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)

A surface coat of host serum proteins was detected on virulent Treponema pallidum by sodium dodecyl sulfate-gel electrophoresis. The loosely associated serum proteins could be removed by repeated washings in a protein-free medium. Washed T. pallidum retained the ability to readsorb numerous host proteins from rabbit serum as well as iodinated rabbit or human albumin. In addition, various avidly associated host serum proteins including albumin, alpha(2)-macroglobulin, transferrin, ceruloplasmin, immunoglobulin G, immunoglobulin M, and C3 were identified on the outer envelope of washed treponemes by an immunoadsorbent technique with protein A-bearing staphylococcus. Hyaluronidase treatment did not remove the avidly associated host proteins from the surface of washed treponemes, whereas trypsin treatment resulted in decreased levels of agglutination. Electrophoretic patterns of trypsin-treated treponemes showed that treponemal proteins as well as adsorbed host proteins were released concurrently by protease digestion. Reacquisition studies involving alpha(2)-macroglobulin and transferrin suggested the presence of noncompetitive binding sites for serum proteins on the treponemal outer envelope. Finally, differences among the T. pallidum preparations from individual rabbits with respect to incorporation of [(35)S]methionine, extent of agglutination with antisera, and length of time required for removal of avidly associated host proteins by trypsin treatment indicated biological variability among the treponemal populations.
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PMID:Surface-associated host proteins on virulent Treponema pallidum. 9 74

Staphylococcus saprophyticus was found to differ from Staphylococcus epidermidis and Staphylococcus aureus by its ability to agglutinate sheep erythrocytes. On testing 30 strains of each species, 28 strains of S. saprophyticus and one strain each of the other two species, caused agglutination. Twenty-eight of 30 strains of staphylococcus cohnii and Staphylococcus xylosis failed to cause haemagglutination. The haemagglutinating activity of S. saprophyticus, when using a 10 per cent bacterial suspension was demonstrated in dilutions of 1:2-1:32. It was reduced twofold, at most, when exposing the bacteria to 56 degrees C for 30 minutes, while no agglutination could be demonstrated after treatment for 10 minutes at 86 degrees C. No haemagglutination could be demonstrated after treatment of the bacteria with 5 per cent solution of trypsin. Treatment of S. saprophyticus with 0.1 M EDTA did not affect the haemagglutinating activity, whereas exposure of the bacteria to 10 per cent trichloroacetic acid reduced the activity. The haemagglutination was D-mannose-resistant, and it was inhibited by homologous rabbit antiserum. The agglutinates dispersed when heated at 45-56 degrees C for 30 minutes. A few of the strains of S. saprophyticus tested also agglutinated human, bovine, and guinea pig erythrocytes.
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PMID:Haemagglutination by Staphylococcus saprophyticus and other staphylococcal species. 10 21

Specific antitrypsin precipitating sera obtained by intraconjunctival immunization of rabbits with crystalline trypsin was used to reveal in the supernant of staphylococcal cultures protease having antigenic character common with that of trypsin. This is confirmed by the trypsin accumulation in the process of staphylococcus cultivation, by the inhibition of the proteolytic activity of the antitrypsin precipitating sera and by the production of protein-precipitate as a result of incubation of the supernant with the antitrypsin precipitating sera.
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PMID:[Identification of proteases of staphylococci by means of an antitrypsin precipitating serum]. 122 77

Vascular endothelial cell factor VIII/von Willebrand factor antigen (FVIII/vWF Ag) of normal and disordered gastric tissues was studied with staphylococcus protein A-gold (PAG) labelling followed by photochemical silver reaction. FVIII/vWF Ag was localized clearly in the tissue fixed with various common fixatives and embedded in paraffin without enzyme treatment. The most satisfactory staining and the least nonspecific background were observed in the tissues fixed with Zamboni's and Bouin's solutions. The staining reaction could be enhanced, if the sections were pretreated with trypsin and subtilisin. Under the electron microscope, the gold particles were found over the Weibel-Palade bodies of vascular endothelial cells in the tissues fixed either in Zamboni's solution or in Zamboni's solution-osmium tetroxide, and embedded either with Lowicryl K4M or with Epon 812. It has been proved to be a better technique in investigation of FVIII/vWF Ag in vascular endothelial cells.
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PMID:Immunohistochemical localization of vascular endothelial cell factor VIII/von Willebrand factor antigen in human normal and disordered gastric tissues. 251 30

The association of Staphylococcus aureus, Staphylococcus epidermidis, and Staphylococcus saprophyticus with tissues of the upper respiratory tract were compared by using an in vivo ferret model. Ferrets were challenged intranasally with a 1-ml volume of radiolabeled staphylococci (3 mg [dry weight]), were allowed to clear the bacteria in vivo for 90 min, and were sacrificed. Tissues from the right nasal fossa were harvested and processed for radioassay or histology. Of the recoverable staphylococci, greater than or equal to 96% was associated with mucus gel overlaying mucosa of the turbinates. A quantitative radioassay was developed to study the binding of labeled staphylococci to immobilized crude ferret nasal mucin (FM) and bovine submaxillary gland mucin (BM). Binding showed saturation kinetics and was blocked specifically by BM but not by human Tamm-Horsfall glycoprotein nor orosomucoid. Binding to both FM and BM was significantly inhibited (P less than or equal to 0.01) when cocci were pretreated with trypsin but not when treated with beta-galactosidase or sodium metaperiodate (except for binding of S. saprophyticus to FM). These results suggest that mucin-binding receptors of the cocci may have protein components. The staphylococcus-binding receptors of both FM and BM appear to contain protein components, based on sensitivity to pretreatment with trypsin.
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PMID:Binding of staphylococci to mucus in vivo and in vitro. 280 45

Lysostaphin, a staphylococcus-derived staphylocidal substance, has widely been used in assays of granulocyte phagocytic and bactericidal capability. It rapidly kills extracellular bacteria. Thus, a separate determination of intracellular surviving bacteria can be performed. One prerequisite for this approach is the safe inactivation of lysostaphin (usually brought about by trypsin) before the intracellular bacteria are externalized for plating. This inactivation has been found by others to be incomplete. Data are presented demonstrating a safe inactivation of lysostaphin by trypsin, if the pH value is maintained within the alkaline range. A low variation of results is obtained by plotting the total number of bacteria killed per incubate vs the logarithm of initial bacterial inoculum or of the intracellular surviving bacteria, leading to linear regression lines. The variation of the results increases greatly for initial bacteria/granulocyte proportions of greater than 5/1. The results obtained for two different St. aureus strains are significantly different. Dexamethasone pretreatment (12 mg p.o. within 8 h) had no detectable influence, when fresh blood was assayed, while blood storage at room temperature for 12 h (without dexamethasone pretreatment) led to a significant functional impairment, mainly of bactericidal capability when analyzed in a pairwise fashion. A major limitation of this kind of assays is that killed bacteria cannot be determined directly.
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PMID:Lysostaphin-based assay of human granulocyte functions: a reevaluation. 353 97

The influence of trypsin on the formation of immune response induced by a thymus-dependent antigen at different periods of localized staphylococcal infection has been studied. A single intramuscular injection of bovine trypsin has been found to enhance immune response to sheep red blood cells (SRBC) in healthy mice and, to a still greater degree, in mice with localized staphylococcal infection. the development of localized staphylococcal infection has been shown to have no influence on the manifestation of the immuno-suppressive effect of splenocytes in SRBC-immunized mice or to enhance this effect. The injection of trypsin decreases the immunosuppressive effect of splenocytes in healthy or staphylococcus-infected hyperimmune mice.
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PMID:[Effect of trypsin on the immune response in localized staphylococcal infection]. 623 24

The effect of ionizing radiation of 0.05-10 Mrad on trypsin immobilized on dialdehyde cellulose was being studied. After irradiation the activity of native trypsin decreases by 25%, as compared with the initial, while the activity of immobilized trypsin remains constant. Before immobilization cellulose undergoes special pretreatment that leads to a decrease in the initial contamination. Some samples of modified cellulose were contaminated by staphylococcus culture (200,000 microbes per 0.2 g) and then exposed to irradiation of 0.05-0.4 Mrad. A distinct correlation between the irradiation dose (0.05-0.4 Mrad) and contamination of the object was registered.
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PMID:[Effect of gamma irradiation on immobilized trypsin]. 650 73

Staphylococcus epidermidis is the most commonly isolated coagulase-negative staphylococcus from the skin, gut and upper respiratory tract. Although it is less virulent than Staphylococcus aureus, it has emerged in recent years as an important causative agent of infections associated with metal implants, prosthetic devices and i.v. lines. We have previously demonstrated that a saline wash of S. aureus contained proteins which had potent bone-resorbing activity in vitro. The purpose of this study was to determine whether gently washing S. epidermidis in saline also released osteolytically active proteins. The so-called surface-associated material (SAM) eluted from S. epidermidis in saline was able to induce osteolysis, and activity was heat and trypsin sensitive, suggesting that the active component was proteinaceous. Fractionation studies have suggested that activity is due to a small number of cationic proteins. This SAM-induced bone resorption was not inhibited by the cyclo-oxygenase inhibitor, indomethacin, or the 5-lipoxygenase inhibitors BWA70C and MK886. However, it was partially inhibited by high concentrations of interleukin-1 receptor antagonist and was completely blocked by a neutralizing antibody to tumour necrosis factor-alpha. Thus, the SAM from this organism is a potent osteolytic agent which differs from that of S. aureus SAM in not being inhibited by cyclo-oxygenase inhibitors. As adjunctive therapy is becoming necessary in infectious diseases, either as a result of the side-effects of antibiotics or their lack of efficacy, consideration should be given to the future treatment of bone infections with staphylococci in the light of the different mechanisms of action of the surface proteins produced by these bacteria.
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PMID:Staphylococcus epidermidis produces a cell-associated proteinaceous fraction which causes bone resorption by a prostanoid-independent mechanism: relevance to the treatment of infected orthopaedic implants. 937 91

Lipid rafts and the formation of an immunological synapse are crucial for T-cell activation. Binding of cholera toxin B subunit (CTB) to ganglioside GM1 is a marker to identify lipid rafts. Primary human T cells were isolated from healthy donors and were stimulated with superantigen staphylococcus enterotoxin B (SEB) and stained with cholera toxin B-fluorescein isothiocyanate (CTB-FITC). An optimized staining procedure is required to stain lipid rafts exclusively on the cell surface. Unstimulated T cells show a few CTB binding spots on the cell surface. The size and number of CTB-binding lipid rafts are strongly upregulated during T-cell activation in SEB-stimulated CD4(+) T cells. However, our data show that the specificity of CTB for GM1 ganglioside is limited, because the binding capacity is partly resistant to inhibition of ganglioside synthesis and sensitive to trypsin digestion. Our results indicate that the binding of FITC-labeled CTB can be divided into at least three different categories: a specific binding of CTB to ganglioside GM1, a nonspecific binding of CTB probably to glycosylated surface proteins and a nonspecific binding of FITC to the cell surface.
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PMID:Cholera toxin binds to lipid rafts but has a limited specificity for ganglioside GM1. 1732 93


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