Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.4 (trypsin)
 42,187 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Soluble blood group substances, with human H and A activity, have previously been shown to block the interaction between guinea pig peritoneal macrophages and migration inhibition factor from fetal calf serum (FCS-MIF). Conversely, incubation of macrophages at 37 degrees C for 1 h in the presence of 0.1% blood group substance, followed by thorough washing, potentiates the action of FCS-MIF. The sensitivity of the macrophages is markedly increased, allowing detection of subthreshold levels of FCS-MIF. Blood group substances (BGS) labeled with radioidine are taken up by macrophages, and a proportion remains on the surface. This radiolabeled BGS is lost from the surface spontaneously, and the rate of loss is increased by treatment with trypsin. It is suggested that the BGS mimic the natural macrophage receptor for FCS-MIF and potentiate its effect by incorporating new receptors into the macrophage membrane.
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PMID:Potentiation of the macrophage response to migration inhibition factor from fetal calf serum by blood group substances with human H activity. 79 86

Using an assay of macrophage migration, where the cells emigrate from an agarose droplet, it was found that the neutral proteases trypsin, chymotrypsin, Pronase and elastase have MIF-like activity. Appropriate enzyme inhibitors counteract this effect. To twelve synovial fluids from patients with inflammatory arthritis, which have MIF-like activity (migration index between 0-3 and 0-7) protease indhibitors (Trasylol, ovomucoid and soybean inhibitor) were added. Ten of the fluids lost some of their MIF-like activity with at least one inhibitor. Phenylmethylsulphonylfluoride counteracted totally the MIF-like activity of the two fluids tested. It is concluded that MIF-like activity of inflammatory synovial fluids is due, at least partially, to proteases.
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PMID:Migration inhibition factor-like activity in inflammatory synovial fluids might be due to proteases. 79 49

It was found that a preparation of mouse L cell interferon induced by Newcastle disease virus (NDV) possessed not only interferon activity but also inhibitory activity upon migration of guinea pig peritoneal macrophages (MIF activity). These activities were also observed in a preparation of human leukocyte interferon induced by NDV. The interferon and MIF activities shared common characteristics in the dose response, time course of in vitro production, thermal stability, sensitivity to trypsin and periodate, and elution pattern in CM-Sephadex column chromatography. However, gel filtration pattern with Sephadex G-100 showed two separate peaks. Fractions collected from the first peak, corresponding to a molecular weight of about 45 000, had only the MIF activity, while those collected from the second peak, corresponding to a molecular weight of about 30 000, had both the interferon and MIF activities. A preparation of mouse brain interferon induced by Japanese encephalitis virus had a much weaker MIF activity than the L cell interferon, although these preparations were equal in interferon activity (5000 units/ml).
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PMID:Inhibition of macrophage migration by virus-induced interferon preparations. 124 96

After presenting processed glycoprotein of Leishmania donovani to T-cell, macrophage seeks the help of a panel of T-cells lymphokines to transform from a state that sustains intra cellular replication of parasite to an effector state for destructing parasites. But esterase and trypsin of macrophage membrane prevent T-cells to release MIF. Role of soya-bean trypsin inhibitor (STI) has been exposed in the present study with a view to alter esterase functional behaviour of macrophage for control of T-cell activation and also, if T-cells once made responsive to antigen by STI do alter macrophage response to T-cells or not. Results establish STI as potent effector molecule, which can serve as an adjuvant to candidate T-cell epitope and synthetic peptide for development of anti-Kala-azar vaccine protocol in future.
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PMID:Reversal of T-cell unresponsiveness through serine-esterase inhibitors mediated enhanced lymphokine induced microbicidal activities in kala-azar. 150 18

A nonspecific inhibitor of macrophage migration was found in large quantities in the cell-free ascitic fluids from patients with ovarian tumours. MIF-like activity was assigned by the ability of various dilutions of ascitic fluids to inhibit migration of guinea pig macrophages from agarose droplets. The factor was purified in 3 subsequent steps including ion exchange chromatography, gel filtration, and isoelectric focusing. The data obtained indicate molecular heterogeneity according to net charge and molecular weights. The main MIF activity was found at about 45, 20, and 10 kD, respectively, and partially at less than 10 kD. Isoelectric focusing of the various MIF species revealed activity peaks in the pH range from 3.8 to 5.0. A further peak was detected at pH 6.0 in crude material. The factor was purified about 10 000-fold compared to the starting material. The action of OC-MIF was inhibited by L-fucose, and when target cells were incubated with alpha-L-fucosidase, they did not respond any longer to OC-MIF. Furthermore, purified MIF-like activity is a nondialyzable glycoprotein, sensitive to treatment with neuraminidase, chymotrypsin, trypsin and pronase, however, unaffected by incubation at 60 degrees C for 1 h. The physicochemical properties of OC-MIF activity studied are comparable to lymphocyte-derived conventional MIF.
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PMID:Inhibition of macrophage migration by a factor from ascites fluids of ovarian cancer patients. I. Biochemical characterization and purification. 351 10

Human T-cell hybridomas were established by hybridization of concanavalin A (Con A)-stimulated human peripheral blood T lymphocytes with cells from a 6-thioguanine-resistant, aminopterin-sensitive mutant line designated CEM-WH4, derived from the continuously growing human T cell line, CEM. High levels of MIF activity were demonstrated in the supernatants of two hybridoma lines, T-CEMA and T-CEMB but not of CEM-WH4 when stimulated with phorbol myristate acetate and phytohemagglutinin. In comparison, MIF derived from Con A-stimulated peripheral blood mononuclear cells showed 100 times less activity. Upon isoelectrofocusing, MIF activity of T-CEMB was found exclusively between pH 4.6 and 5.3 whereas MIF derived from T-CEMA showed heterogeneity with a major peak of MIF recovered at pH 4.6-5.3 and a minor peak at pH 2.4-3.3. These molecules, however, were all found to have an apparent MW of 68,000 and were resistant to trypsin. Most of these characteristics are in accordance with second day pH 3- and pH 5-MIF derived from peripheral blood mononuclear cells. When spleen cells from BALB/c mice immunized with T-CEMB-MIF were used to fuse with NS-1 mouse myeloma cells, nine hybridomas secreting antibodies to human MIF were obtained. Clone D112 which demonstrated the highest MIF-neutralizing activity was found to neutralize MIF derived from T-CEMA, peripheral blood mononuclear cells, and a T cell line, Mo.
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PMID:Generation of human hybridomas producing migration inhibitory factor (MIF) and of murine hybridomas secreting monoclonal antibodies to human MIF. 388 Nov 87

Supernatants from 24 hr cultures of PHA-pulsed human T lymphocytes inhibit the migration of human peripheral blood T lymphocytes and guinea pig macrophages in vitro. The factor responsible for the inhibition of T lymphocytes provisionally called TIF (T cell migration inhibitory factor) was separated from MIF by preparative PAGE, had apparent molecular weight (m.w.) of 1,000-10,000 daltons and isoelectric point of 3.1. TIF activity was resistant to treatment with trypsin, chymotrypsin and neuraminidase but sensitive to PMSF (phenyl-methyl-sulfonyl-fluoride). This suggests that TIF is presumably different from human MIF and may represent a novel lymphokine which preferentially affects T cell migration in vitro.
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PMID:Partial purification and physicochemical properties of human T cell migration inhibitory factor (TIF). 639 62

Delta-sleep-inducing peptide (DSIP)-like material was detected in human breast milk of two women by RIA with a recovery of about 90%. The high concentration of DSIP-like immunoreactivity (DSIP-LI) in colostrum (30 ng/ml) decreased to about 10 ng/ml in milk. The concentration continued to decrease over the next 2 months in one women. In the same woman, a significant circadian rhythm of the amount of breast milk DSIP was found with the peak in the afternoon and the trough in the morning. A significant effect of the sampling procedure was detected in the other woman examined; lower amounts of DSIP-LI were found when the milk was collected before and higher concentrations after nursing. Gel chromatography revealed that most of the immunoreactive DSIP-LI in milk and colostrum occurred in a form larger than the nonapeptide. The presence of DSIP itself, however, was demonstrated by high pressure liquid chromatography, which also showed additional peptides reacting with the antibody. Digestion of the large immunoreactive DSIP-LI by trypsin produced a peak on Sephadex G-10 that coeluted with DSIP. This peak contained three immunoreactive fractions with retention times on high pressure liquid chromatography similar to DSIP, phosphorylated DSIP, and N-tyrosine-DSIP. Plasma samples taken during pregnancy were assayed for DSIP but no difference from normal values was found. Slightly higher amounts were found in placenta than in blood, which might be due to interfering substances. No Tyr-MIF-1 or corticotropin-releasing hormone was detected by RIA in human breast milk. Peptides and proteins of milk can be absorbed from the gastrointestinal tract of babies, but it is not known if the DSIP-LI in human milk is involved in the induction of a sleep-wake cycle in neonates.
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PMID:Presence of delta-sleep-inducing peptide-like material in human milk. 654 44

Hodgkin and Reed-Sternberg (HRS) cells in Hodgkin lymphoma (HL) secrete factors that interact with inflammatory background cells and may serve as biomarkers for disease activity. To detect new proteins related to pathogenesis, we analyzed the secretome of HRS cells. Proteins in cell culture supernatant of 4 HL cell lines were identified using 1DGE followed by in-gel trypsin digestion and LC-MS/MS. In total, 1290 proteins, including 368 secreted proteins, were identified. Functional grouping of secreted proteins revealed 37 proteins involved in immune response. Sixteen of the 37 proteins (ie, ALCAM, Cathepsin C, Cathepsin S, CD100, CD150, CD26, CD44, CD63, CD71, Fractal-kine, IL1R2, IL25, IP-10, MIF, RANTES, and TARC) were validated in HL cell lines and patient material using immunohistochemistry and/or ELISA. Expression of all 16 proteins was confirmed in HL cell lines, and 15 were also confirmed in HL tissues. Seven proteins (ALCAM, cathepsin S, CD26, CD44, IL1R2, MIF, and TARC) revealed significantly elevated levels in patient plasma compared with healthy controls. Proteomics analyses of HL cell line supernatant allowed detection of new secreted proteins, which may add to our insights in the interaction between HRS cells and infiltrating lymphocytes and in some instances might serve as biomarkers.
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PMID:Proteomics analysis of Hodgkin lymphoma: identification of new players involved in the cross-talk between HRS cells and infiltrating lymphocytes. 1807 Sep 85

Aqueous extracts of the thymus of animals which had been challenged immunologically have been shown to contain MIF activity. This MIF could be purified by precipitation with 70% ethanol, concentrated by ultrafiltration between 30,000 and 50,000 daltons, isoelectrically focused at pH 6.8-7.1, and electrophoresed on preparative acrylamide gels. The resulting product is electrophoretically homogeneous at pH 4.3 in polyacrylamide-gel electrophoresis and SDS-gel electrophoresis. It has a molecular weight of 36,000 daltons. It is trypsin- and neuraminidase-labile and is thermostable. It degrades and reassembles in electrophoresis at pH 7.0. It is not chemotactic for macrophages but apparently activates them phagocytically. It has no proteolytic activity.
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PMID:Purification of thymic macrophage migration inhibitory factor (MIF). 2419 28


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