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)

By use of the indirect peroxidase-antiperoxidase immunohistochemical technique, nerve terminals exhibiting vasoactive intestinal polypeptide (VIP)-like-immunoreactivity were demonstrated in the pineal gland of the Mongolian gerbil (Meriones unguiculatus). Incubation of the superficial pineal gland of the gerbil with 60 pM of 125I-VIP showed that the gland exhibited saturation kinetics, and about 80% of the bound 125I-VIP could be displaced by adding a surplus of cold VIP. Incubation of unfixed, 0.1% and 4% paraformaldehyde-fixed cryostat sections of the gerbil forebrain with 125I-VIP also exhibited saturation kinetics, and displacement was possible by adding a surplus of the cold tracer. Receptor autoradiography on cryostat sections that had been incubated for 60 min with 125I-VIP showed a large number of grains over cortical areas, especially over the pyramidal layer of the hippocampus and the granular layer of the dentate gyrus. A prominent labelling of the pineal gland was also observed. The presence of VIP-like-immunoreactive nerve terminals and receptors for this molecule in the pineal gland of the Mongolian gerbil supports the biochemical studies demonstrating a stimulatory function of this molecule in the synthesis of melatonin.
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PMID:The presence of vasoactive intestinal polypeptide (VIP)-like-immunoreactive nerve fibres and VIP-receptors in the pineal gland of the Mongolian gerbil (Meriones unguiculatus). An immunohistochemical and receptor-autoradiographic study. 299 94

An 8.2 kb fragment of E. coli chromosomal DNA, when cloned in increased copy number, suppresses the dnaA46 mutation, and an abundant protein of about 68 kd (60 kd when measured by us), encoded by the fragment, is essential for the suppression (Takeda and Hirota 1982). Mapping experiments show that the fragment originates from the 94 min region of the chromosome. It encodes several proteins but only one abundant polypeptide of the correct size, the product of the groEL gene. Suppression by the fragment is allele specific; those mutations which map to the centre of the gene are suppressed. Other initiation mutants including dnaA203, dnaA204, dnaA508, dnaAam, dnaC, dnaP and dnaB252 are not suppressed. Most suppressed strains are cold-sensitive suggesting an interaction between the mutant proteins (or their genes) and the suppressing protein or proteins.
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PMID:A DNA fragment containing the groE genes can suppress mutations in the Escherichia coli dnaA gene. 301 70

Acetate kinase from Salmonella typhimurium and Escherichia coli was purified to electrophoretic homogeneity. The amino acid compositions of both proteins were similar, and the apparent molecular weights were the same, about 40,000 for the putative monomers. The native proteins gave higher molecular weights, suggesting that the enzymes may be oligomers, perhaps with two polypeptide subunits. Steady-state kinetic studies were performed with the enzymes isolated from both organisms and the kinetic constants were determined. The Km values were 0.07 and 7 mM for ATP and acetate, respectively. In contrast to earlier studies using less pure preparations, the homogeneous enzymes from both strains were active only with acetate but not with propionate or butyrate. The enzyme activity was cold-labile, and the length of reactivation time in the presence of Mg X ATP and acetate was dependent on protein concentration, suggesting that the monomer may not be catalytically active. The enzyme was phosphorylated with [gamma-32P]ATP and the phosphoprotein was isolated. Phosphoacetate kinase was capable of transferring the phosphate group to either ADP or acetate. The accompanying paper (Fox, D. K., Meadow, N. D., and Roseman, S. (1986) J. Biol. Chem. 261, 13498-13503) shows that the phosphoryl group of phosphoacetate kinase can also be reversibly transferred to Enzyme I of the phosphoenolpyruvate:glycose phosphotransferase system.
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PMID:Isolation and characterization of homogeneous acetate kinase from Salmonella typhimurium and Escherichia coli. 302 34

At 76 min on the E. coli genetic map there is a cluster of genes affecting essential cellular functions, including the heat shock response and cell division. A combination of in-vivo and in-vitro genetic analysis of cell division mutants suggests that the cell division gene fts E is the second gene in a 3 gene operon. A cold-sensitive mutant, defective in the third gene, is also unable to divide at the restrictive temperature, and we designate this new cell division gene fts X. Another cell division gene, fts S, is very close to, but distinct from, the 3 genes of the operon. The fts E product is a 24.5 Kd polypeptide which shows strong homology with a small group of proteins involved in transport. Both the fts E product and the protein coded by the first gene (fts Y) in the operon have a sequence motif found in a wide range of heterogeneous proteins, including the Ras proteins of yeast. This common domain is indicative of a nucleotide-binding site.
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PMID:A new cell division operon in Escherichia coli. 302 56

Regardless of the A, B, H, Le(a), Le(b), I and i activity, purified water-soluble blood group glycoproteins from human ovarian cyst fluid have a similar overall structure. They are polydisperse macromolecules (Mr 2.0 x 10(5) to several million) of similar composition (75 to 85% carbohydrate, 15 to 20% protein) and consist of multiple heterosaccharide side chains attached by an O-glycosidic linkage at their internal reducing ends to serine or threonine of the polypeptide backbone. About 90% of these carbohydrate side chains range in size from one to less than twenty-four sugar residues (twelve sugars in the internal structure and twelve key sugars specific as blood group determinants). Three-fourths of these side chains contain fewer than twelve sugars. A generalized blood group active carbohydrate chain is shown above. Three disaccharide units-Type I chain (Gal beta 1----3GlcNAc beta 1----3), Type II chain (Gal beta 1----4GlcNAc beta 1----6) and T determinant [Gal beta 1----3GalNAc alpha 1----Ser(Thr)]-are used to elucidate the internal structure of the carbohydrate chains. The complete internal structure is considered to have a core structure with four branches, to which the blood group key sugars are attached at the appropriate locations. The core structure is a tetrasaccharide, composed of one unit of Type I chain at the nonreducing end and the T determinant at the other end, linked to Ser or Thr of the protein moiety. Branch I is Type I chain and Branch II is Type II chain. They are linked to Gal at the nonreducing end of the core structure. Branch III is usually a Type II chain, but may sometimes be a Type I chain, linked to the GalNAc of the reducing end. The length of Branch III can be increased by adding one or more monosaccharides of Type I chain sequence such as Gal beta 1----3GlcNAc beta 1----3Gal beta 1----4GlcNAc beta 1----6GalNAc alpha 1----Ser(Thr), a combination of Type I and Type II chains. A new Branch IV is made up of Type II chain, which in turn is linked to the Gal end of the T determinant. The Type II chains react with the antibody to the type XIV pneumococcal capsular polysaccharide and with the anti-I(Ma) cold agglutinin.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Structural concepts of the human blood group A, B, H, Le(a), Le(b), I and i active glycoproteins purified from human ovarian cyst fluid. 305 18

L1, a major granulocyte protein, was purified and analysed by use of two-dimensional polyacrylamide gel electrophoresis (2D-PAGE). Three subunits were visualized, and they were found to have molecular weights of 12.5 kDa, 13.3 kDa and 8.3 kDa. They were extracted from 2D-gels, and different combinations of subunits and two L1 antisera were analysed by immunodiffusion in agarose gel. The 8.3 kDa polypeptide in combination with one or both of the other polypeptides, gave immunoprecipitation with one of the L1 antisera, while no precipitation occurred when the three polypeptides were tested separately. Neither was there any precipitation when the two heavier polypeptides were tested in combination. By use of another L1 antiserum, all the L1 polypeptides were found to be antigenic and give immunoprecipitations. The L1 protein has a great affinity for calcium, and calcium was necessary for immunoprecipitation with the L1 subunits to occur. Autoradiographs of 2D-PAGE gels with labelled leucocytes visualized the L1 subunits in the same position as the subunits from purified, cold L1, indicating no significant alteration of the L1 protein during the purification procedure.
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PMID:L1, a major granulocyte protein: antigenic properties of its subunits. 314 35

The ability of crude cerebrum supernatant to stabilize, at a low temperature, cold-labile microtubules purified from beef brain was studied during development in the rat. The cold-stabilizing activity of the supernatant was low during the first postnatal week, rose significantly during the second postnatal week, and thereafter continued to increase to the adult level. The partial purification of stable-tubule-only polypeptide (STOP) from the supernatant showed that high amounts of this protein exist at all ages, especially in young animals. The age-related increase in the microtubule cold-stabilizing activity of the cerebrum supernatant resulted from a developmental decrease in factors inhibiting STOP activity. The present study shows that (1) a close temporal correlation exists between the in vitro and in situ acquisition of cold-stable microtubules during brain development, (2) STOP activity may account for this acquisition, and (3) STOP activity is controlled by inhibiting factors that decrease with age, in turn allowing increased stability of the microtubular apparatus, a necessary condition for the development of neuronal processes.
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PMID:Developmental study of factors controlling microtubule in vitro cold-stability in rat cerebrum. 321 80

The innervation of blood vessels in the brood patch (thoracic skin) of the domestic fowl was studied by use of the catecholamine fluorescence technique, acetylcholinesterase staining, and the immunoperoxidase technique for demonstration of vasoactive intestinal polypeptide (VIP). Large arteries and veins were sparsely innervated, whereas arteriovenous anastomoses (AVAs) were densely innervated by adrenergic, acetylcholinesterase-positive, and VIP-immunoreactive nerve fibres. The rich supply of different vasomotor nerves to AVAs emphasizes the importance of these vascular shunts in regulating blood flow and, in turn, the transport of heat to the brood patch. Furthermore, the presence of VIP-immunoreactive nerve fibres in the vasculature of the brood patch suggests that VIP might be the mediator of the previously reported cold-induced vasodilatation.
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PMID:Innervation of arteriovenous anastomoses in the brood patch of the domestic fowl. 328 49

A proteinase isolated from the respiratory pathogen, Coccidioides immitis, was shown to have collagenolytic and elastinolytic activity, as well as the ability to cleave human serum immunoglobulin G and secretory immunoglobulin A. Proteolytic activity was demonstrated with a bovine casein digestion assay in conidial culture exudates, mycelial and spherule culture filtrates, conidial and spherule wall material, and Sephacryl S-300 fractions of the isolated soluble conidial wall material described previously. One of the latter fractions (fraction 2) demonstrated high proteolytic activity. The proteinase was purified from this chromatographic fraction by cold acetone extraction followed by Sephadex G-50 gel filtration and was identified as a polypeptide band of 36,000 Mr by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. By means of tandem two-dimensional immunoelectrophoresis, the proteinase was identified as antigen 11 on the basis of its reaction in the coccidioidin/anticoccidioidin reference system. The proteinase is characterized by a broad substrate specificity, optimal activity at 35 to 40 degrees C (pH 8.0) in the presence of human collagen, elastin, or hemoglobin, an isoelectric point of pH 4.5, and inhibition by organofluorides, N-tosyl-L-phenylalanine chloromethyl ketone, chymostatin, and alpha-1-antitrypsin. These features of the enzyme are comparable to those of chymotrypsinlike serine proteinases. Demonstration that the proteinase can cleave human immunoglobulins and digest ubiquitous tissue structural proteins (e.g., collagen and elastin) suggests that it may play a role in the virulence of the fungal pathogen.
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PMID:Isolation and characterization of an extracellular proteinase of Coccidioides immitis. 330 58

alpha- and beta-Tubulin are encoded in vertebrate genomes by a family of approximately 6-7 functional genes whose polypeptide products differ in amino acid sequence. In the chicken, one beta-tubulin isotype (c beta 6) has previously been found to be expressed only in thrombocytes and erythroid cells, where it is assembled into a circumferential ring of marginal band microtubules. In light of its unique in vivo utilization and its divergent assembly properties in vitro, we used DNA transfection to test whether this isotype could be assembled in vivo into microtubules of divergent functions. Using an antibody specific to c beta 6, we have found that upon transfection this polypeptide is freely coassembled into an extensive array of interphase cytoplasmic microtubules and into astral and pole-to-chromosome or pole-to-pole microtubules during mitosis. Further, examination of developing chicken erythrocytes reveals that both beta-tubulins that are expressed in these cells (c beta 6 and c beta 3) are found as co-polymers of the two isoforms. These results, in conjunction with efforts that have localized various other beta-tubulin isotypes, demonstrate that to the resolution limit afforded by light microscopy in vivo microtubules in vertebrates are random copolymers of available isotypes. Although these findings are consistent with functional interchangeability of beta-tubulin isotypes, we have also found that in vivo microtubules enriched in c beta 3 polypeptides are more sensitive to cold depolymerization than those enriched in c beta 6. This differential quantitative utilization of the two endogenous isotypes documents that some in vivo functional differences between isotypes do exist.
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PMID:In vivo coassembly of a divergent beta-tubulin subunit (c beta 6) into microtubules of different function. 331 49


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