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:3.4.25.1 (proteasome)
28,817 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Pen a 1, the major shrimp allergen from the brown shrimp Penaeus aztecus was purified by preparative SDS-PAGE. Peptides were generated from Pen a 1 by CNBr cleavage and endoproteinase (Lys-C, Glu-C, trypsin, alkaline protease, Arg-C, chymotrypsin) digestion. The molecular weights of the resulting CNBr cleavage and enzymatic digestion products, separated by peptide SDS-PAGE, ranged from 1.5 to 20 kD. Following SDS-PAGE and semidry blotting, the analysis of monoclonal antibody (mAb) and subjects' IgE reactivities demonstrated that with the exception of alkaline protease, all cleavage procedures yielded IgE-binding peptides. However, since not all peptides of every digest bind IgE, it appears that IgE-binding epitopes are restricted to certain parts of the Pen a 1 molecule. mAbs bound to CNBr, Lys-C, trypsin, Glu-C and Arg-C peptides. Since mAbs reacted to several peptides from the same digest, Pen a 1 may have several similar epitopes. The comparison of IgE and mAb reactivities demonstrated similar but not identical binding patterns.
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PMID:Antigenic analysis (IgE and monoclonal antibodies) of the major shrimp allergen Pen a 1 (Tropomyosin) from Penaeus aztecus. 754 76

The Yoshida sarcoma (YS) is characterized by growth as "free cells" in ascites. Long-survival Yoshida sarcoma (LY) variants, which develop after transplantation of YS into immunologically conditioned Donryu rats, in contrast, form "islands" in ascites. A representational difference analysis (RDA) approach was adopted to isolate genes differentially expressed between YS and LY variants to elucidate the molecular mechanism of their development. Fifteen clones presenting differences in expression were characterized. Nine genes (those encoding for the high-affinity IgE receptor gamma chain, pJG116 repetitive sequence, non neuronal enolase, proteasome subunit RC1, cytotoxic T lymphocyte-associated gene transcript CTLA-1, interleukin-2 receptor gamma chain, and three unknown sequences) expressed mRNA in YS, but showed lower or no expression of mRNA in LYs. The mRNAs of the other six genes (those encoding for cytokeratin 8, cytokeratin18 (Endo B), TIMP2 and three unknown sequences) were not found in YS, but were present in LYs. Interestingly, CTLA-1 is a non-epithelial (hematopoietic) cell-specific gene in terms of transcription, while cytokeratin 8 and cytokeratin 18 are both epithelium-specific genes. Immunohistochemically, YS expressed T-cell specific antigens CD2 and CD3, and T cell receptor beta and gamma chain genes were rearranged in YS, but not in LYs. Moreover, using restriction fragment length polymorphism probes, we found that LYs exhibited different cell lineage from YS. Thus, our present findings, unexpectedly, raise fundamental questions concerning the cellular origins of YS and LY variants rather than pointing to any specific mechanism to explain the LY phenomenon.
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PMID:Isolation of genes differentially expressed between the Yoshida sarcoma and long-survival Yoshida sarcoma variants: origin of Yoshida sarcoma revisited. 782 94

The Aspergillus cell wall contains most of the antigens secreted by the fungus during its active in vitro or in vivo growth. These antigens, which bind to the IgE and IgG of allergic and aspergilloma patients or are secreted in the biological fluids of patients with invasive aspergillosis, are of primary importance in the diagnosis of aspergillosis. Located at the interface between host and pathogen cells, the fungal cell wall plays a major role during fungal invasion. It contains several surface receptors involved in adhesion of the fungus to host proteins and cells. Some of the wall antigens are also directly involved in the colonization of the host tissues by the fungus. Very few of these putative virulence factors have been purified until now. A 33-kDa alkaline protease of the subtilisin family can hydrolyze several extracellular matrix proteins such as collagen, fibrinogen, elastin. However, gene disruption experiments have shown that protease-deficient mutants are still able to infect mice. An 18-kDa antigen, which has been detected in the urine of patients with invasive aspergillosis, is present in vivo in the lung of mice infected with A. fumigatus. It has a ribonuclease activity that cleaves a single phosphodiester bond in a highly conserved region of the ribosomal RNA. Its role in the virulence of A. fumigatus has not been demonstrated until now. Biochemical and molecular characterization of the wall antigenic aggressins should be pursued.
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PMID:Cell wall antigens in Aspergillus fumigatus. 829 77

Thirty-six employees who produced industrial enzymes from selected strains of bacteria and fungi were evaluated by epicutaneous threshold testing and enzyme-linked immunosorbent assays (ELISA) for specific IgE and IgG antibodies. The workers complained of 'asthma- and flu-like' symptoms, which generally lessened away from work. The enzymes evaluated were: alpha-amylase (1,4-alpha-d-glucan glucanohydrolase) from Bacillus licheniformis (alpha ABl), B. subtilis formation 1 (alpha A1Bs) and B. subtilis formation 2 (alpha A2Bs); purified alpha-amylase from B. licheniformis (C alpha ABl) and A. oryzae (C alpha AAo); alkaline protease from B. licheniformis (APBl) and purified alkaline protease (CAPBl); amyloglucosidase (1,4-alpha-d-glucan glucohydrolase) from A. niger (AGAn) and purified amyloglucosidase (CAGAn). Statistically significant increases (P > 0.05) in the proportion of workers having positive skin tests to CAPBl, AGAn and CAGAn were found. Significantly elevated (P > 0.05) mean specific IgE results were observed for C alpha AAo CAGAn and AGAn, and elevated (P > 0.05) mean specific IgGs were observed for C alpha AAo, CAGAn, AGAn, alpha A1Bs, alpha AB1 and alpha A2Bs. These results indicate that occupational exposure to some industrial enzymes can cause immediate-onset cutaneous hypersensitivity reactions, pulmonary function deficits and significantly elevated specific antibody levels. Our results are equivocal as to whether work-related respiratory and cutaneous hypersensitivity reactions are antibody mediated, as there was no statistically significant association between these reactions and specific IgE or IgG levels.
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PMID:Hypersensitivity reactions and specific antibodies in workers exposed to industrial enzymes at a biotechnology plant. 893 88

The present study unequivocally demonstrated the expression of CD28 on murine bone marrow-derived cultured mast cells and a mast cell line, MCP-5. Stimulation of surface CD28 molecules on mast cells with anti-CD28 mAbs induced tyrosine phosphorylation of cellular proteins, including several protein tyrosine kinases and their substrates, such as Itk/Emt (Emt), Btk, Syk, c-Cbl, Shc, and Vav. CD28-stimulated tyrosine phosphorylation was followed by a rebound hypophosphorylation. Interestingly, CD28 stimulation alone elicited a low level secretion of TNF-alpha. On the other hand, cross-linking of the high affinity IgE receptor (Fc epsilon RI) on mast cells induces a set of activation events, i.e., degranulation, secretion of eicosanoids, secretion of cytokines, and DNA synthesis. Concurrent stimulation of mast cells through CD28 enhanced Fc epsilon RI-induced TNF-alpha secretion in a dose-dependent manner. Together, the present data suggest a role for CD28-mediated costimulation of mast cells in the initiation and progression of allergic responses and other diseases.
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PMID:Increased secretion of TNF-alpha by costimulation of mast cells via CD28 and Fc epsilon RI. 903 88

The clinical studies show that heparin, well known as an anticoagulant, inhibits early asthmatic response (EAR) and bronchial hyperactivity after allergen challenge in allergic patients. We have previously shown that heparin attenuates also the late phase of allergic reaction (LAR) Recently it has been shown that heparin modulates mastocyte mediator release. This could explain the beneficial role of heparin in EAR. The goal of this study was to explore the protective mechanism of heparin on LAR. Basophils are important cells in the development of LAR. We studied the effect of heparin on histamine release from basophils induced by anti-IgE and monocyte chemotactic-activating factor/monocyte chemotactic protein (MCAF/MCP-I). MCAF belongs to the chemokine family and is the most potent histamine releasing factor. Basophils were isolated from peripheral blood of 12 asthmatic patients. The cells were incubated with heparin in various concentrations: 10, 25, 50 and 100 U. Histamine was measured by spectrophotofluorometric method. We observed that incubation of basophils with heparin inhibits histamine release as shown in the table: [table: see text] Preincubation of anti-IgE or MCAF/MCP-I with heparin did not induce any changes in histamine release. The suggest that action of heparin depends on interaction with the cells but not with the agonists.
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PMID:[The effect of heparin on release of histamine from basophils under the influence of MCAF/MCP-I in patients with bronchial asthma]. 948 30

The proopiomelanocortin (POMC)-derived neuropeptide alpha-melanocyte stimulating hormone (alpha-MSH) is known to modulate some aspects of inflammation through direct effects on T cells, B cells, and monocytes. To determine whether alpha-MSH might similarly influence mast cell responsiveness, mast cells were examined to see if they expressed the receptor for alpha-MSH, melanocortin-1 (MC-1), and whether alpha-MSH altered mast cell function. We thus first identified MC-1 on bone marrow cultured murine mast cells (BMCMC) and a murine mast cell line (MCP-5) employing flow cytometry and through detection of specific binding. Subsequent treatment of mast cells with alpha-MSH increased the cAMP concentration in a characteristic biphasic pattern, demonstrating that alpha-MSH could affect intracellular processes. We next examined the effect of alpha-MSH on mediator release and cytokine expression. IgE/DNP-human serum albumin-stimulated histamine release from mast cells was inhibited by approximately 60% in the presence of alpha-MSH. Although activation of BMCMC induced the expression of mRNAs for the inflammatory cytokines IL-1beta, IL-4, IL-6, TNF-alpha, and the chemokine lymphotactin, mRNAs for IL-1beta, TNF-alpha, and lymphotactin were down-modulated in the presence of alpha-MSH. Finally, IL-3-dependent proliferative activity of BMCMC was slightly but significantly augmented by alpha-MSH. Taken together, these observations suggest that alpha-MSH may exert an inhibitory effect on the mast cell-dependent component of a specific inflammatory response.
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PMID:Receptor-mediated modulation of murine mast cell function by alpha-melanocyte stimulating hormone. 1047 6

The Aspergillus genus of fungi is known to be one of the most prevalent aeroallergens. On two-dimensional immunoblotting using patients' sera containing IgE specific for Asp f 13, an allergen with a molecular mass of 33 kDa and a pI of 6.2 was identified. This allergen was also present in A. fumigatus culture filtrates. Furthermore, the sequence of the Asp f 13 cDNA was identical to that for alkaline protease isolated from A. fumigatus and showed 42-49% identity of amino acids with two proteases from P. cyclopium and T. album and with the Pen c 1 allergen from P. citrinum. Asp f 13 coding sequences were expressed in Escherichia coli as a [His](6)-tagged fusion protein which was purified by Ni(2+)-chelate affinity chromatography. Recombinant Asp f 13 was recognized by rabbit polyclonal antibodies against Asp f 13 and by IgE antibodies from subject allergic to A. fumigatus. To identify and characterize the linear epitopes of this allergen, a combination of chemical and enzymatic cleavage and immunoblotting techniques, with subsequent N-terminal sequencing and mass spectrometry, were performed. At least 13 different linear epitopes reacting with the rabbit anti-Asp f 13 antiserum were identified, located throughout the entire molecule. In contrast, IgE from A. fumigatus-sensitive patients bound to three immunodominant epitopes at the C-terminal of the protein.
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PMID:Identification and expression of an allergen Asp f 13 from Aspergillus fumigatus and epitope mapping using human IgE antibodies and rabbit polyclonal antibodies. 1067 62

Proteinases are known to be capable of prolonging the survival of endoparasites in a host. We were therefore interested in knowing whether immunization of lambs against a proteasome (multisubunit proteinases) preparation obtained from Trichostrongylus colubriformis infective third-stage larvae (L3) would have any effect on the immune response to a single challenge infection with the same organism. A total of 21 penned lambs aged 8 months were divided into 3 equal groups. Group 1 was immunized on three occasions with increasing amounts of a proteasome-enriched fraction obtained from infective L3. Group 2 was given a similar amount of protein from the initial supernatant of homogenized larvae. Group 3 (controls) received adjuvant plus saline solution only. All groups were challenged with 60,000 infective T. colubriformis larvae at 28 days after the last immunization. Significant protection was obtained only when the initial supernatant extract was used to immunize lambs. The proteasome preparation seemed to have immunosuppressive effects through the stimulation of nonspecific IgE production. Significantly lower levels of specific IgE were observed in lambs immunized with the proteasome-enriched fraction, and levels of specific IgG antibodies were increased. We suggest that proteasome fractions of T. colubriformis may serve as useful preparations for the study of mechanisms of IgE production in parasitized sheep.
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PMID:Immunomodulation of lambs following treatment with a proteasome preparation from infective larvae of Trichostrongylus colubriformis. 1083 17

Engagement of the high affinity receptor for IgE (FcepsilonRI) on mast cells and basophils results in FcepsilonRI beta and gamma subunits ubiquitination by an as yet undefined mechanism. Here we show that, upon FcepsilonRI engagement on RBL-2H3 cells Syk undergoes ubiquitination and Syk kinase activity is required for its own ubiquitination and that of FcepsilonRI beta and gamma chains. This requirement was demonstrated by overexpression of Syk wild-type or its kinase-dead mutant in RBL cells or using an Syk-deficient RBL-derived cell line transfected with wild-type or a kinase inactive form of Syk. We also identify c-Cbl as the E3 ligase responsible for both Syk and receptor ubiquitination. Furthermore, we demonstrate that Syk controls tyrosine phosphorylation of Syk-associated Cbl induced after receptor engagement. These data suggest a mutual regulation between Syk and Cbl activities. Finally, we show that a selective inhibitor of proteasome degradation induces persistence of tyrosine-phosphorylated receptor complexes, of activated Syk, and of FcepsilonRI-triggered degranulation. Our results provide a molecular mechanism for down-regulation of engaged receptor complexes by targeting ubiquitinated FcepsilonRI and activated Syk to the proteasome for degradation.
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PMID:Activation of Syk tyrosine kinase is required for c-Cbl-mediated ubiquitination of Fcepsilon RI and Syk in RBL cells. 1214 91


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