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:3.4.21.1 (chymotrypsin)
10,938 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Colony-stimulating factors (CSF) active on both human and murine bone marrow colony-forming units in culture (CFU-C) were found in the conditioned medium of Yoshida sarcoma cells (line YSSF-212T), although the cells originated from rats. The CSF were inactivated by digestion with trypsin, alpha-chymotrypsin, and pronase. By chromatography on DEAE-cellulose, the CSF were separated into five subgroups with different capacities to stimulate mouse granulocyte and macrophage progenitors. CSF in these five peaks were eluted from an Ultrogel AcA 44 gel filtration column with apparent molecular weights of 22,000-25,000 daltons. CSF of nonhuman origin stimulating human CFU-C would be useful in hematologic studies of bone marrow cells.
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PMID:Colony-stimulating factors active on human bone marrow cells from a Yoshida sarcoma cell line. 30 93

Human granulocyte elastase (EC 3.4.21.11) differs from hog pancreatic elastase in its specificity for synthetic substrates. Although hydrolyzing peptide bonds adjacent to the carboxyl group of alanine, the granulocyte enzyme prefers valine at the cleaved bond, in contrast to the pancreatic enzyme which prefers alanine. Peptide bonds involving the carboxyl group of isoleucine can be hydrolyzed by the granulocyte enzyme but are not hydrolyzed to any significant extent extent by pancreatic elastase. This difference in specificty could explain the lower sensitivity of the granulocyte enzyme to inhibitors containing alanine analogs, such as the peptide chloromethyl ketones and elastatinal. The human granulocyte chymotrypsin-like enzyme differs from pancreatic chymotrypsin by being able to cleave substrates containing leucine in addition to those containing the aromatic amino acids.
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PMID:Sbustrate specificity of the elastase and the chymotrypsin-like enzyme of the human granulocyte. 40 49

Several human granulocyte proteinases sensitive to the thermo- and acid-resistant proteinase inhibitor from rabbit serum (TASPI) were revealed, using TASPI-Sepharose 4B. It was found that TASPI inhibits the following human granulocyte proteinases: granules-localized kininogenase and chymotrypsin-like kininase (serine proteinases), elastase-like proteinase and benzoyl arginine ethyl ester esterase, as well as chymotrypsin-like kininase from the post-granule supernatant. These enzymes were compared to known granulocyte proteinases. Some carboxylic kininogenase sensitive to TASPI was identified in the granulocyte membrane debris fraction. The capability to inhibit neutral kininogenase suggests that TASPI is a first natural proteinase inhibitor, which can differentiate granulocyte and blood plasma kininogenases. Using trypsin-Sepharose 4B in the granulocyte post-granule supernatant, the acid-resistant trypsin and chymotrypsin inhibitor was identified. The data obtained are indicative of an antiinflammatory function of TASPI in mammals.
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PMID:[Inhibition of human granulocyte proteinases by a heat and acid-stable proteinase inhibitor from rabbit serum]. 43 77

A chymotrypsin-like enzyme (EC 3.4.21.-) was purified from granules of human neutrophiles (polymorphonuclear leucocytes). The isolation procedure included differential salt extractions of the granules followed by affinity chromatography on 4-phenylbutylamine-Affi-Gel. This rapid purification method resulted in obtaining pure enzyme in relatively high yield in short time. The purified granulocyte chymotrypsin-like enzyme has a minimum Mr of 22 378, calculated from its amino acid composition. The Mr value obtained by sodium dodecyl sulphate gel electrophoresis was 20 000-23 000. The enzyme did not react with antibodies which are monospecific to granulocyte elastase. The granulocyte chymotrypsin-like enzyme was inactivated by Dip-F and by the chloromethyl ketone derivatives Z-PheCH2Cl and Z-(Gly)2-PheCH2Cl but not by Tos-PheCH2Cl. It therefore appears that the enzyme has serine and histidine side chains in its active site, like pancreatic chymotrypsin. The granulocyte enzyme substrate specificity is similar to that of pac-Tyr-Nan and Ac-Phe-1-ONap. It also has an intrinsic weak hydrolytic activity towards some classical elastase substrates such as Boc-Ala-ONp and Ac-DL-Ala-1-ONap. The granulocyte enzyme is inhibited by human serum and by human alpha1-antitrypsin. Its affinity for alpha1-antitrypsin is weaker than that of granulocyte elastase for the same inhibitor. The enzyme is stable at neutral pH at 37 degrees C, but unstable at pH 3.5 and at elevated temperature.
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PMID:A rapid method for purification of human granulocyte cationic neutral proteases: purification and characterization of human granulocyte chymotrypsin-like enzyme. 108 Oct 3

We have identified a late, committed stage in the differentiation of the mast cell progenitor just before granulation. Mast cell committed progenitors (MCCP) are nongranulated cells with a density of 1.060 to 1.070 g/ml which can be harvested from the mesenteric lymph node of mice infected with Nippostrongylus brasiliensis. Mast cell-committed progenitors are able to proliferate and differentiate in the absence of IL-3 or IL-4 when cultured on a monolayer of embryonic skin or 3T3 fibroblasts and can form colonies in methylcellulose supplemented with fibroblast conditioned medium. Fibroblast conditioned medium appears to contain a soluble MCCP proliferation factor that maintains biologic activity when heated to 56 degrees C for 45 min but is destroyed by incubation with either trypsin or chymotrypsin. It can be selectively precipitated with 60 to 70% saturated ammonium sulfate. The factor is not absorbed by immobilized antibodies to nerve growth factor. The MCCP proliferation activity of the factor could not be mimicked by IL-1, IL-2, IL-4, granulocyte-macrophage-CSF, granulocyte-CSF, macrophage-CSF, IFN-alpha/beta, IFN-gamma, nerve growth factor, epidermal growth factor, serum fibronectin, heparin, or a number of glycosaminoglycans. At high salt concentrations, the factor passes through a 50-kDa membrane and can be concentrated above a 5-kDa membrane. MCCP acquire a connective tissue phenotype when cultured on a fibroblast monolayer and a mucosal phenotype when cloned in the presence of conditioned medium from PWM-stimulated spleen cells. When cultured in the absence of IL-3 on a monolayer of embryonic skin or 3T3 fibroblasts, mast cell-committed progenitors produce mast cells which stain with berberine sulfate suggesting a connective tissue phenotype; however, the mast cells that develop when mast cell-committed progenitors are cultured in the presence of IL-3 or conditioned media from PWM-stimulated spleen cells do not stain with berberine sulfate. MCCP intercalate into monolayers of embryonic skin or 3T3 fibroblasts, but T cells are not able to associate with the monolayer and can be completely washed away. Attempts to enrich mast cell-committed progenitors by intercalation and elution from embryonic skin monolayers proved unsuccessful, but some enrichment of mast cell-committed progenitors could be achieved by discontinuous Percoll gradients. Thus, we have identified a way to obtain late-stage, mast cell-committed progenitors in an environment that is virtually uncontaminated with other hematopoietic progenitors.
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PMID:The mast cell-committed progenitor. I. Description of a cell capable of IL-3-independent proliferation and differentiation without contact with fibroblasts. 278 62

The amino acid sequence has been determined for rat mast cell protease I (RMCP I), a product of peritoneal mast cells. The active enzyme contains 227 residues, including three corresponding to the catalytic triad characteristic of serine protease (His-57, Asp-102, and Ser-195 in chymotrypsin). A computer search for homology indicates 73% and 33% sequence identity of RMCP I with rat mast cell protease II from mucosal mast cells and bovine chymotrypsin A, respectively. When the structure of RMCP I is compared to those of cathepsin G from human neutrophils and two proteases expressed in activated lymphocytes, 48-49% of the sequences are identical in each case. RMCP I has six half-cystine residues at the same positions as in RMCP II, cathepsin G, and the two lymphocyte proteases, suggesting disulfide pairs identical with those reported for RMCP II. A disulfide bond near the active site seryl residue and substrate binding site, present in pancreatic and plasma serine proteases, is not found in RMCP I or in the other cellular proteases. These results indicate that RMCP I and other chymotrypsin-like proteases of granulocyte and lymphocyte origin are more closely related to each other than to the pancreatic or plasma serine proteases.
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PMID:Amino acid sequence of rat mast cell protease I (chymase). 312 23

Conditioned medium (CM) prepared from bone marrow (BM) or spleen (SPL) cells from mice injected with PGE2 in doses ranging from 0.0001 to 10 micrograms was found to contain an activity inhibitory to the proliferation of granulocyte-monocyte progenitor cells (CFU-GM). This activity was found in medium conditioned for 24 to 48 h, but was not present in medium conditioned for longer time intervals. BM cells from PGE2-treated mice incubated over a concentration range of 0.1 to 1.0 x 10(6) cells/ml and SPL cells over a range of 1.0 to 10 x 10(6) cells/ml produced CM with equivalent degrees of inhibition for CFU-GM proliferation. Titration of this activity revealed a significant inhibitory effect still present at a 1/256 dilution. Inhibitory activity was similar whether or not CM was prepared in the presence or absence of FCS. Inhibition of CFU-GM development was approximately equal in the presence of either PWM SPL CM or L cell CM as sources of CSF activity. Morphologic analysis of CFU-GM revealed an equivalent inhibition of monocyte, monocyte-neutrophil, and neutrophil CFU-GM by the PGE2-stimulated inhibitory activity. Equivalent picogram amounts of PGE were measured in CM derived from BM or SPL cells from either control or PGE2-treated mice, indicating a low probability that injected PGE2 was carried over in the CM and contributed to CFU-GM inhibition. Protease digestion of BM or SPL cell CM from PGE2-treated mice revealed a loss of inhibitory activity after trypsin, chymotrypsin, pronase, and neuraminidase treatment. Inhibitory activity was also ablated by heat treatment at 56 degrees C for 30 min and 100 degrees C for 5 min. Acrylamide-agarose gel filtration of BM CM revealed an active inhibitory fraction in the Mr range of 5.5 to 8.0 kDa. The results of the present study suggest that one of the mechanisms by which PGE2 exerts its in vivo myelopoietic inhibitory action may be by stimulating the production of an inhibitory factor or factors from BM and SPL cells.
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PMID:In vivo modulation of myelopoiesis by prostaglandin E2. IV. Prostaglandin E2 induction of myelopoietic inhibitory activity. 317 Nov 82

We have identified a neutrophil chemotactic factor (NCF) in supernatants from human blood mononuclear cells (MNC) cultured in the presence of phytohaemagglutinin (PHA). Maximal activity was observed 48 hr after culture. Following gel filtration, NCF eluted as a single major peak, together with proteins, having a molecular size of approximately 10,000 MW. The material gave a single band on SDS-PAGE but was heterogeneous following chromatofocusing (pIs approximately 6.8-7.0, 5.5-6.0 and 5.0). The biological activity of the partially purified material was abolished by trypsin and chymotrypsin treatment. NCF was heat stable (70 degrees, 60 min) and promoted both directional migration (chemotaxis) of neutrophils and, to a lesser extent, stimulated random locomotion (chemokinesis). The factor was not associated with detectable amounts of IL-1, IL-2 or interferon-gamma (IFN-gamma). MNC-derived NCF had a molecular size lower than recombinant granulocyte-monocyte colony-stimulating factor (rGM-CSF) and recombinant tumour necrosis factor (rTNF), and was considerably more active in chemotaxis. Optimal chemotactic concentrations of partially purified MNC-derived NCF were of comparable potency to FMLP and LTB4 and had about 60% of the activity of optimal concentrations of C5a, C5a-des-Arg and platelet-activating factor (PAF). These experiments indicate that the human MNC-derived NCF is a potent chemo-attractant distinct from other cytokines previously reported to promote neutrophil locomotion.
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PMID:The identification and partial characterization of a human mononuclear cell-derived neutrophil chemotactic factor apparently distinct from IL-1, IL-2, GM-CSF, TNF and IFN-gamma. 329 7

Serum-free medium conditioned by the normal rat kidney (NRK) cell line contains colony-stimulating factors (CSF) that stimulate the in vitro formation of granulocyte and macrophage colonies from rat, mouse, and human marrow. There are two types of CSF: NRK-CSF I stimulates rat and mouse marrow, while NRK-CSF II stimulates the human marrow. The NRK-CSF I has been partially purified to a specific activity of 5 X 10(7) units/mg by employing methods such as preparative isoelectrofocusing, gel filtration chromatography, and preparative gel electrophoresis. It has an isoelectric point of 5.1 and an apparent molecular weight of 35,000 daltons as estimated by gel filtration. It is stable at 50 degrees C for 30 min and relatively resistant to papain, but highly sensitive to trypsin, chymotrypsin, and subtilisin. The secretion of CSF by NRK cells is inhibited by actinomycin D (0.5 micrograms/ml) and cycloheximide (0.5 micrograms/ml), but not by cytosine arabinoside (5 micrograms/ml). Although the CSF activity is inactivated by periodate oxidation (5 mM), thus suggesting its glycoprotein nature, treatment of the CSF with neuraminidase and other glycosidases has no effect on its activity. Anti-NRK-CSF I antibody inhibits the rat/mouse-active CSF from all rat sources, but has no effect on the human-active CSF. Comparative studies with CSF from media conditioned by the transformed cell line (442) and from rat lung and spleen have shown that CSF I from different rat sources share similar isoelectric points, molecular weights, and immunological properties.
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PMID:Granulocyte-macrophage colony-stimulating factor from cultured normal rat kidney cell line. 620 75

Various flower bulbs and vegetable and legume seeds were tested for inhibitors of polymorphonuclear leukocyte elastase, pancreatic elastase, cathepsin G, cathepsin B, trypsin, alpha-chymotrypsin, Hageman factor fragments, plasma kallikrein, and plasmin. Calla bulbs contained a 33,000 dalton polymorphonuclear leukocyte elastase inhibitor and a 4,000 dalton cathepsin G inhibitor. Seeds of some members in the Cruciferae family, such as radish and broccoli, were found to contain one or more 2,500-4,000 dalton inhibitors which inhibited cathepsin G, trypsin, Hageman factor fragments, and plasmin, but not plasma kallikrein. These seeds also contained a 1,000 dalton cathepsin B inhibitor. The above inhibitors were probably polypeptides which inhibited proteinases by making an enzyme-inhibitor complex, with the exception of the cathepsin B inhibitor. These newly found inhibitors with their characteristic profiles of inhibition should be useful in biochemical and pathophysiological studies on granulocyte proteinases and enzymes of the coagulation and fibrinolytic pathways.
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PMID:Survey of plant inhibitors of polymorphonuclear leukocyte elastase, pancreatic elastase, cathepsin G, cathepsin B, Hageman factor fragments, and other serine proteinases. 634 Jun 94


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