Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:O76050 (neu)
 3,969 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The antigen MUSE11 detected by a monoclonal antibody (MAb) is an adenocarcinoma-associated antigen, while CA15-3 is a representative breast cancer-associated antigen detected by MAbs 115D8 and DF3. MAb MUSE11 showed higher binding activity to a synthetic peptide corresponding to the tandem repeat motif of the mucin core protein than that of MAb DF3, although MAb DF3 also had a significant binding activity indicating that MAbs MUSE11 and DF3 could recognize an identical polypeptide core. The reactivity of MAb DF3 to a breast cancer cell line MRK-neu-1 was completely abolished by neuraminidase treatment whereas that of MAb MUSE11 was partly conserved. The simultaneous measurement of the antigens MUSE11 and CA15-3 in sera from 35 cancer patients demonstrated that the incidence of abnormal serum level of CA15-3 was lower than that of antigen MUSE11. These data suggest that at least a part of the structural basis for the difference between the serum levels of antigen MUSE11 and CA15-3 could be carbohydrate side chains including sialic acids.
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PMID:Circulating tumor-associated antigens detected by monoclonal antibodies against the polypeptide core of mucin--comparison of antigen MUSE11 with CA15-3. 137 32

Authors describe the clinico-pathological and immunohistochemical findings of two mediastinal (seminoma and yolk-sack) and a pineal mixed (seminoma and yolk-sack) tumours. In the mediastinal yolk-sack tumour the light microscopic picture of cellular components, alpha-fetoprotein (AFP), haemoglobin F (Hgb F), blood group antigen, carcinoembryonal antigen (CEA), post-digestion (neuraminidase) peanut antigen (neu-PNA) positivities suggest hepatic and intestinal differentiation. In some cells of mediastinal seminoma the glucose- and mannose-binding concanavalin-A (Con A) showed reaction. In the mixed tumour of the pineal region in addition to AFP positive cell cords some cell groups reacted with Leu-M1 (CD15) monoclonal antibodies raised against stage specific embryonic antigen 1 (SSEA1).
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PMID:[Extra-gonadal germ-cell tumors]. 267 89

Mortality from D-galactosamine hydrochloride (D-GalN)-induced acute liver failure (ALF) in rats can be reduced by (1) transplanting intact hepatocytes; (2) injecting cytosol from fractionated hepatocytes dispersed from a liver subjected to 70% hepatectomy 24 hr earlier (CYT-H); (3) injecting a cell-free supernate derived from cultured hepatocytes (SUP); or (4) injecting neuraminidase-treated plasma where the plasma is drawn 24 hr after donor rats are subjected to 70% hepatectomy (PHP-neu). These treatments are effective when administered 20-24 hr after D-GalN poisoning, but experiments to determine the alterations in mortality rates as a function of time of treatment in relation to poisoning have not been performed. Two experiments are reported here. In the first the survival of lethally poisoned rats was compared after intravenously injecting either SUP prepared from cultured hepatocytes of syngeneic adult or fetal rat sources, or CYT-H from syngeneic adult rats 20 hr after poisoning. Untreated rats, rats treated with culture media alone, or rats treated with CYT from a nonregenerating source had an 88-100% mortality, with all deaths occurring within 72 hr following poisoning. Improved survival followed all other treatments: 55% of the rats receiving adult SUP, 70% of the rats receiving fetal SUP, and 80% of the rats receiving CYT-H survived. In the second experiment the survival of poisoned rats was compared after injecting them with PHP-neu, PHP not treated with neuraminidase (PHP without neu), and neuraminidase-treated plasma from sham-operated rats (SP-neu) or normal, nonoperated rats (NP-neu) 20 hr after poisoning.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Factors effective in reducing rat mortality due to acute liver failure as induced by D-galactosamine poisoning. 670 1

Glycosphingolipids are assumed to play a crucial role in cell-cell and cell-substrate interactions, including cell adhesion, proliferation, differentiation and apoptosis. Furthermore, cell surface glycolipid profile changes in the so called "social disorders", such as malignant transformation. To better investigate these modifications, the ganglioside composition in different solid tumours and in two transformed cell lines was analyzed. In some of these models we also tried to correlate the pattern of gangliosides to the key enzymes involved in their metabolism. The results we obtained can be summarized as follows:(1), meningiomas with or without chromosome 22 deletion: predominance of ganglioside GD3 in the former and of ganglioside GM3 in the latter. Correlation between GM3/GD3 ratio and SAT-2 activity; (2), mammary carcinomas developed in MMTV/c-neu transgenic mice: accumulation of GM3-derived species. The different ganglioside distribution seems to correlate with the tumour size; (3), Sarcoma Galliera-strain cells SGS/3A and normal syngenic murine fibroblasts FG: transformed cells exhibit a lower activity of sialyltransferases (SAT-1, SAT-2, SAT-4) compared to normal fibroblasts, suggesting a possible correlation with the ganglioside pattern. The neuraminidase activity seems to correlate to the glycoprotein sialic acid content; (4), 3T3 normal murine fibroblasts and SVT2 transformed cells: GM3 is absent in 3T3, while it accounts for the main ganglioside species in SVT2. On the contrary, GM2 present in a large amount in normal fibroblasts, is practically absent in transformed cells. No correlation has been observed between ganglioside profile and glycosyltransferase activities so far examined.
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PMID:Glycosphingolipid expression in solid tumours and transformed cell lines. 934 46

Lysosomal neuraminidase (sialidase) occurs in a high molecular weight complex with the glycosidase beta-galactosidase and the serine carboxypeptidase protective protein/cathepsin A (PPCA). Association of the enzyme with PPCA is crucial for its correct targeting and lysosomal activation. In man two genetically distinct storage disorders are associated with either a primary or a secondary deficiency of lysosomal neuraminidase: sialidosis and galactosialidosis. In the mouse the naturally occurring inbred strain SM/J presents with a number of phenotypic abnormalities that have been attributed to reduced neuraminidase activity. SM/J mice were originally characterized by their altered sialylation of several lysosomal glycoproteins. This defect was linked to a single gene, neu-1 , on chromosome 17, which was mapped by linkage analysis to the H-2 locus. In addition, these mice have an altered immune response that has also been coupled to a deficiency of the Neu-1 neuraminidase. Here we report the identification in SM/J mice of a single amino acid substitution (L209I) in the Neu-1 protein which is responsible for the partial deficiency of lysosomal neuraminidase. We propose that the reduced activity is caused by the enzyme's altered affinity for its substrate, rather than a change in substrate specificity or turnover rate. The mutant enzyme is correctly compartmentalized in lysosomes and maintains the ability to associate with its activating protein, PPCA. We propose that it is this mutation that is responsible for the SM/J phenotype.
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PMID:A point mutation in the neu-1 locus causes the neuraminidase defect in the SM/J mouse. 942 40

Sialidase (neuraminidase), encoded by the neu-1 gene in the major histocompatibility complex locus catalyzes the intralysosomal degradation of sialylated glycoconjugates. Inherited deficiency of sialidase results in sialidosis or galactosialidosis, both severe metabolic disorders associated with lysosomal storage of oligosaccharides and glycopeptides. Sialidase also plays an important role in cellular signaling and is specifically required for the production of cytokine interleukin-4 by activated T lymphocytes. In these cells, neu-1-encoded sialidase activity is increased on the cell surface, suggesting that a specific mechanism regulates sorting of this enzyme to the plasma membrane. We investigated that mechanism by first showing that sialidase contains the internalization signal found in lysosomal membrane proteins targeted to endosomes via clathrin-coated pits. The signal consists of a C-terminal tetrapeptide (412)YGTL(415), with Tyr(412) and Leu(415) essential for endocytosis of the enzyme. We further demonstrated that redistribution of sialidase from lysosomes to the cell surface of activated lymphocytes is accompanied by increased reactivity of the enzyme with anti-phosphotyrosine antibodies. We speculate that phosphorylation of Tyr(412) results in inhibition of sialidase internalization in activated lymphocytes.
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PMID:Intracellular distribution of lysosomal sialidase is controlled by the internalization signal in its cytoplasmic tail. 1157 Dec 82