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 influence of season, photoperiod and ambient temperature on the content of proteins, sialo-glycoproteins and gangliosides and on the composition of gangliosides of three different brain regions (cortex, cerebellum and basalbrain) of the Djungarian dwarf hamster (Phodopus sungorus) had been investigated. Concomittantly changes in body wt and fur colouration were recorded. Dwarf hamsters living under natural photoperiod and ambient temperature conditions ("outside") showed a distinct annual cycle in body wt (summer: about 45 g; winter: about 25 g) and fur colouration (summer: dark grey; winter: whitish). Among the three brain regions the mean concentration of proteins ranged between 120 and 155 mg protein/g wet wt. The sialo-glycoprotein content varied between 260 and 410 micrograms NeuAc/g wet wt, and that of gangliosides between 800 and 1650 micrograms NeuAc/g wet wt. Seasonal fluctuations were not found. The composition of brain gangliosides remained uninfluenced throughout the year in the cerebellum, whereas seasonal variations were observed in cortex and basalbrain. Consequently the concentration ratio of the two major mammalian ganglioside fractions GD1a vs GT1b remained almost stable in cerebellum (0.3). In contrast to this the seasonal values of cortex and basalbrain changed from 0.6 and 0.8 in winter to 0.7 and 1.1 in summer. This indicated a higher polarity of the gangliosides in these brain regions during cold adaptation. The results are discussed with regard to modulatory functions of neuronal gangliosides for the process of synaptic transmission during seasonal adaptation.
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PMID:Seasonal variability of sialo-glycoconjugates in the brain of the Djungarian hamster (Phodopus sungorus). 356 24

The cold agglutinin from the albumin gland of the snail Achatina fulica was purified to homogeneity by using sheep gastric mucin-Sepharose 4B as affinity column followed by gel filtration on Bio-Gel P-300. The homogeneity was checked by alkaline gel electrophoresis, immunodiffusion and immunoelectrophoresis. The purified cold agglutinin is a glycoprotein of native M2 220,000 consisting of three non-covalently bound subunits of Mr 84,000, 74,000 and 62,000 and having a pI value of 4.5. The predominant amino acids are aspartic acid and glutamic acid (or amides) and serine, which account for 39% of the residues. About 3% of the residues are half-cystine. The lectin is a glycoprotein with about 30.7% carbohydrate, the most abundant sugars being galactose, N-acetylgalactosamine and N-acetylglucosamine. Mannose, xylose and fucose are also present. The inhibition of agglutination of human umbilical-cord erythrocytes by the cold agglutinin is specific for methyl beta-D-galactoside and also for glycolipids present on cord erythrocytes. The c.d. data show only negative ellipticity values in the far-u.v. region for the protein at various concentrations and temperatures and also in the presence of the hapten lactose (at different concentrations), indicating the presence of a random-coil conformation in the agglutinin that varies according to temperature.
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PMID:Further characterization of the cold agglutinin from the snail Achatina fulica. 359 52

Lectin-binding sites located on the endothelial cell (EC) surfaces in unaltered, leaking and resorbing micro-blood vessels (MBVs) in cryo-injured cat brain were studied. Lectin or glycoprotein-gold complexes and brain samples embedded in hydrophilic resin Lowicryl K4M were used. The lectins tested recognize the following residues: beta-D-galactosyl (Ricinus communis agglutinin 120, RCA and peanut agglutinin, PNA), sialyl (Limax flavus agglutinin), N-acetyl-D-galactosaminyl (Helix pomatia agglutinin and soybean agglutinin, SBA), alpha-D-glucosyl and alpha-D-mannosyl (concanavalin A). The luminal front was labeled with SBA, and both fronts of the EC were labeled with PNA only after neuraminidase digestion. The most abundant and regularly distributed on both fronts of the EC were beta-D-galactosyl residues (RCA). These residues were also most affected in altered MBVs. The labeling of sialic acid residues was less pronounced on both sides of the EC. Following alteration of the function of the blood-brain barrier by cold-lesion injury, in leaking MBVs which represent increased luminal transport, we observed a conspicuous diminution of the labeling of the luminal surface of the EC with some lectins. On the other hand, in resorbing blood vessels located in the area of edema, where a presumably reverse (abluminal) transport occurs, major changes in the distribution of lectin-binding sites occurred on the abluminal front of the EC and in the basement membrane. The results reported here indicate that luminal and abluminal fronts of the EC change their properties in various functional conditions of MBVs, and that these changes can also be a reflection of functional polarity of brain endothelium.
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PMID:Changes in the distribution of endothelial surface glycoconjugates associated with altered permeability of brain micro-blood vessels. 373 20

Mucous glycoprotein (MGP) hypersecretion is a cause of chronic pulmonary obstructive disease and is also a common response of the pulmonary airways to toxicant-induced injury. To examine the feasibility of employing pulmonary lavage to assess the airway MGP content of the rat, the MGP removed from the lungs of male Sprague-Dawley rats by three successive lavages with cold isotonic saline were solubilized with urea and mercaptoethanol, and were purified by ultrafiltration and Sepharose CL-6B gel chromatography. MGP, which elute with the void volume of this gel, were quantitated by their carbohydrate content. Initial studies revealed that succeeding lavages removed succeedingly less MGP, suggesting that some pool of MGP was being washed out by this procedure. In a second study, isoproterenol was administered by a regimen known to produce MGP hypersecretion in the rat as assessed by histologic criteria (100 mg/kg/day, sc, for 6 days). Lavage MGP content of isoproterenol-treated rats averaged 450 micrograms compared to 210 micrograms in vehicle-treated controls (p = 0.01). In summary, it is possible to purify and quantitate the MGP removed from the airways of the rat by pulmonary lavage and the amount of lavagable MGP is approximately doubled by isoproterenol, an agent known to induce the morphologic signs of mucous hypersecretion.
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PMID:Quantitation of mucous glycoprotein removed from the respiratory tract of the rat by pulmonary lavage. 375 38

Human peripheral blood monocytes secrete a cell membrane-associated glycoprotein, cold insoluble globulin (fibronectin). Since fibronectin binds to gelatin-coated surface, we developed a simple technique for separation of human peripheral blood monocytes from whole mononuclear cell preparation. These preparations are characterized by a high monocyte purity (more than 90%), low platelet contamination and excellent viability.
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PMID:Purification of human monocytes on gelatin-coated surfaces. 379 46

Plasma fibronectin (FN) is one of the major blood opsonins. The content of the glycoprotein reduces in sepsis which in turn may aggravate the course of the infection. FN is detectable in the content of cryoglobulins and cryofibrinogen. The formation of the heparin precipitate following plasma incubation in the cold in the presence of heparin is determined by FN involvement. Fibrinogen (FG) is another main component of the heparin precipitate. To determine the functional activity of plasma FN in sepsis and other pathological conditions, a study was made of the ability of FN and FG to go into the precipitate formed in blood plasma in the cold after its incubation with heparin. Unlike normal subjects in whom over 80% of FN on the average and about 20% of FG went into the heparin precipitate, in patients with hemoblastoses and aplastic anemia complicated by sepsis, less than 40% of FN on the average and about 7% of FG went into the precipitate. In some patients with sepsis, the heparin precipitate did not form. The reduction of FN ability to go into the heparin precipitate correlated with the gravity of the patients' condition. In uncomplicated hemoblastoses, cryoglobulinemia and cryofibrinogenemia and in immunocomplex pathology, the consumption of FN and FG during heparin precipitate formation did not significantly differ from the control. The data indicate that sepsis patients with blood system pathology may develop not only quantitative FN deficiency in the blood but also disorder of the functional activity of the opsonin.
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PMID:[Decreased effectiveness of cold-induced heparin precipitation of plasma fibronectin in infection]. 379 36

Two A strain influenza viruses, A/Hong Kong/123/77 (A/HK/123/77) (H1N1) and A/Queensland/6/72 (A/Qld/6/72) (H3N2), and the two cold-adapted reassortants which possess the surface antigens of these strains (CR35 and CR6, respectively) were tested for their ability both to induce primary cytotoxic T-cell (Tc cell) responses in mice and to sensitize mice for a second Tc cell response when challenged with a distantly related A strain virus, A/Shearwater/72 (H6N5). After intranasal inoculation, A/Qld/6/72 replicated to higher titers in the lung (1 to 2 log10 50% egg infective doses) than did A/HK/123/77 or either of the reassortants. A/Qld/6/72 induced higher Tc cell responses in the lung than did CR6, and both were more effective than either A/HK/123/77 or CR35 in this respect. When similar doses (10 or 10(3) hemagglutinin units) of each virus were injected intravenously into mice and the spleens were tested for Tc cell activity 6 days later, both A/Qld/6/72 and CR6 were ca. 100-fold better at inducing a primary Tc cell response than A/HK/123/77 or CR35. In contrast, the H1N1 and H3N2 viruses gave rather similar anti-hemagglutinin antibody titers (after intravenous injection) and delayed-type hypersensitivity reactions (after subcutaneous injection). If mice were primed with a low dose of these viruses (10(4) 50% egg infective doses intranasally), A/Qld/6/72 and CR6 were more effective than A/HK/123/77 or CR35 at sensitizing for a secondary Tc cell response when challenged with A/Shearwater/72, but if larger doses were given either intranasally (10(6) 50% egg infective doses) or intravenously (10 to 10(3) hemagglutinin units), all viruses sensitized the mice equally well, despite the fact the A/Shearwater/72 gives a poor primary Tc cell response in mice. Thus, the viral glycoprotein antigens can be important in determining the immunogenicity of the virus and, particularly, the class I antigen-restricted Tc cell response of the host.
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PMID:Sensitization of mice with wild-type and cold-adapted influenza virus variants: immune response to two H1N1 and H3N2 viruses. 387 84

A relatively simple, specific and sensitive radioimmunoassay system has been developed for the detection of heterophile Hanganutziu-Deicher (H-D) antigen(s) and antibodies. The 125I-labeled H-D antigen-active molecule used for the assay is a bovine erythrocyte major glycoprotein previously found to have a strong H-D antigen potency. The antigen-antibody complex was precipitated with normal human serum as the carrier protein, followed by the addition of rabbit anti-human IgG F(ab')2 serum. With this method, different H-D antigen-active molecules were compared for heterophile H-D antigen potency with reasonable sensitivity detecting about 0.3 ng of cold glycoprotein. 8 different lung cancer tissues were assayed for H-D antigen. The sera from the 8 lung cancer patients were also screened by ELISA and RIA in an attempt to correlate expression of H-D antigen on tissues with elevation of H-D antibodies. The results showed that all patients' tissues expressed the antigen(s) but only 3 of them had abnormal levels of H-D antibodies. This could have been due to excess antigens in circulation or immune complexes.
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PMID:A potential radioimmunoassay system for detection of Hanganutziu-Deicher type heterophile antigen(s) and antibodies in tissues and fluids. 387 40

Laminin, a major structural glycoprotein of basement membranes, has been found to self-associate in vitro into large polymers. The formation of these complexes can be followed by the development of turbidity upon incubation in neutral phosphate buffer at 21-35 degrees C and is seen to be time-, concentration-, and temperature-dependent. The process is thermally reversible at 4 degrees C and the protein can be cycled between a dispersed and an aggregated state by alternating between 4 and 35 degrees C. Following incubation at 35 degrees C much of the monomeric laminin, which sediments at 11.4 S, is now seen to sediment at greater than 25 S. Both by turbidometric and sedimentation analysis, an apparent critical concentration for assembly of about 0.1 mg/ml (10(-7) M) is observed and is interpreted as evidence for a nucleation-propagation polymerization mechanism. The relative paucity of intermediates seen in a size-distribution analysis lends further support for this model. On platinum replicas obtained by rotary shadowing analysis, mostly free monomers are seen in the cold while after incubation at 35 degrees C, large multimeric aggregates with smaller amounts of oligomers are observed. The interaction between individual molecules appears to be specific because the dimers, trimers, and smaller oligomers are only associated at the terminal globular domains of the laminin molecules. In addition, removal of the globular domains of laminin with pepsin, which yields fragment P1, abolishes self-association. A divalent cation dependency for polymerization can be demonstrated and incubation in the presence of EDTA stops the polymerization at an oligomeric intermediate step. Hence overall laminin self-assembly can be divided into at least two steps: an initial temperature-dependent, divalent cation independent step followed by a divalent cation-dependent step.
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PMID:Laminin polymerization in vitro. Evidence for a two-step assembly with domain specificity. 399 91

A method is described for the rapid purification of serologically active high titer anti-I and anti-i cold antibodies from the sera of patients with chronic cold agglutinin disease (CCAD). The purification procedure is based on thermal affinity chromatography, using desialated orosomucoid (alpha 1-acid glycoprotein)-Sepharose 4B conjugated beads. The nature of the interaction between the cold agglutinins (CA) and the desialated orosomucoid is unknown. Inhibition studies, however, revealed that the cold hemagglutinating activities of all the anti-i sera were inhibited by desialated orosomucoid while only 1 out of 4 of the anti-I sera was similarly affected. Anti-I or anti-i antibodies were separated from whole sera in 7 out of 7 samples with a recovery in most cases of 100% of the cold hemagglutinating activity. The resultant products were purified monoclonal IgM fractions which could react with anti-kappa and anti-mu but not with anti-lambda sera. The homogeneity, purity and specificity of all preparations were confirmed by immunodiffusion analysis against purified I and i blood group antigens isolated from human erythrocyte membranes, zonal and right-angle electrophoresis and hemagglutination or hemagglutination inhibition studies.
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PMID:Rapid purification of anti-I and anti-i cold antibodies by affinity chromatography. 401 43


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