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:2.7.10.1 (ERK)
95,504 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Neuraminidase-1 (NEU-1) is one of two neuraminidase isozymes which can be detected electrophoretically in mouse liver extracts. The inheritance of variation in NEU-1 and the linkage relationships of the gene controlling this variation were studied through a backcross analysis involving the SM/J and MA/MyJ inbred strains, and by examination of NEU-1 phenotypes in three congenic strains: B10.SM, B10.SM(22R) and B10.RVB. The data indicate that NEU-1 is controlled by Neu-1, a gene previously identified by its effect on total liver neuraminidase activity in whole tissue homogenates. Analysis of the congenic strains revealed identical low activity (SM/J-type: Neu-1a/Neu-1a) NEU-1 phenotypes in all three strains. This indicates that Neu-1 lies in the segment of the SM/J-derived H-2 region that is common to all three strains: H-2E alpha to H-2D. In addition, we examined the relationship between NEU-1 and phenotypic variation in liver acid phosphatase (AP; for which a new typing method is described) and linkage order among several other enzyme-coding genes linked to H-2. In all animals that could be scored confidently for AP, the NEU-1 and AP phenotypes were concordant, adding support to the hypothesis that both phenotypes are controlled by Neu-1. Recombination rates among six H-2-linked marker loci were unexpectedly low, but were sufficient to verify the position of Upg-1 as the telomeric flanking marker relative to Glo-1, H-2 (C4), Neu-1 (Apl), Ce-2 and Pgk-2.
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PMID:Electrophoretic analysis of liver neuraminidase-1 variation in mice and additional evidence concerning the location of NEU-1. 374 25

Two recently identified isozymes of neuraminidase in rat liver were examined for transmission patterns and linkage relationships, and for variation among inbred strains. The isozymes, designated neuraminidase-1 (NEU-1) and neuraminidase-2 (NEU-2), exhibited no electrophoretic mobility variants among the 22 inbred strains examined, but did possess striking interstrain variation in activity phenotypes on electrophoretic gels. The results of a backcross analysis involving the KGH and ACP strains revealed that NEU-1 and NEU-2 phenotypes are independently controlled, each by a single autosomal locus with additively acting alleles. The two loci are unlinked to one another, but the gene controlling NEU-1 is tightly linked to RT1, the rat major histocompatibility complex. This gene is almost certainly identical to Neu-1, a gene identified previously through its effect on "total" activity levels of liver neuraminidase as determined by fluorometric assay of tissue homogenates. NEU-2 and the gene controlling its phenotype were not detected by the fluorometric technique. We designate the genes controlling the NEU-1 and NEU-2 phenotypes as Neu-1 and Neu-2, respectively. Data from this and other studies place Neu-1 between Glo-1 and dw-3. The location of Neu-2 is unknown.
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PMID:Genetic analysis of liver neuraminidase isozymes in Rattus norvegicus: independent control of NEU-1 and NEU-2 phenotypes. 377 Apr 67

The endogenous neuraminidase activity of various mouse lymphoid subpopulations and tissue compartments was examined by a sensitive fluorometric assay. These analyses indicated that activated T lymphocytes possessed a significantly higher level of intracellular neuraminidase than activated B or resting T or B lymphocytes. Examination of the level of neuraminidase in bone marrow, thymus, lymph node, and unfractionated spleen indicated that these lymphoid tissues contained significantly less neuraminidase than was detected in stimulated T cells. Kinetic studies revealed that the majority of the increase in neuraminidase activity occurred between 24 and 48 h following stimulation. Analysis of activated T lymphocytes prepared from a panel of inbred mouse strains indicated that cells from mice of the H-2v haplotype, which possess the Neu-1a allele and are deficient in liver neuraminidase, exhibited a level of activity which was significantly lower than that detected in stimulated T cells from other mouse strains. These results indicate that the endogenous neuraminidase activity of T lymphocytes increases upon stimulation, and that the level of this enzyme activity in lymphoid cells is also controlled by the Neu-1 locus, which is located in the H-2 region of the major histocompatibility complex.
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PMID:Activation of T lymphocytes results in an increase in H-2-encoded neuraminidase. 387 51

Much of the total genomic variation in eukaryotic organisms may be due to genes other than those coding the primary translation product. Allelic variation, especially as detectable by electrophoresis, in the post-translational processing of enzymes has been briefly reviewed with considerable attention given to a mouse gene (Neu-1) and its pleiotropic effects on several lysosomal hydrolases. Liver acid phosphatase, alpha-mannosidase, arylsulfatase B, and alpha-glucosidase are differentially sialylated as the result of allelic variation for a gene controlling liver neuraminidase activity. Strain SM/J has only 15-20% of the total neuraminidase activity of control strains and is almost totally deficient in the more heat labile of two components of liver activity. The locus controlling this variation (Neu-1) maps very near the D end of H-2 on chromosome 17, apparently within the S region of H-2. A homologous gene has been mapped near the MHC of the rat. The exact nature of the mouse mutant and its relationship to several human diseases characterized by neuraminidase deficiency has not been determined.
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PMID:Post-translational modification of enzymes: processing genes. 635 Feb 18

Supernatants from 24 hr cultures of PHA-pulsed human T lymphocytes inhibit the migration of human peripheral blood T lymphocytes and guinea pig macrophages in vitro. The factor responsible for the inhibition of T lymphocytes provisionally called TIF (T cell migration inhibitory factor) was separated from MIF by preparative PAGE, had apparent molecular weight (m.w.) of 1,000-10,000 daltons and isoelectric point of 3.1. TIF activity was resistant to treatment with trypsin, chymotrypsin and neuraminidase but sensitive to PMSF (phenyl-methyl-sulfonyl-fluoride). This suggests that TIF is presumably different from human MIF and may represent a novel lymphokine which preferentially affects T cell migration in vitro.
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PMID:Partial purification and physicochemical properties of human T cell migration inhibitory factor (TIF). 639 62

Our chemoimmunotherapy study shows significantly longer remission and survival in acute myelocytic leukemia (AML) patients who have been immunized with neuraminidase-treated allogeneic myeloblasts as compared to patients who received chemotherapy alone or neuraminidase-treated myeloblasts plus MER. MER impairs the immunotherapeutic effectiveness of neuraminidase-treated allogeneic myeloblasts in AML patients. The in vivo and in vitro immunologic status in each arm of the protocol correlate well with the duration of remission and survival of the patient.
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PMID:Therapeutic effectiveness of neuraminidase-treated allogeneic myeloblasts as immunogen in acute myelocytic leukemia. 680

Congenic lines B10.KPA42, B10.KPA132, B10.SNA57, B10.DRB62, and B10.WOA105 carry H-2 haplotypes of wild mice on the genetic background of the strain C57BL/10Sn. Two of the lines (B10.DRB62 and B10.WOA105) have H-2 haplotypes indistinguishable from H-2v of B10.SM. The H-2 haplotype of one line (B10.SNA57) seems to have arisen from H-2v by recombination between the D and Qa-2 loci. The H-2 haplotypes of the remaining two lines probably arose from H-2v by recombination between the C4 and D loci. Since all six and no other lines carry the rare Neu-1a allele, the neuraminidase-1 locus is probably located proximal to the H-2D locus. Typing of H-2s recombinants for the enzyme acid phosphatase liver, the processing of which is controlled by the Neu-1 locus, suggests that the locus resides between the E alpha and D loci, that is in the S region.
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PMID:Evidence for placing the Neu-1 locus within the mouse H-2 complex. 711 40

The low activity of liver neuraminidase that is characteristic of mouse strain SM/J is inherited as a single gene on chromosome 17, near the major histocompatibility complex. This gene, neuraminidase-1 (Neu-1), is represented by the low activity allele Neu-1s in SM/J and the high activity allele Neu-1b in C57BL/6J and most other strains. Previously described variations in the posttranslational processing of acid phosphatase, alpha-mannosidase, arylsulfatase-B, and alpha-glucosidase are attributed to pleiotropic effects of this gene.
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PMID:Gene for neuraminidase activity on mouse chromosome 17 near h-2: pleiotropic effects on multiple hydrolases. 720 20

An enzyme which catalyzes the transfer of N-acetylneuraminic acid (NeuNAc) to a tetrahexosylceramide (asialo-GM1) in young rat brain is described. The enzymic product is a new monosialoganglioside containing a neuraminidase-labile neuraminic acid, GM1b. The activity of this sialyltransferase is higher in fetal and young rat brains. The enzyme exhibits a pH optimum of 6.5 in cacodylate buffer. The incorporation of radioactivity into GM1b is stimulated in the presence of asialo-GM1 and CMP-NeuNAc and is dependent on the quantity added. The detergent mixture, Tween 80 and CF54, is required for optimal activity. Recent demonstration of the natural occurrence of GM1b in the free cell types of rat ascites hepatopa cells suggests a functional importance of this CMP-Neu-NAc:asialo-GM1 sialyltransferase in the in vivo formation of this novel monosialoganglioside.
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PMID:The enzymic synthesis of GM1b: rat-brain CMP-N-acetylneuraminic acid: asialo-GM1 sialyltransferase. 721 83

The cell-surface expression of sialic acids in wild-type Crithidia fasciculata and three drug-resistant mutants (FU(R)11, TR3, and TFRR1) was analyzed using fluorescein-labeled Limulus polyphemus agglutinin (LPA) binding, glycosidase of known sugar specificity, and thin-layer chromatography (TLC). Gas-liquid chromatography-mass spectrometry (GC-MS) analysis using both electron-impact (EI-MS) and chemical ionization (CI-MS) by isobutane with selected ion monitoring (SIM) was also used. The surface location of sialic acid was inferred from LPA binding to whole cells abrogated by previous treatment with neuraminidase. An exception occurred with the TFRR1 strain, which after incubation with neuraminidase showed increased reactivity with the fluorescent lectin. Both N-acetyl- and N-O-diacetyl-neuraminic acids were identified in the flagellates by TLC, with a clear predominance being noted for the former derivative. However, the content of N-O-diacetyl-neuraminic acid was preferentially found in the TFRR1 strain. The GC-MS analysis of the acidic component of the TFRR1 mutant strain confirmed the occurrence of N-acetyl-neuraminic acid (Neu5Ac) by the presence of the diagnostic ions (m/z values: 684 and 594 for CI-MS and 478, 298, and 317 for EI-MS) and also by comparison with the standard Neu5Ac retention time. GC-MS analysis also showed fragments (m/z values: 654 and 564 for CI-MS and 594, 478, 298, and 317 for EI-MS) expected for the 7-O- and 9-O-acetyl-N-acetyl-neuraminic acids (Neu5,7Ac2 and Neu 5,9Ac2, respectively).
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PMID:Occurrence of N-acetyl- and N-O-diacetyl-neuraminic acid derivatives in wild and mutant Crithidia fasciculata. 750 43


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