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

Normal human sera contained 10-60 ng/ml of soluble membrane cofactor protein (MCP, CD46) whereas sera of > 50% of the cancer patients contained > 60 ng/ml. MCP purified by immunoaffinity chromatography from both normal and cancer patients' sera consisted of three bands of 56, 47 and 29 kDa on SDS-PAGE/immunoblotting. The upper two components were increased in cancer patient sera. The 56 and 47 kDa soluble forms served as a cofactor for factor I-mediated cleavage of C3b. MCP expressed on Chinese hamster ovary (CHO) cells protects host cells from human C3 deposition and complement-mediated cytolysis, especially by activation of the alternative pathway. In this same assay system, exogenously added soluble MCP also protected untransfected CHO cells; however, its potency was much less than that of the endogenous membrane form. For example, 8 micrograms/ml of soluble MCP was equal to 10(4) copies/cell of the expressed MCP. Recombinant soluble forms possessed similar activity to the naturally occurring soluble forms and high doses (> 150 micrograms) blocked Arthus-like reaction induced in guinea-pigs by anti-Forssman antibody. These data establish that soluble forms of MCP are present in human sera that possess cofactor activity and their concentrations, especially the 56 and 47 kDa forms, are increased in sera of cancer patients. High doses of the recombinant soluble forms may be therapeutically useful for suppressing inflammatory responses.
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PMID:Purification and functional properties of soluble forms of membrane cofactor protein (CD46) of complement: identification of forms increased in cancer patients' sera. 754

Six basic proteins of 26 to 38 kDa with isoelectric points (pI) > or = 8.5 were abundant in proteins separated by two-dimensional SDS-PAGE from adult rat peritoneal mast cells (MC). One was identified previously as rat mast cell proteinase (RMCP) 1, a chymase of 26 to 28 kDa, pI > 9.0. Microsequence analyses showed that two polypeptides of about 29 and 30 kDa had NH2 terminal amino acid sequences homologous to mouse MC proteinase 5 (MCP-5), whereas the amino terminals of the 33, 35, and 36 kDa proteins were homologous to MC carboxypeptidase A (MC-CPA). Rabbit Abs produced against synthetic peptides of the identified NH2 terminal sequences were used in immunoblot studies. At least three proteins reacted with Abs to MC-CPA, whereas Abs to MCP-5 detected three adjacent polypeptides, rather than just the two identified by using microsequence analysis. Removal of oligosaccharide side chains using peptide:N-glycosidase F reduced the heterogeneity of each set of three polypeptides (MCP-5 and MC-CPA) to a band of each protein of a lower M(r). The serine proteinase inhibitor [3H]diisopropylfluorophosphate ([3H]DFP) bound to a proteinase of 30 to 35 kDa, which is probably MC tryptase (pI < or = 6.0). Immunoblot analysis of proteins from intestinal mucosal mast cells showed RMCP-2, but not RMCP-1, MCP-5, or MC-CPA. This is the first report of MCP-5 in the rat and of clearly distinguishable glycosylated forms of MC CPA. These proteinases appear to be restricted in their distribution to selected MC populations, but little is known about their functions.
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PMID:Proteinases of rat mast cells. Peritoneal but not intestinal mucosal mast cells express mast cell proteinase 5 and carboxypeptidase A. 759 1

The ocular lens grows by laying down new cells on top of old in a differentiation process that results in loss of protein-synthesizing capacity, but preservation of the cells themselves for the lifetime of the organism. The transparency and refractive index of the lens depend on protein integrity and longevity, yet proteolysis is needed for normal growth and development. Therefore, control of proteolysis must be stringent. Here we review the structural features and major proteolytic enzymes of the lens and the properties of the bovine lens multicatalytic proteinase complex, including native and SDS-PAGE patterns, and activation and inhibition by cations, amphiphilic molecules and temperature.
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PMID:Bovine lens multicatalytic proteinase complex. 769 20

The lobster proteasome is primarily a cytosolic enzyme in crustacean striated muscles, although a small amount (< 1% of total) occurs in aggregates associated with invaginations of the cell membrane. The complex exists in vitro in three distinct catalytic states (basal, SDS-activated, and heat-activated forms) which have identical subunit compositions. This review summarizes recent results showing that the branched-chain amino acid-preferring (BrAAP) activity mediates the hydrolysis of myofibrillar proteins by the heat-activated proteasome: (a) only the BrAAP activity is stimulated by heat treatment; (b) the BrAAP activity is strongly inhibited by protein substrates, and (c) both the BrAAP and proteolytic activities show similar sensitivities to cations and protease inhibitors.
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PMID:Lobster muscle proteasome and the degradation of myofibrillar proteins. 769 21

Thermostable alkaline protease from an alkaliphilic thermophile Bacillus sp. B18' was purified by using DEAE- and CM-Toyopearl 650M column chromatographies. Molecular weights of the enzyme determined by SDS-PAGE and gel filtration were 30,000 and 28,000, respectively. The optimum pH and temperature toward the hydrolysis of casein were pH 12-13 and 85 degrees C, both of which are higher than those of a mesophilic alkaline protease from an alkaliphile, Bacillus sp. B21-2. The enzyme was stable at pH 5.0-12.0 and about 60% of the initial enzymatic activity was retained after a 60 min incubation period at pH 10.0 and 70 degrees C. Thermostability of the enzyme was enhanced by Ca2+. The enzyme activity was inhibited by DFP, suggesting that the enzyme is a serine protease. The NH2-terminal amino acid is Gln, which is that of many subtilisin-type proteases. The 20 residues of the NH2-terminal amino acid sequence have a comparative high homology with those of other alkaline proteases from alkaliphiles (40-50%), especially thermostable alkaline protease from Bacillus sp. No. AH-101 (95%) and Thermoactinomyces sp. HS682 (95%).
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PMID:Purification and properties of the highly thermostable alkaline protease from an alkaliphilic and thermophilic Bacillus sp. 776 36

We transformed Acremonium chrysogenum with the genomic DNA of the alkaline protease (Alp) from Fusarium sp. S-19-5 including its promoter. Most of the transformants thus obtained produced a large amount of Alp. PCR and Southern hybridization analysis of genomic DNAs from these transformants showed chromosomal integration of the full-length Alp gene. SDS-PAGE analysis of the supernatant from the transformants showed the presence of Fusarium Alp. The amino terminus of the Alp produced in A. chrysogenum was identical to that of native Fusarium Alp. These results indicate that the Alp promoter, signal sequence, and introns functioned correctly in A. chrysogenum. One of the transformants produced more than 4 g of the Alp per liter in a jar fermentor.
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PMID:High level expression of Fusarium alkaline protease gene in Acremonium chrysogenum. 776 54

The Sf-9 insect cells infected with a recombinant baculovirus integrated with a cDNA encoding human monocyte chemoattractant protein-1 (MCP-1) produced three different MCP-1s, which were isolated by reverse-phase HPLC as 13kDa, 14kDa, and 15kDa bands on SDS-PAGE. The heterogeneity between these MCP-1s was ascribed to the different degree of O-glycosylation with Gal beta 1-3GalNAc beta 1-Ser/Thr, while the 13kDa was regarded as carbohydrate-free. The integrity of the N-termius was confirmed by the amino acid sequence analysis. Each MCP-1 isolated showed equipotent monocyte chemotactic activity, which was rather higher than that of the E. coli-derived one.
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PMID:Full active baculovirus-expressed human monocyte chemoattractant protein 1 with the intact N-terminus. 783 10

Prosomes, also called "multicatalytic proteinase" or proteasomes, were purified from chick embryos of different developmental stages by a simple, single-step procedure. These were characterized by their characteristic protein patterns determined by SDS polyacrylamide gel electrophoresis (SDS PAGE) and immunoblotting with four monoclonal antibodies, namely, anti-p27, -p28, -p29 and -p31, prepared against duck prosomes. In vitro labeling of embryos with 35S-methionine followed by SDS PAGE and fluorography of the purified prosomes revealed that their polypeptides are differentially synthesized at various stages during development. Among 12 polypeptides (p21 to p56), p21 is synthesized at the beginning of gastrulation (stage 2) followed by the synthesis of p24 at stage 3. Nine other polypeptides (p25 to p35) are synthesized at the head-fold stage (stage 6), while the synthesis of polypeptide p56 is only detected at stage 10 (10-somite stage). Indirect immunofluorescence studies, with the 4 monoclonal antibodies, demonstrated 3 distinct, developmental stage-specific patterns of cytodistribution of these four prosome polypeptides in the embryos. During early embryogenesis, these are uniformly nuclear in location, while at later stages (stage 4 onwards) they are also present in the cytoplasm. Interestingly, one of the antigens (p 28), although found uniformly in all types of tissues in the embryos up to the gastrulation stage, is undetectable in the neural tissues and nonuniformly distributed in other tissues of stage-10 embryos. These data suggest that there are subcomponents of prosomes which are synthesized as well as distributed in an independent manner during development, possibly reflecting subcomponent-specific multiple functions of these particles.
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PMID:Differential synthesis and cytolocalization of prosomes in chick embryos during development. 784 36

Proteasomes are large multicatalytic proteinase complexes found in all eukaryotic organisms investigated so far. They have been shown to play a central role in cytosolic and nuclear proteolysis. According to their sedimentation coefficients two types of these particles can be distinguished: 20S proteasomes and 26S proteasomes. In contrast to 20S proteasomes, which were mainly characterized on the basis of their ability to cleave small chromogenic peptide substrates and certain proteins in an ATP-independent manner, 26S proteasomes degrade ubiquitinylated proteins in an ATP-dependent reaction. 20S proteasomes have been found in all eukaryotes from yeast to man. So far 26S proteasomes have only been discovered in higher eukaryotes. We now report the existence of the 26S proteasome in a lower eukaryote, the yeast Saccharomyces cerevisiae. Formation of the 26S proteasome could most effectively be induced in crude extracts of heat stressed yeast cells by incubation with ATP and Mg2+ ions. This treatment yielded a protein complex, which eluted from gel filtration columns at molecular masses higher than 1500 kDa. Besides chromogenic peptide substrates, this complex cleaves ubiquitinylated proteins in an ATP-dependent fashion. In non-denaturing-PAGE, the purified 26S proteasome disintegrated and migrated as four protein bands. One of these bands could be identified as the 20S proteasome. On SDS-PAGE, the 26S proteasome showed a complex pattern of subunit bands with molecular masses between 15 and 100 kDa. Further evidence for the 20S proteasome being the proteolytically active core of the 26S proteasome was obtained by following peptide cleaving activities in extracts of yeast strains carrying mutations in various subunits of the 20S proteasome.
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PMID:The 26S proteasome of the yeast Saccharomyces cerevisiae. 795 66


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