caused by the imperfect oxygenation due to cellular edema after blood reflow. However, the levels of these metabolites recovered within 60 days after transplantation.
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PMID:Hepatocellular metabolic change after orthotopic liver transplantation in rats. 204 Dec 42

The question of whether nonhydrolyzable nucleotide analogues and other nucleoside triphosphates support tubulin assembly was addressed. Tubulin which contained residual GTP at the exchangeable site polymerized in the absence of added GTP in the presence of DMSO or glycerol. After maximum absorbance was reached, disassembly occurred at a slow rate. When 0.5 mM GMPPCP, GMPPNP, or ATP was included in the assembly reaction, disassembly did not occur, and about 0.1 mol of these nucleotides per mole of tubulin was incorporated into the protein. When 5 mM nucleotide was used or alkaline phosphatase was included in the case of the nonhydrolyzable analogues, a greater amount of assembly occurred and about 0.7-0.8 mol of analogue was incorporated. The products of the assembly reaction were cold-labile microtubules and protofilament ribbons. After cold-depolymerization of the microtubules and ribbons, a second cycle of assembly produced some microtubules, but cold-stable amorphous polymers were the major product. In addition, when GTP at the exchangeable site was first removed by a cycle of assembly, followed by depolymerization, assembly in the presence of GMPPCP, GMPPNP, or ATP produced a mixture of microtubules and cold-stable polymers, both of which contained bound analogue. Incorporation of GMPPCP, GMPPNP, or ATP into polymerized tubulin always occurred at the expense of GDP at the exchangeable site, the content of which decreased correspondingly. Incubation of tubulin with 5 mM GMPPCP, GMPPNP, or ATP under nonassembly conditions also displaced GDP.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:GTP analogues interact with the tubulin exchangeable site during assembly and upon binding. 210 23

Ultracytochemical features of microvessels and tumor cells of the human meningiomas were examined by light and electron microscopy with special reference to the distribution of Mg2(+)-ATPase and alkaline phosphatase (ALPase) activity on the walls of the vessels and tumor cell surfaces. Materials used were 4 cases of meningiomas, 2 of which were meningotheliomatous type, one fibroblastic type and one malignant meningioma respectively. For ultracytochemistry, specimens were quickly fixed in an ice-cold 0.1 M cacodylate buffer containing 8% sucrose (pH 7.2) for one hour and transferred to a substrate solution for detection of Mg2(+)-ATPase and ALPase. The preparations were incubated at 37 degrees C for 15-30 min in the medium described by Mayahara et al. for ALPase and for 15-20 min in the medium described by Wachstein and Meisel. The control samples were incubated in a medium containing 1 mM Bromotetramisole for ALPase and also in a substrate free medium for Mg2(+)-ATPase. At the light microscopy, Mg2(+)-ATPase and ALPase activities appeared to be mainly restricted to the capillary wall and around or in the tumor cell nest showing whorl formation. Both enzyme activities were negative in the control study. By electron microscopy, reaction products representing Mg2(+)-ATPase activity were distributed in the basolateral plasma membrane of the endothelial cells on the surface of the pericytes and on the surface of the tumor cells. Reaction products of ALPase activity located mainly on the abluminal surfaces of the endothelial cells and in some specimen on both luminal and abluminal surfaces of those cells. Intense reaction products were distributed evenly on all round surfaces of the tumor cells.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Cytochemical study of Mg2(+)-ATPase and ALPase activity in human meningiomas]. 214 82

Cold-sensitive mutations in the secD locus of Escherichia coli result in severe defects in protein export at the non-permissive temperature of 23 degrees C. DNA sequence of a cloned fragment that includes the secD locus reveals open reading frames for seven polypeptide chains. Both deletions and TnphoA insertions in this clone have been used in maxicell and complementation studies to define the secD locus and its products. The secD mutations fall into two complementation groups, defining genes we have named secD and secF. These two genes comprise an operon, the first case of two genes involved in the export process being co-transcribed. The DNA sequence of the two genes along with alkaline phosphatase fusion analysis indicates that they code for integral proteins of the cytoplasmic membrane. We suggest that these two proteins may form a complex in the membrane which acts at late steps in the export process.
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PMID:The secD locus of E.coli codes for two membrane proteins required for protein export. 224 73

Complete replacement of the nucleotide on the exchangeable binding site of purified calf brain tubulin by the non-hydrolyzable GTP-analogue guanylyl-(beta,gamma-methylene)diphosphonate (GMPPCP) has been achieved by treatment of tubulin-GDP with phosphodiesterase-free alkaline phosphatase. GMPPCP binds to tubulin with a low affinity relative to GTP or GDP. Binding of the analogue is linked to magnesium ion concentration and, like the binding of other guanine nucleotides, is promoted by high concentrations of glycerol. The complex of pure tubulin and GMPPCP readily assembles at 37 degrees C into microtubules or curled ribbons of protofilaments, depending on buffer composition. Assemblies are cold-reversible at 0-2 degrees C, and multiple reversible assemblies can be observed during repeated heating/cooling cycles.
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PMID:Interactions of tubulin with guanylyl-(beta-gamma-methylene)diphosphonate. Formation and assembly of a stoichiometric complex. 233 45

The effects of temperature acclimation of carp upon the hydrocarbon order of intestinal membranes has been determined. A fractionation technique has been developed for the simultaneous purification of brush-border and basolateral membrane fractions from the intestinal mucosa. The specific activity of alkaline phosphatase in the brush-border fraction was enhanced 6.4-fold over that of the initial homogenate, whilst the (Na(+)-K+)-stimulated ATPase was enhanced 5.8-fold in the basolateral fraction. The specific activities of NADPH-cytochrome-c reductase, succinate-cytochrome-c reductase and acid phosphatase were not increased in these two fractions. Membrane hydrocarbon order in membranes from 10 and 30 degrees C-acclimated carp has been compared by measuring the steady-state fluorescence polarization of 1,6-diphenyl-1,3,5-hexatriene over a range of temperatures. In the brush-border fraction, polarization was identical in both cold- and warm-acclimated groups, whilst large differences were observed in the basolateral fraction sufficient to offset approx. 75% of the temperature-induced ordering effects of cold. The fatty acid composition of the major phosphoglyceride fractions in the brush-border fraction was also largely unaffected by thermal acclimation, whilst the basolateral fraction showed significant increases in the proportion of unsaturated fatty acids in the cold. It is concluded that whilst the basolateral membrane of intestinal mucosa displays a large homoeoviscous response that correlates with a shift in lipid composition, the brush-border membrane does not. These findings are consistent with evidence of functional adaptations of the basolateral membrane during thermal acclimation (Gibson, J.S., Ellory, J.C. and Cossins, A.R. (1985) J. Exp. Biol. 114, 355-364).
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PMID:Temperature adaptation of biological membranes: differential homoeoviscous responses in brush-border and basolateral membranes of carp intestinal mucosa. 237 86

Small cultures of human amniotic cells were preincubated for 24 h. Human prolactin was then added to the medium. After a further short period of incubation the tubes were chilled, the medium removed and the cells rinsed with saline. The tubes then received cold Tris-sucrose and were frozen, to disrupt the cells. After thawing, adenosine triphosphatase (ATPase) and p-nitrophenyl phosphatase (PNPase) were measured. Buffer was added containing either ATP or PNP and the tubes were incubated for 30 min. Inorganic phosphate released from ATP and p-nitrophenol was measured spectrophotometrically. Prolactin stimulated both enzyme activities. The ATPase log dose-response curve was linear between approximately 12.5 and 200 mIU/l. It was inhibited by ouabain. Isobutyl-1-methylxanthine inhibited the ATPase but not the alkaline phosphatase activity. One of these human amniotic cell enzymes may provide the basis for a sensitive bioassay for human prolactin.
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PMID:Enzyme activation of human prolactin: a potential basis for a bioassay. 247 90

Incomplete warm hemolysins (IWHs) form an independent class of red blood cell (RBC) autoantibodies. We studied eight sera in which autoantibodies with the characteristic features of IWHs were demonstrated. The case reports of those patients revealed that IWHs were predominantly associated with a serious course of autoimmune hemolytic disease. In four sera we found a combination of IWHs and cold agglutinins with the specificity anti-I. The cold agglutinins could be separated from the IWHs by affinity chromatography with immobilized I-active RBC material. The binding of IWHs to RBCs was demonstrated on the RBC surface with a modified enzyme-linked immunoassay (APAAP-EIA: monoclonal anti-immunoglobulin antibodies + bridging antibody + alkaline phosphatase/anti-alkaline phosphatase complexes). With the APAAP-EIA technique and different primary anti-immunoglobulin antibodies we found that seven sera contained IgM-IWHs and one contained IgG-IWHs. In three sera, IgM-IWHs with monotypical kappa light chains were detected.
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PMID:Incomplete warm hemolysins. I. Case reports, serology, and immunoglobulin classes. 249 9

The nasal passages are anatomically complex, and while there have been a number of descriptions of nasal structure in many species, there is very little information available on the distribution of enzymes in the nasal mucosa. In rodents, this delicate mucosa is the first site within the respiratory tract to be exposed during inhalation toxicology studies designed to assess human risks from such exposures. However, the nasal mucosa presents problems for histologic preparation because it is encased in brittle bones. Because of recent interest in the nose as a target site, and findings from biochemical studies which indicate that the nose is very active metabolically, studies were carried out to determine the value of cold glycol methacrylate (GMA) processing for localization of nasal enzymes. For these studies, liver and kidney were used as positive controls. Published histochemical procedures for acid and alkaline phosphatase, adenosine triphosphatase, glucose-6-phosphatase, gamma-glutamyl transpeptidase, and naphthyl butyrate esterase were applied, with modifications, to undecalcified nasal passages of Fisher-344 rats. Frozen sections exhibited excellent enzyme preservation but very poor morphology, while GMA gave good enzyme preservation and excellent morphology. For GMA, acetone fixation generally resulted in the best preservation of enzyme activity. It was concluded that cold GMA processing provides a useful approach to studies of nasal enzyme distribution and that this technique of value for inhalation toxicology studies. Details of enzyme distribution in the squamous, respiratory, and olfactory epithelia, associated glands, and other structures of the nose of the rat are described and discussed.
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PMID:Enzyme histochemistry of the rat nasal mucosa embedded in cold glycol methacrylate. 288 3

The authors have examined the enzyme histochemical staining of surgically removed human thyroid tissue in an attempt to identify markers that might be useful in the histopathologic diagnosis of thyroid neoplasms. Fresh thyroid glands and other tissues were fixed in cold (4 degrees C) 4% paraformaldehyde and embedded in glycol methacrylate. Forty-two specimens were studied in thin sections, which gave excellent histologic detail and enzyme preservation. Cytologic detail was similar to that in Papanicolaou-stained smears, with good definition of nuclear inclusions and grooves, particularly in cases of papillary carcinoma. The enzyme histochemical reactions studied were as follows: adenosine triphosphatase, alkaline and acid phosphatases, alpha-naphthyl acetate esterase, and 5'-nucleotidase. Thyroid epithelial cells and the benign neoplasms derived from them were typically positive for 5'-nucleotidase, alpha-naphthyl acetate esterase, and acid phosphatase, and negative for adenosine triphosphatase and alkaline phosphatase. Staining for adenosine triphosphatase was present in papillary and follicular carcinomas and was seen in benign glands only under certain circumstances such as Graves' disease. The adenosine triphosphatase reaction therefore appears to be helpful in distinguishing between benign and malignant neoplasms derived from thyroid epithelium in humans and may be a useful adjunct to routine morphology.
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PMID:Enzyme histochemistry and thyroid neoplasia. 301 Jun 99


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