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)

Serum alpha1-antichymotrypsin (alpha1-ACT) of the patient with rheumatoid arthritis was studied by means of single radial immunodiffusion method. There was a significant elevation of the alpha1-ACT concentration in the patients with rheumatoid arthritis, and positive relationships were observed between the concentrations of alpha1-ACT and of other glycoproteins such as alpha1-acid glycoprotein and alpha1-antitrypsin in individual patients, and between C-reactive protein (CRP) rates and the (CRP) rates and the alpha1-ACT concentrations in individual specimens. These facts suggest that alpha1-ACT belongs to a group of acute phase proteins like alpha1-antitrypsin or CRP. An inverse proportional correlation was revealed between alpha1-ACT and fibrinolytic activity. No influences were observed on the alpha1-ACT concentration, activity index or articular index by the oral administration of alpha-chymotrypsin in patients with rheumatoid arthritis.
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PMID:Alpha1-antichymotrypsin in rheumatoid arthritis. 108 4

Serum amyloid P component (SAP) is a decamer of 10 identical 25.5-kDa subunits. Limited proteolysis of SAP with alpha-chymotrypsin cleaves the subunit into two fragments of 18 and 7.5 kDa, although the fragments stay together in the decamer under nondenaturing conditions. Proteolysis does not occur in the presence of Ca2+ (10 mM). Cleavage with alpha-chymotrypsin prevents the Ca(2+)-dependent binding of SAP to zymosan extract, nucleosomes, and DNA. The alpha-chymotrypsin cleavage site identified is in a region of SAP that is highly conserved in members of the human C-reactive protein (CRP) family of proteins (pentraxins) to which SAP belongs and is similar to the Ca(2+)-binding site in calmodulin and related Ca(2+)-binding proteins (Nguyen, N.Y., Suzuki, A., Boykins, R.A., & Liu, T.-Y., 1986, J. Biol. Chem. 261, 10456-10465). Treatment of SAP with other proteases (trypsin, Pronase, and Nagarse protease) yields fragmentation patterns upon sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) that are similar to those obtained with alpha-chymotrypsin. Two other members of the pentraxin family of proteins, hamster female protein and rabbit CRP, also exhibit similar fragmentation patterns on SDS-PAGE when treated with the various proteases. Recently, it has been shown that the homologous protein, human CRP, is cleaved in the same homologous position as cleavage of SAP by alpha-chymotrypsin, resulting in the loss of Ca(2+)-binding (as shown by equilibrium dialysis) and Ca(2+)-dependent binding reactivities (Kinoshita, C.M., Ying, S.-C., Hugli, T.E., Siegel, J.N., Potempa, L.A., Jiang, H.J., Houghten, R.A., & Gewurz, H., 1989, Biochemistry 28, 9840-9848).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:A protease-sensitive site in the proposed Ca(2+)-binding region of human serum amyloid P component and other pentraxins. 130 12

The influence of diclofenac, given by continuous i.v. infusion starting preoperatively, on postoperative pain and inflammation was assessed in a double-blind, randomized, placebo-controlled study in 40 patients scheduled for major orthopedic surgery. Starting 30 min before induction the patients received either diclofenac (0.35 mg.kg-1 bolus followed by a constant-rate infusion of 90 micrograms.min-1) or placebo for 24 h. The pain intensity (VAS) and the amount of rescue narcotic (piritramide on demand) were significantly lower in the diclofenac group from 4 and 6 h postsurgery, respectively, till end of infusion. Acute phase proteins used as inflammation markers (C-reactive protein, alpha 1-chymotrypsin, alpha 1-acid glycoprotein, haptoglobin and coeruloplasmin) showed similar variations in both groups for 24 h. The diclofenac treatment had no influence on hematological and coagulation profiles, nor on muscle and liver enzymes in comparison with placebo. Both patients and observer rated the diclofenac treatment as significantly superior to the placebo treatment.
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PMID:Prophylactic diclofenac infusions in major orthopedic surgery: effects on analgesia and acute phase proteins. 137 1

Previous studies indicated that synthesis of B beta chain may be a rate-limiting factor in the production of human fibrinogen since Hep G2 cells contain surplus pools of A alpha and gamma but not of B beta chains, and fibrinogen assembly commences by the addition of preformed A alpha and gamma chains to nascent B beta chains attached to polysomes. To test whether B beta chain synthesis is rate limiting Hep G2 cells were transfected with B beta cDNA, and its effect on fibrinogen synthesis and secretion was measured. Two sets of stable B beta cDNA-transfected Hep G2 cells were prepared, and both cell lines synthesized 3-fold more B beta chains than control cells. The B beta-transfected cells also synthesized and secreted increased amounts of fibrinogen. Transfection with B beta cDNA not only increased the synthesis of B beta chain but also increased the rate of synthesis of the other two component chains of fibrinogen and maintained surplus intracellular pools of A alpha and gamma chains. Transfection with B beta cDNA did not affect the synthesis of albumin, transferrin, or anti-chymotrypsin and had a small inhibitory effect on the synthesis of C-reactive protein. Taken together these studies demonstrate that increased B beta chain synthesis specifically causes increased production of the other two component chains of fibrinogen and that unequal and surplus amounts of A alpha and gamma chains are maintained intracellularly.
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PMID:Regulation of fibrinogen assembly. Transfection of Hep G2 cells with B beta cDNA specifically enhances synthesis of the three component chains of fibrinogen. 231 59

The concentration of 19 serum proteins was determined by radial immunodiffusion in 23 patients with Crohn's disease before and after treatment with parenteral nutrition. The results were related to body weight and Crohn's Disease Activity Index. An increased serum concentration of retinol-binding protein, prealbumin, and transferrin paralleled an increase of body weight. Alpha-1-glycoprotein, alpha-2-chymotrypsin, alpha-1-antitrypsin, C-reactive protein, and haptoglobin decreased during parenteral nutrition and showed a positive correlation to the Crohn's Disease Activity Index. The determination of certain proteins is clinically useful, since their serum concentration reflects the influence of parenteral nutrition on nutritional status and disease activity. Measurement of these proteins provides a useful guide to the management of patients with Crohn's disease treated with parenteral nutrition.
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PMID:[Effect of parenteral nutrition on serum proteins in patients with Crohn disease]. 680 21

The effects of vegetarian fasting were evaluated in 14 grossly obese patients who participated in a program comprising 5 weeks' fasting in a lactovegetarian health center. Before and after the fasting period the patients were hospitalized and put on a standardized weight-maintaining diet; at the health center they consumed vegetable juices containing less than 1 MJ and 3 g of protein per day. The weight reduction (mean +/- S.D.) was 13.4 +/- 5.0 kg (from 132.0 +/- 27.2 to 118.6 +/- 16.1 kg). Except for the first few days the patients had no severe hunger sensations. No severe adverse clinical effects were noted. The laboratory status--comprising serum or plasma levels of minerals, protein, and lipids; hematological data; and variables reflecting liver and thyroid function--revealed abnormal group mean values only for ferritin and the acute-phase reactants haptoglobin, C-reactive protein, and anti-chymotrypsin in the obese. The levels of potassium, retinol-binding protein, and haptoglobin decreased, and aminotransferase and lactate dehydrogenase activities and free fatty acid and glycerol concentrations increased as a result of the fasting. The most striking effect of the weight reduction was an increase in the HDL cholesterol levels. Fasting according to the described regimen thus seems to provide a safe method for treatment of obese patients.
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PMID:Vegetarian fasting of obese patients: a clinical and biochemical evaluation. 713 69

Thermally modified human C-reactive protein (H-CRP) and IgG (AHGG) each activate isolated human platelets to reactions of aggregation and secretion. As these molecules exhibit many functional similarities, we questioned whether they might also share a receptor on the platelet membrane. Neither plasmin nor phospholipase C altered the platelet response to H-CRP or AHGG, although these reagents enhanced the platelet expression to acid soluble collagen (ASC). Conversely, chymotrypsin treatment of platelets resulted in an elevated response to each H-CRP and AHGG, but not to ASC. These data suggest that the H-CRP and AHGG platelet receptors share characteristics which contrast with those of the receptor for collagen. However, monomeric IgG, which can bind with the platelet and inhibit the response to AHGG, exerted no effect on the platelet response to H-CRP. Further, a functional receptor for thermally modified human or rabbit CRP was detected on rabbit platelets in the absence of a demonstrable Fc receptor for aggregated IgG. These data indicate that the platelet receptors for the modified forms of CRP and IgG are distinct.
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PMID:Comparison of the enzymatic sensitivities of the platelet receptor for human C-reactive protein and its functional relationship to the platelet IgG Fc receptor. 717 7

To evaluate the effect of interleukin 10 (IL-10) on acute phase response, we determined serum levels of IL-10, interleukin 6 (IL-6), C-reactive protein (CRP), alpha-1-acid glycoprotein (AGP), alpha-1-anti-chymotrypsin (ACT) in 34 rheumatoid arthritis (RA) patients. IL-10 and IL-6 levels were evaluated using an enzyme-linked immunoassay (ELISA). CRP, AGP and ACT levels were measured using rocket immunoelectrophoresis. The results showed that IL-10 serum level was increased in RA patients as compared to controls (60.0 +/- 17.5 pg/ml vs. 7.2 +/- 1.9 pg/ml). IL-6 level was significantly elevated (87.3 +/- 32.7 pg/ml vs. 45 +/- 19 pg/ml, p < 0.05). CRP was significantly increased as compared to healthy controls (34 +/- 19 mg/1 vs. 3 +/- 2 mg/1, p < 0.05). AGP and ACT serum levels were increased in RA patients, but we did not find these changes to be statistically significant. A good negative correlation between IL-10 and IL-6 serum level was found (r = -0.73, p < 0.05). A positive significant correlation between IL-6 serum level and CRP (r = 0.62, p < 0.05), AGP (r = 0.74, p < 0.05) and ACT (r = 0.45, p < 0.05) was established. Moreover, a negative correlation between IL-10 and serum level of CRP (r = -0.76, p < 0.05), AGP (r = -0.60, p < 0.05) and ACT (r = -0.37, p < 0.05) was also shown. According to the data thus far obtained it seems that IL-10 decreases IL-6 production, and by that indirectly affects acute phase response, decreasing CRP, AGP and ACT synthesis.
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PMID:Interleukin 10 inhibits interleukin 6 production and acute phase response in rheumatoid arthritis. 874 78

A study was carried out to investigate the efficacy of trypsin: chymotrypsin (Chymoral forte DS) preparation on burn patients by analysing the changes taking place in serum acute-phase proteins. Serum proteins were analysed qualitatively and quantitatively for both control and enzyme-treated groups by the methods of Western Blot, ELISA and Turbidimetric assays. Furthermore, the trypsin inhibitory capacity (TIC) of the sera was also determined. Significant differences were observed between a control group of patients and a parallel group treated with trypsin: chymotrypsin preparation. During the first phase of burn wounds an initial rise was seen in C-reactive protein, alpha 1-antitrypsin, alpha 2-macroglobulin and TIC in both the groups. In the following days, enzyme preparation inhibited the rise in C-reactive protein titres and enhanced the rise in alpha 1-antitrypsin, alpha 2-macroglobulin and TIC. The above studies clearly indicate that the changes in serum acute-phase proteins between the control and treated groups reflect the anti-inflammatory activity and hence the therapeutic efficacy of Chymoral forte DS.
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PMID:Action of trypsin:chymotrypsin (Chymoral forte DS) preparation on acute-phase proteins following burn injury in humans. 917 94

Two-dimensional (2-D) gel analysis was used to examine differences in the levels of 19 plasma proteins: before and after an acute inflammatory reaction (parenteral typhoid vaccination) in normal subjects, between rheumatoid arthritis (RA) patients and normals and in RA patients treated with tenidap (120 mg) and piroxicam (20 mg). Typhoid vaccination increased levels of SAA, haptoglobin alpha1, haptoglobin alpha2, haptoglobin beta and alpha1-anti-chymotrypsin but decreased transthyretin and apolipoprotein E. In RA patients, serum amyloid A (SAA), haptoglobin alpha2, haptoglobin beta, alpha1-antichymotrypsin and C3 proactivator levels were elevated while apolipoprotein A-I, apolipoprotein A-IV, transthyretin, Gc-globulin, alpha2-HS glycoprotein, alpha2-macroglobulin and alpha1-B glycoprotein levels were decreased, compared to normals. Compared to piroxicam, tenidap lowered levels of alpha1-antiprotease and SAA but raised the levels of transthyretin, Gc-globulin, alpha2-HS-glycoprotein and alpha2-macroglobulin in RA patients. C-reactive protein (CRP) could not be quantified on 2-D gels but, when measured by rate nephelometry, levels were reduced after treatment with tenidap compared to piroxicam. The general pattern of the acute phase protein response to an acute inflammatory response to typhoid vaccination is similar to that in the chronic inflammatory condition, RA. The impact of tenidap on both positive and negative acute-phase proteins in RA patients could clearly be distinguished from that of piroxicam.
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PMID:Analysis of changes in acute-phase plasma proteins in an acute inflammatory response and in rheumatoid arthritis using two-dimensional gel electrophoresis. 954 3


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