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:3.4.21.4 (trypsin)
42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Capsular antigens were isolated from Pasteurella multocida, strain P-1059 and their immunogenicity was tested in turkeys. The crude capsular antigen (CCA) was extracted from bacterial cells grown on membranes by heating at 56 C in a 2.5% NaCl solution. The purified polysaccharide antigen (PPA) was obtained by precipitation of CCA by cetylpyridinium chloride. Young adult turkeys were inoculated at 0 and 14 days and were challenge exposed at 28 days by IM inoculation of a live culture of P-1059. The turkeys were observed for 2 weeks and mortality was recorded; bacterial isolation was done at the time of necropsy. In 3 trials, CCA provided 80% to 100% protection; in 1 trial, PPA failed to provide protection. Freund's incomplete adjuvant and aluminum hydroxide gel were effective as potentiating agents when higher than 280 microgram of CCA was used. The CCA showed significant (P less than 0.05) protection after treatment with heat (100 C, 5 min), chloroform, or trypsin, but lost its immunogenicity completely by acid hydrolysis. The CCA was not toxic to mice at 2 mg. The limulus lysate test showed that CCA contained endotoxin in less than or equal to 5% of the total solids. These results indicate that the surface antigen isolated from P multocida by saline extraction was immunogenic in young adult turkeys.
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PMID:Immunogenicity of capsular antigens of Pasteurella multocida in turkeys. 732 54

Autonomous, factor-independent growth and differentiation of malignant cells in preleukemic and leukemic disease states is a well-recognized phenomenon and is often associated with a poor prognosis. Mast cells are distinct hematopoietic cells and express a unique profile of antigens. Growth and differentiation of normal mast cells is dependent on mast cell growth factor (MGF), the ligand of the c-kit protooncogene product. In this study, we screened for mast cell-lineage involvement in 52 patients suffering from myeloid leukemias, myelodysplastic syndromes (MDS), systemic mastocytosis, or other diseases by probing for mast cell-related molecules (c-kit, tryptase, histamine, and MGF) and by analyzing kit ligand/MGF-independent growth of mast cells in long-term suspension culture. Of the 52 patients tested, 2 patients with refractory anemia with excess of blast cells in transformation and 1 patient suffering from chronic myeloid leukemia blast crisis (CML-BC) were diagnosed as mastocytic disease. These patients were characterized by complex chromosomal abnormalities, splenomegaly, high percentages of circulating metachromatic cells (5% to 25%), high levels of cellular tryptase (> 10 ng/10(5) peripheral blood mononuclear cells/mL) and a tryptase/histamine (ng:ng) ratio greater than 1. The metachromatic cells expressed the mast-cell-related surface antigen c-kit, but not basophil-related antigens (CD11b, CDw17). Furthermore, in these 3 patients, spontaneous, MGF-independent growth of mast cells along with spontaneous synthesis of tryptase was demonstrable in long-term culture. No autocrine production, paracrine production, or overproduction of MGF was found. The spontaneous growth of mast cells could neither be abbrogated by addition of monoclonal antibodies (MoAbs) to c-kit nor by MoAbs against MGF (< 5% inhibition), whereas factor (MGF)-dependent differentiation of mast cells in these patients could be abbrogated by MoAbs to c-kit or MoAbs to MGF (> 70% inhibition, P < .001). In addition, serum MGF levels in these patients were within the normal range and MGF could not be detected in cell-free culture supernatants. All 3 patients showed rapid progression of disease and had a survival time of less than 1 year. In conclusion, we describe a unique form of transformation in MDS and CML-BC characterized by mast cell lineage involvement and factor-independent differentiation of mast cells. This form of leukemic transformation has to be delineated from chronic myeloid leukemia with basophilia or basophil crisis, from primary mast cell leukemia, and from monocytic leukemias and myelodysplastic disorders associated with basophilia.
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PMID:Kit ligand/mast cell growth factor-independent differentiation of mast cells in myelodysplasia and chronic myeloid leukemic blast crisis. 752 72

CD6 is a 130-kD glycoprotein expressed on the surface of thymocytes and peripheral blood T cells that is involved in TCR-mediated T cell activation. In thymus, CD6 mediates interactions between thymocytes and thymic epithelial (TE) cells. In indirect immunofluorescence assays, a recombinant CD6-immunoglobulin fusion protein (CD6-Rg) bound to cultured human TE cells and to thymic fibroblasts. CD6-Rg binding to TF and TE cells was trypsin sensitive, and 54 +/- 4% of binding was divalent cation dependent. By screening the blind panel of 479 monoclonal antibodies (mAbs) from the 5th International Workshop on Human Leukocyte Differentiation Antigens for expression on human TE cells and for the ability to block CD6-Rg binding to TE cells, we found one mAb (J4-81) that significantly inhibited the binding of CD6-Rg to TE cells (60 +/- 7% inhibition). A second mAb to the surface antigen identified by mAb J4-81, J3-119, enhanced the binding of CD6-Rg to TE cells by 48 +/- 5%. Using covalent cross-linking and trypsin digestion, we found that mAb J4-81 and CD6-Rg both bound to the same 100-kD glycoprotein (CD6L-100) on the surface of TE cells. These data demonstrate that a 100-kD glycoprotein on TE cells detected by mAb J4-81 is a ligand for CD6.
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PMID:Identification and characterization of a 100-kD ligand for CD6 on human thymic epithelial cells. 753 42

The receptor for urokinase-type plasminogen activator (uPA-R) localizes uPA to the cell surface. The receptor-bound uPA converts plasminogen to the trypsin-like endopeptidase plasmin. Thus uPA is involved in the initiation of pericellular proteolysis. Pericellular proteolysis is assumed to facilitate the cellular infiltration into surrounding tissue. The uPA-R has recently been identified as a surface antigen of activated human T lymphocytes. We have characterized the uPA-R of the human CD4 T cell line Jurkat by immunological (flow cytometry), biochemical (ligand blotting), and physico-chemical (Scatchard blotting) methods. The collective data suggest that the human CD4+ T cell line Jurkat expresses a cell surface receptor for uPA similar to that of myelo/monocytes and normal T cells with regard to size, affinity, ligand specificity, and antigenicity. Binding studies using exogenous uPA and subsequent functional assays revealed that receptor-bound uPA retains its enzymatic activity. Saturation of the Jurkat cell uPA-R with exogenous uPA facilitated cellular invasion into fibrin matrices in vitro. uPA-dependent invasion was inhibited in the presence of an anti-catalytic monoclonal anti-uPA antibody. We propose that uPA-R-bound uPA may facilitate the invasiveness of uPA-R-positive T lymphocytes.
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PMID:Urokinase-type plasminogen activator enhances invasion of human T cells (Jurkat) into a fibrin matrix. 791 95

Hepatitis B surface antigen (HBsAg), devoid of 75% of its total lipids has been reconstituted with several phospholipids by the detergent dialysis method, using the non-ionic detergent beta-D-octyl glucoside. Upon reconstitution with both neutral and acidic phospholipids, HBsAg particles had the same morphology and, as indicated by trypsin hydrolysis, the topology of the surface proteins was maintained. However, only negatively charged phospholipids were able to completely revert the conformational changes which had been induced by removal of the lipids. The helical content, as indicated by CD techniques, and the antigenic activity, as measured by binding to polyclonal antibodies, of HBsAg reconstituted with acidic phospholipids were practically identical to those of the native antigen. Cholesterol had no effect on the antigenic activity recovered by reconstitution with any of the phospholipids.
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PMID:Reconstitution of hepatitis B surface antigen proteins into phospholipid vesicles. 820 49

Glucocorticoids exert their anti-inflammatory activity by modulating the functions of various cell types including macrophages. They also induce the generation of a distinct macrophage subtype defined by the surface antigen RM3/1 which appears to be associated with the down-regulation of inflammation. Supernatants from these cells were found to exert a dose-dependent anti-inflammatory effect, particularly in the early phase as shown in the 5-hydroxytryptamine (5-HT) induced footpad edema of mice. By using conventional purification methods the anti-inflammatory factor was found to have a molecular mass of about 78 kD and an isoelectric point of about 7.9. Heat lability and sensitivity to trypsin and proteinase K indicate the protein nature of the anti-inflammatory factor. The inhibition of the early phase of inflammation and the molecular weight suggest that the anti-inflammatory agent released from RM3/1 macrophages is a novel protein different from other anti-inflammatory proteins described so far.
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PMID:Characterization of a novel anti-inflammatory factor produced by RM3/1 macrophages derived from glucocorticoid treated human monocytes. 878 34

During part of its life cycle, the protozoan parasite Plasmodium falciparum lives within the human red blood cell and modifies both the structural and functional properties of the red cell. It does this by synthesizing a number of polypeptides that it transports into the red cell cytoplasm and to the red cell membrane. One of these transported proteins, MESA (mature parasite-infected erythrocyte surface antigen), is anchored to the red cell membrane by noncovalent interaction with erythrocyte protein 4.1. We have utilized a combination of in vitro transcription and translation and a membrane binding assay to identify the protein sequence involved in anchoring MESA to the membrane. Labeled fragments of different regions of the MESA protein were evaluated for their ability to bind to inside-out vesicle membrane preparations of human red cells. Binding was dependent on the presence of red cell membrane proteins and was abolished either by trypsin treatment or by selective depletion of membrane proteins. Binding was specific and could be inhibited by the addition of competing protein, with an IC50 of (6.3 +/- 1.2) x 10(-7) M, indicative of a moderate affinity interaction. Fractionation studies demonstrated that binding fragments interacted most efficiently with membrane protein fractions that had been enriched in protein 4.1. Binding inhibition experiments using synthetic peptides identified the binding domain of MESA for protein 4.1 as a 19-residue sequence near the amino terminus of MESA, a region capable of forming an amphipathic helix.
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PMID:Defining the minimal domain of the Plasmodium falciparum protein MESA involved in the interaction with the red cell membrane skeletal protein 4.1. 918 57

A protective surface antigen (200 kDa) on C. salmositica was detected using a monoclonal antibody (mAb-001). Enzymatic studies on the epitope indicated that it was sensitive to nonspecific protease K and to site-specific trypsin and protease V8 but not to alpha-chymotrypsin. The reactivity of the epitope with mAb-001 was not affected when the antigen was denatured with 8 M urea; however, reduction of the antigen with dithiothreitol destroyed the epitope. The epitope was susceptible to sodium m-periodate oxidation and N-glycosidase F, but not to O-glycosidase or neuraminidase. It was also sensitive to mild potassium hydrochloride hydrolysis and to phospholipase C, which is specific for phosphatidylinositol. These results suggest that the epitope consists of a polypeptide, a carbohydrate, and probably a phospholipid. The asparagine-bound N-glycosidically linked hybrid-type carbohydrate chain has the minimum length of a chitobiose core unit. There is probably a phosphatidylinositol residue which anchors the polypeptide to the surface membrane. The antigen is extensively posttranslationally modified.
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PMID:Biochemical characterisation of an epitope on the surface membrane antigen (Cs-gp200) of the pathogenic piscine haemoflagellate Cryptobia salmositica Katz 1951. 950 43

Six isolates of Mycoplasma bovoculi obtained from cattle herds with bovine keratoconjunctivitis were analyzed by gel electrophoresis and immunoblotting techniques. All six strains showed similarity in their protein profiles although no two patterns were identical. Antigenic differences between strains were detected in immunoblots reacted with post-exposure calf serum. A common 94 kDa protein band designated p94 was detected in all six strains reacted with monoclonal antibody MA25.5 developed to one of the strains. The p94 was also recognized in these strains by the calf serum. Trypsin treatment of intact mycoplasma cells resulted in the removal of p94 from immunoblots reacted with MA or hyperimmune rabbit serum. Other trypsin-resistant antigens shared between strains or being strain-specific in nature were identified when trypsin-treated mycoplasma cells were reacted with hyperimmune rabbit serum. The p94 antigen was shown to be of mycoplasmal origin by radio-immunoprecipitation using the MA or hyperimmune rabbit serum. These studies identify the presence of a surface antigen (p94) on M. bovoculi membrane in all strains examined that is trypsin sensitive by the use of monoclonal antibody, calf serum and hyperimmune rabbit serum.
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PMID:Identification and localization of a 94 kDa membrane protein found in Mycoplasma bovoculi strains. 977 58

The attachment of two strains of Mycoplasma bovoculi to erythrocytes was measured using 35S-methionine-labelled organisms. Receptor sites of M. bovoculi involved in this attachment are trypsin-sensitive, since mild trypsin treatment of the intact organisms abolished this process completely. Pretreatment of erythrocytes with trypsin or increasing concentrations of neuraminidase resulted in no measurable effect. Monoclonal antibody MA25.5 directed against a M. bovoculi surface antigen of 94 kDa termed p94 blocked 40% of the attachment, while MA18.13 directed against a 57 kDa protein band of M. bovoculi had no effect on the attachment process. Other properties of M. bovoculi were tested using six strains of the mycoplasma and erythrocytes from several animal species. None of the strains showed haemagglutinating or haemadsorbing activities.
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PMID:Interactions of Mycoplasma bovoculi with erythrocytes: role of p94 surface protein. 1041 66


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