Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.21.1 (chymotrypsin)
 10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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

Supernatants from spleen cells, derived from mice injected with BCG and cultured with PPD, specificially inhibited the migration of normal mouse peritoneal macrophages when compared with control supernatants. Migration inhibitory supernatants were also shown to decrease the detachment of adherent macrophages in a novel test system. Both macrophage migration and detachment inhibitory activities were abrogated by neuraminidase and chymotrypsin treatment of supernatants but were thermostable, suggesting that the detachment test is a sensitive index of MIF activity.
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PMID:Effects of migration inhibiting factor(s) on the in vitro detachment of macrophages. 110 Jul 29

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

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