Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Cellular morphology, macromolecular composition, (DNA, RNA and Protein content) marker enzyme activities for neurons [neuron specific enolase (NSE)] and astrocytes [glutamine synthetase (GS)] and plasma membrane protein profiles in the bulk isolated neurons and astrocytes from control and ethanol treated rats were studied. One month aged Wistar rats were given ethanol as sole drinking fluid for 10 weeks. Scanning electron microscopy revealed a characteristic cell surface smoothening in astrocytes due to ethanol treatment. DNA levels were unaltered, while RNA and Protein contents were decreased in astrocytes and neurons. Further, 3H-leucine incorporation into proteins was decreased in neurons and astrocytes derived from ethanol treated rats indicating reduced protein synthesis in neurons and astrocytes. GS activity was affected severely suggesting impairment in astrocytic functions. Plasma membrane protein composition was analyzed by 2-D electrophoresis. The analysis indicated several protein defects in the plasma membranes of neurons and astrocytes, which might be involved in 'membrane disorder' during ethanol challenge. 125I-Wheat Germ agglutinin binding studies showed three prominent proteins (160, 116 and 97 kDa) in astrocyte membrane fraction suggesting the possible involvement of N-terminal glycoproteins in altered astrocyte morphology during ethanol ingestion. Impairment in the astrocyte cell functions, protein changes in plasma membrane and cellular morphology studies suggest that astrocytes may be more vulnerable than neurons for ethanol effects.
Mol Cell Biochem 1994 Jan 12
PMID:Differential changes in cell morphology, macromolecular composition and membrane protein profiles of neurons and astrocytes in chronic ethanol treated rats. 751 15

Corticosteroids used orally and intravenously lead to lung diseases and vascular disorder. To investigate whether enolase levels are also changed by treatment with synthetic steroid dexamethasone (as alteration in the enolase levels have been correlated with lung cancer) we performed the following studies. A cDNA library was prepared from poly(A) mRNA extracted from human lung fibroblast cells. cDNA clone HLE1 containing 1.7 kb insert coding for enolase was isolated. Its identity was confirmed by (a) translation of the hybrid selected mRNA and (b) nucleotide sequence analysis of the insert and comparison with known enolase sequences from other species. The lung enolase is coded by a polypeptide of 458 amino acid residues (mr = 49.5 kD). Nucleotide sequencing and derived amino acid sequence data suggest that the cloned enolase is non-neuronal isoform of enolase (NNE). In lung fibroblast cells, dexamethasone caused remarkable increase in the abundance of the enolase mRNA, which was concentration and time dependent. The induction by dexamethasone required de novo RNA synthesis but not de novo protein synthesis.
Biochem Mol Biol Int 1993 Jun
PMID:Human lung enolase: cloning and sequencing of cDNA and its inducibility with dexamethasone. 768 84

The GCR1 gene product is required for maximal transcription of yeast glycolytic genes and for growth of yeast strains in media containing glucose as a carbon source. Dominant mutations in two genes, SGC1 and SGC2, as well as recessive mutations in the SGC5 gene were identified as suppressors of the growth and transcriptional defects caused by a gcr1 null mutation. The wild-type and mutant alleles of SGC1 were cloned and sequenced. The predicted amino acid sequence of the SGC1 gene product includes a region with substantial similarity to the basic-helix-loop-helix domain of the Myc family of DNA-binding proteins. The SGC1-1 dominant mutant allele contained a substitution of glutamine for a highly conserved glutamic acid residue within the putative basic DNA binding domain. A second dominant mutant, SGC1-2, contained a valine-for-isoleucine substitution within the putative loop region. The SGC1-1 dominant mutant suppressed the GCR1 requirement for enolase, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, phosphoglycerate mutase, and pyruvate kinase gene expression. Expression of the yeast enolase genes was reduced three- to fivefold in strains carrying an sgc1 null mutation, demonstrating that SGC1 is required for maximal enolase gene expression. Expression of the enolase genes in strains carrying gcr1 and sgc1 double null mutations was substantially less than observed for strains carrying either null mutation alone, suggesting that GCR1 and SGC1 function on parallel pathways to activate yeast glycolytic gene expression.
Mol Cell Biol 1995 May
PMID:The GCR1 requirement for yeast glycolytic gene expression is suppressed by dominant mutations in the SGC1 gene, which encodes a novel basic-helix-loop-helix protein. 773 44

The distribution of type I interleukin-1 receptor (IL-1R1) mRNA in the rat brain was examined by in situ hybridization technique. IL-1R1 mRNA was expressed in several brain regions including the anterior olfactory nucleus, medial thalamic nucleus, posterior thalamic nucleus, basolateral amygdaloid nucleus, ventromedial hypothalamic nucleus, arcuate nucleus, median eminence, mesencephalic trigeminal nucleus, motor trigeminal nucleus, facial nucleus and Purkinje cells of the cerebellum. Furthermore, we identified neuronal expression of IL-1R1 mRNA using simultaneous detection (double in situ hybridization) of IL-1R1 mRNA with neuron specific enolase mRNA. In addition to the expression in neuronal cells, IL-1R1 mRNA was also expressed on the vascular walls and the epithelial cells of the choroid plexus and the ventricles. These findings suggest the possibility that IL-1 produces its multiple effects on the central nervous system through the actions not only on neuronal cells but also on endothelial and epithelial cells.
Brain Res Mol Brain Res 1994 Nov
PMID:Localization of type I interleukin-1 receptor mRNA in the rat brain. 787 51

Neurochemical observations on cortical biopsies form 48 patients under surgical treatment for pharmacoresistant partial epilepsy showed a 70-80% increase in glutamate concentration when expressed in relation to neuron specific enolase. Intraperitoneal administration of one of its receptor agonists, kainic acid (KA), to the rat led to increased epileptogenic activity of the limbic type in a dose-dependent fashion. The KA injection also led to a neuronal cell death and a gliosis, closely correlated to the extent of seizure activity. In biopsies from human epileptogenic cortex, the concentration of neuron specific enolase correlated inversely to that of glial fibrillary acidic protein, a marker for astrocytic glial cells. Stimulation of the KA receptor decreased the extent of phosphorylation of the largest subunit of neurofilaments (NF-H) that have consequences for structural stability and axonal transport. Phosphorylated NF-H decreased also in human epileptic cortex, indicating either an overactivity of excitatory neurotransmitters or a loss of axonal compartments.
Mol Neurobiol
PMID:Excitotoxicity. Experimental correlates to human epilepsy. 788 4

The two moulds, Alternaria alternata and Cladosporium herbarum, are recognized as major causes of fungal allergies. Cloning, sequencing and heterologous expression of the allergens of the two moulds is a necessary step in understanding fungal allergy and in the development of new and improved methods of diagnosis and therapy. The seven new mould allergens presented here represent four new allergen proteins: aldehyde dehydrogenase (ALDH), enolase, YCP4 (previously found as a Saccharomyces cerevisiae protein of unknown function), and the acidic ribosomal protein, P2. Three of them (ALDH, YCP4 and P2) were found to be allergens in both fungi, Alternaria and Cladosporium. All allergens found so far are cytoplasmic proteins and are rather well conserved in evolution even when comparing distant species. Most of the allergens have "household" functions (ALDH, enolase). One allergen (P2) is a homolog of a very highly conserved human lupus erythematodes (LE) antigen. None of the fungal allergens is clearly related to other known non-fungal allergens.
Mol Immunol 1995 Feb
PMID:Molecular cloning of major and minor allergens of Alternaria alternata and Cladosporium herbarum. 789 96

A multiple alignment procedure for aligning the beta-sheet residues of the (beta/alpha)8-barrel structures is described. It uses a two-dimensional numbering scheme which is based on the covalent and hydrogen-bonding pattern of the beta-sheet. Two different scoring functions were used: one measured the sequence and topological similarity and the other the root-mean-square deviation of the coordinates of the matched residues. The procedure was applied to obtain multiple alignments of the beta-barrels of ten (beta/alpha)8-barrel proteins of known structure. Two kinds of alignments were derived: one in which the beta-strand numbering was preserved and another in which the beta-strands were allowed to be cyclically permuted. It is shown that-preservation of the beta-strand numbering corresponds to aligning only the layer structure of the beta-barrels. In order to obtain the optimal rotational alignment of the barrels as well, the beta-strands must be allowed to be renumbered. Although the 2-fold or 4-fold rotational symmetry of the beta-barrels makes it difficult to obtain unique rotational alignment of the barrels, the results of the alignment indicate that the beta-strands in the beta-barrel of enolase, xylose isomerase, taka-amylase, and possibly fructose biphosphate aldolase, must be cyclically permuted in order to be optimally aligned to those of the other proteins, which include triose phosphate isomerase, the alpha-subunit of tryptophan synthetase, flavocytochrome b2, ribulose-1, 5-biphosphate carboxylase/oxygenase, and glycolate oxidase.
J Mol Biol 1994 Nov 25
PMID:Alignment of beta-barrels in (beta/alpha)8 proteins using hydrogen-bonding pattern. 796 29

We previously reported the isolation from Entamoeba histolytica of a novel rac family protein kinase gene, termed Ehrac1, for "related to cAMP-dependent protein kinases and protein kinase Cs". To study the function and properties of this kinase gene further, we fused the full-length coding region and the truncated catalytic domain of the Ehrac1 gene in frame with the gene encoding glutathione S-transferase in the pGEX-KG vector and expressed the fusion in Escherichia coli. The thrombin-cleaved and uncleaved fusion proteins, GST-Ehrac1 and GST-Ehrac1-c (catalytic domain), were purified and found to exhibit similar protein kinase activities. The Ehrac1 fusion kinase was found to phosphorylate serine/threonine residues exclusively in vitro. The preferred substrate for the enzyme was histone H1 with a Km of approx. 14 microM. Histone H3 and kemptide were phosphorylated at about half the rate of histone H1. Protamine, enolase, bovine serum albumin, and poly (Glu:Tyr) were not substrates for the enzyme. The protein kinase activity was higher in the presence of Mn2+ than Mg2+. Neither cAMP, Ca2+, nor Ca2+/calmodulin stimulated enzyme activity. The pH optimum of the enzyme was 7.5. The Ehrac1 kinase can utilize GTP as well as ATP as a phosphate donor with an apparent Km of 80 microM. Enzyme activity was inhibited 30-40% by a crude cAMP-dependent protein kinase inhibitor from rabbit and by thiol reagents. The expression and purification of enzymatically active Ehrac1 protein kinase should allow further analysis of the regulation and signal transduction pathways of E. histolytica.
Mol Biochem Parasitol 1994 Jul
PMID:Expression and characterization of a rac family protein kinase of Entamoeba histolytica. 798 73

The structure of a new crystal form of enolase from bakers' yeast has been solved to 2.1-A resolution. Crystals were grown from poly(ethylene glycol) and KCl at pH 8.2 in the presence of Mg2+ and a reaction intermediate analog, phosphonoacetohydroxamate (PhAH). Crystals belong to space group C2; have unit cell dimensions a = 123.5 A, b = 73.9 A, and c = 94.8 A with beta = 93.3 degrees; and contain one dimer per asymmetric unit. The structure was solved by molecular replacement from the X-ray coordinates of apoenolase [Stec, B., & Lebioda, L. (1990) J. Mol. Biol. 211, 235-248]. Both essential divalent metal ions are observed to be complexed with the inhibitor. The two Mg2+ ions are 4.05 A apart and are bridged by a mu-oxyl ligand from the carbonyl moiety of PhAH. The "high-affinity" Mg2+ coordinates to the carboxylate side chains of Asp 246, Glu 295, and Asp 320, one water molecule, and the hydroxamate and carbonyl oxygens of PhAH. The second Mg2+ coordinates to a phosphonyl oxygen, two water molecules, and the mu-bridge carbonyl oxygen of PhAH. Coordination schemes with respect to PhAH and water ligands are fully consistent with those of the Mn2+ complexes determined spectroscopically [Poyner, R.R., & Reed, G. H. (1992) Biochemistry 31, 7166-7173]. Remaining ligands for the second Mg2+ are the carbonyl oxygen and gamma-oxygen of Ser 39. Chelation of this Ser residue to Mg2+ effectively "latches" a flexible loop extending from Gly 37 through His 43 and closes off the entrance to the active site. The position of the second Mg2+ in the active site provides new insight into the stereochemistry of substrate binding.
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PMID:Chelation of serine 39 to Mg2+ latches a gate at the active site of enolase: structure of the bis(Mg2+) complex of yeast enolase and the intermediate analog phosphonoacetohydroxamate at 2.1-A resolution. 804 35

The expression of cerebral type aldolase C was investigated immunohistochemically in six varieties of neuroendocrine (n = 57) and six types of non-endocrine tumor (n = 76) using the avidin-biotin complex method. Aldolase C expression in the neuroendocrine tumors was also compared with those of chromogranin and gamma enolase. Aldolase C was detected in all the islet cell (7/7) and carcinoid tumors (10/10), thyroid medullary carcinomas (7/7), and pheochromocytomas (10/10), as well as in the majority of neuronal tumors (8/10) and bronchial small cell carcinomas (10/13). Chromogranin immunoreactivity was restricted to the tumors with abundant neuroendocrine granules. Gamma enolase positivity was generally similar to that of aldolase C, but there were some differences. Amongst the bronchial small cell carcinomas, three tumors negative for gamma enolase were positive for aldolase C, while another three tumors were positive for gamma enolase only. However all the small cell carcinomas were positive for at least one of these two enzymes. Aldolase C was detected in 28 (37%) of the 76 non-endocrine tumors and tended to be expressed preferentially in the differentiated portions of these tumors. Although aldolase C was expressed in many bronchial squamous cell carcinomas, the immunoreactivity was localized mainly in keratinizing foci and the less differentiated parts of these tumors expressed the enzyme only occasionally. Thus aldolase C, in conjunction with other neuroendocrine-associated markers, may be of value in identifying tumors of neuroendocrine type.
Virchows Arch B Cell Pathol Incl Mol Pathol 1993
PMID:Aldolase C in neuroendocrine tumors: an immunohistochemical study. 828 26


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