Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P15088 (mast cell)
 14,925 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The complete sequence of 157 amino acids of the light (A) chain of high molecular mass urokinase from human urine was determined. The fragmentation strategy included cyanogen bromide cleavage of the S-carboxymethylated A chain at the methionine and/or tryptophan residues and use of the specific endoproteinase Lys-C. For sequence determination automated solid- or liquid-phase techniques of Edman degradation were used. C-terminal amino acids of the A chain were determined by consecutive treatment with carboxypeptidase A and B. The amino acid sequence obtained revealed a significant homology to peptide chains of other serine proteinases. Accordingly, the sequence of the A chain can be divided into three domains: 1) The growth factor domain with homologies to murine epidermal growth factor and a particular sequence of bovine clotting factor X, 2) The "kringle" domain with homologies to "kringle" structures, e.g. in plasminogen, and 3) the connecting peptide domain containing the A1 chain of low molecular mass urokinase. Together with the amino acid sequence of the B chain, which was presented by us in an earlier communication, the sequence data presented complete the primary structure of high molecular mass urokinase from human urine.
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PMID:The primary structure of high molecular mass urokinase from human urine. The complete amino acid sequence of the A chain. 675 69

Phenylpropynal is a specific, irreversible, non-beta-lactam inhibitor of typical beta-lactamases. In the presence of millimolar concentrations of phenylpropynal, the beta-lactamase I of Bacillus cereus and the beta-lactamases of Staphylococcus aureus and Escherichia coli become completely inactivated; the beta-lactamase II of B. cereus is not affected. The E. coli beta-lactamase is considerably more sensitive to the reagent than the gram-positive enzymes. A variety of structural analogs of phenylpropynal are much less effective inhibitors. Bovine alpha-chymotrypsin, bovine carboxypeptidase A, and the D,D-carboxypeptidase/transpeptidase of Streptomyces R-61 were not inactivated by phenylpropynal. The inactivation of the E. coli beta-lactamase can be significantly retarded when the good substrate benzylpenicillin is also present. The development of a characteristic chromophore (lambda max 318 nm) during beta-lactamase inactivation suggests that covalent modification of the enxymes is involved; arginine and/or lysine modification is indicated.
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PMID:Phenylpropynal, a specific, irreversible, non-beta-lactam inhibitor of beta-lactamases. 676 45

The complete amino acid sequences of the alpha and beta subunits of allophycocyanin from the unicellular rhodophyte, Cyanidium caldarium, were determined by automated Edman degradation of the proteins and peptides derived from them by chemical and enzymatic cleavages. The sequence of the alpha subunit was determined from the sequences of tryptic, endoproteinase lysine-C, and cyanogen bromide peptides and carboxypeptidase A and Y digestion of the protein. The sequence of the beta subunit was determined from the sequences of tryptic, endoproteinase lysine-C, Staphylococcus aureus V8 protease, and cyanogen bromide peptides and in addition, a peptide derived from acid cleavage of an aspartyl-prolyl bond. The carboxyl-terminal sequence of the protein was determined by digestion with carboxypeptidase A. The alpha subunit contains 160 amino acids, one phycocyanobilin chromophore attached at residue 80 by a cysteinyl-thioether linkage, and the Mr calculated from the sequence is 18,160. The beta subunit contains 161 amino acids, one phycocyanobilin chromophore attached at residue 81 by a cysteinyl-thioether linkage, and the Mr calculated from the sequence is 18,125. The amino acid sequences of the alpha and beta subunits of allophycocyanin from C. caldarium are the first complete amino acid sequences of an allophycocyanin from a eukaryotic red alga. A matrix comparison of the alpha and beta subunits of C. caldarium allophycocyanin and phycocyanin (Offner, G.D., Brown-Mason, A.S., Ehrhardt, M. M., and Troxler, R. F. (1981) J. Biol. Chem. 256, 12167-12175; Troxler, R. F., Ehrhardt, M. M., Brown-Mason, A. S., and Offner, G. D. (1981) J. Biol. Chem. 256, 12176-12184) shows homology ranging from 26 to 39%. Comparison of the sequences of alpha and beta subunits of C. caldarium allophycocyanin with the sequences of the corresponding subunits of allophycocyanin from two prokaryotic cyanobacteria (Sidler, W., Gysi, J., Isker, E., and Zuber, H. (1981) Hoppe-Seyler's Z. Physiol. Chem. 362, 611-628; DeLange, R. J., Williams, L. C. and Glazer, A. N. (1981) J. Biol. Chem. 256, 9558-9566) shows homology ranging from 81 to 85%. The significance of this with respect to phycobiliprotein structure and function is discussed.
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PMID:Primary structure of allophycocyanin from the unicellular rhodophyte, Cyanidium caldarium. The complete amino acid sequences of the alpha and beta subunits. 688 76

The activation peptide of the monomeric procarboxypeptidase A from porcine pancreas was isolated by means of controlled trypsin digestion of the proenzyme followed by ion-exchange chromatography under dissociating conditions (7 M urea). The molecular weight of the isolated peptide was estimated to be around 11500-12000 (corresponding to approx. 100-103 residues) as judged by SDS electrophoresis and amino acid analysis, a figure that agrees with the differences between the corresponding values for procarboxypeptidase A and carboxypeptidase A (peptidyl-L-amino acid hydrolase, EC 3.4.17.1). The activation peptide has a high content of hydrophobic and acidic amino acids, and lacks cysteine. A remarkable feature is the strong competitive inhibitory action of the peptide on both porcine and bovine pancreatic carboxypeptidase A activity, with a Ki in the nanomolar range, and its null ability to inhibit porcine pancreatic carboxypeptidase B (EC 3.4.17.2). The above properties, and the fact that the peptide has the same N-terminal residue (lysine) as the parent procarboxypeptidase A, suggest that the isolated peptide contains most (if not all) of the activation segment of the proenzyme.
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PMID:The severed activation segment of porcine pancreatic procarboxypeptidase A is a powerful inhibitor of the active enzyme. Isolation and characterisation of the activation peptide. 713 80

The synthesis of the mast cell-degranulating peptide by liquid-phase fragment condensation is described. After the carboxyterminal of the peptide is condensated with polyethylene-glycol (Mr 10000) the following fragments are coupled stepwise on the polymer, a soluble carrier in dichloromethane by the dicyclohexylcarbodiimide/hydroxybenzotriazole-method. Pos. 17-21 Boc-Lys(Z)-Ile-Cys(SiPr)-Gly-Lys(Z) (I) Pos. 12-16 Boc-Pro-His(Trt)-Ile-Cys(Trt)-Arg(Tos) (II) Pos. 8-11 Boc-His(Trt)-Val-Ile-Lys(Z) (III) Pos. 5-7 Boc-Cys(SiPr)-Lys(Z)-Arg(Tos) (IV) Pos. 1-4 Boc-Ile-Lys(Z)-Cys(Trt)-Asn(Mbh) (V) It is practical to crystallize the polyethyleneglycol peptide-coupling products from ethanol after each step. Most of the protecting groups can be removed by treatment of the complete polyethylene-glycol-peptide in trifluoroacetic acid/HBr. In methanol, saturated with ammonia, the peptide is removed in the amid-form from the carrier. The guanidyl-blocking group disappears by solving the peptide in liquid HF. The crude peptide is converted into the tetra-S-sulfonate derivate by oxidative sulfitolysis and purified by ion-exchange and gel chromatography. After reduction by mercaptoethanol a cautious air-reoxidation of the SH- to the SS-peptide followed. Rechromatography on ion-exchange and dextran gels yields a peptide with good biological activity in rat cell histamin-liberation and inflammation inhibition compared with the natural recombinated product.
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PMID:[Basic peptides from bee venom, IV. Synthesis of the mast cell-degranulating peptide by liquid-phase fragment condensation (author's transl)]. 738 Mar 91

Cathepsin B activity was demonstrated histochemically in unfixed cryostat sections of inflamed human gingiva using the 2-methoxy-4-naphthylamide (MNA) substrates Z-Val-Lys-Lys-Arg-MNA and Z-Ala-Arg-Arg-MNA with a post-azo-coupling technique. Enzyme localisation was confirmed by immunocytochemistry with polyclonal sheep anti-human cathepsin B. In both cases, staining was found in connective tissue fibroblasts and also in cells varying in shape from rounded to more irregular forms. The latter were present both in areas of cellular infiltration and in the oral and pocket epithelium. Examination of adjacent sections with monoclonal antibodies directed against leukocyte differentiation antigens showed that the rounded to irregular cells were CD68 positive macrophages and monocytes. The histochemical staining had the form of fine cytoplasmic particles consistent with the known lysosomal occurrence of cathepsin B. Cells stained by the post-coupling method using the tryptase substrates Z-Ala-Ala-Lys-MNA and D-Val-Leu-Arg-MNA showed a different distribution and morphology, with reaction product confined to mast cell granules. The differences between the cathepsin B and tryptase staining patterns were confirmed by differential extraction from cryostat sections with salt-free and high-salt buffers respectively. Biochemical characterisation of activities in the extracts with the 7-amino-4-trifluoromethyl coumarin (AFC) substrates Z-Val-Lys-Lys-Arg-AFC and Z-Ala-Ala-Lys-AFC and protease inhibitors confirmed the identity of the two enzymes. Selective inhibitors could also be used in histochemical incubations to distinguish between cathepsin B and tryptase staining.
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PMID:Comparative histochemical, biochemical and immunocytochemical studies of cathepsin B in human gingiva. 751 62

We compared angiotensin I-converting enzyme (ACE) and carboxypeptidase A (CPA), two zinc metallopeptidases, for the hydrolysis of the usual ACE synthetic substrate benzoylglycyl-histidyl-leucine (HHL) investigating the possible interference by CPA in the determination of ACE activity in biological fluids. Both purified enzymes hydrolyse HHL in a radiochemical assay with the same optimal pH, a characteristic divalent metal requirement, a close similar behavior against inhibitors of other metallopeptidases, such as enkephalinase and kininase I, and the involvement of arginine and lysine residues in their active site. Conversely, CPA does not show the other catalytic properties of ACe, i.e. chloride dependence, low Km for HHL, inhibition by specific synthetic ACE inhibitors and antibody, also hydrolysis of the other ACE substrate furylacryloylphenylalanyl-glycyl-glycine (FAPGG). We advise the use of ACE inhibitors to validate ACE measurement with HHL or, alternatively, FAPGG, which is a more specific substrate for ACE, must be preferred, although the poor sensitivity of the spectrophotometric assay with this substrate limits its use to blood samples.
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PMID:Carboxypeptidase A hydrolyses benzoylglycyl-histidyl-leucine but not furylacryloyl-phenylalanyl-glycyl-glycine, two usual substrates for angiotensin I-converting enzyme. 758 46

When administered by inhalation, adenosine 5'-monophosphate (AMP) provokes dose-related bronchoconstriction in asthmatic subjects by a mechanism believed to involve mast cell mediator release. However, little is known of the change in airway responsiveness to AMP after cyclo-oxygenase blockade. The aim of this study was to investigate the effect of the potent cyclo-oxygenase inhibitor, lysine acetylsalicylate (L-ASA) administered by inhalation, on AMP-induced bronchoconstriction in a group of nine asthmatic subjects. The subjects studied attended the laboratory on six separate occasions to receive nebulized L-ASA (solution of 90 mg.ml-1) or matched placebo (glycine solution, 30 mg.ml-1) 15 min prior to bronchoprovocation tests with AMP, histamine and methacholine in a randomized, double-blind order. Changes in airway calibre were followed as forced expiratory volume in one second (FEV1) and agonist responsiveness was expressed as the provocative concentration causing a 20% fall in FEV1 from baseline (PC20). Administration of both L-ASA and glycine solution caused a small but significant acute fall in FEV1 from baseline, which returned to normal within 15 min. When compared to placebo, inhaled L-ASA reduced the airway responsiveness to AMP in all the subjects studied, the geometric mean (range) values for PC20 AMP increasing significantly from 36.3 (7.9-250.5) to 101.8 (27.2-1300) mg.ml-1 after placebo and L-ASA, respectively. Moreover, nebulized L-ASA induced a small but significant reduction in airway responsiveness to histamine, the geometric mean (range) PC20 values for histamine increasing from 2.77 (1.05-5.49) to 4.36 (1.69-11.24) mg.ml-1 after placebo and L-ASA, respectively.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Inhaled lysine acetylsalicylate (L-ASA) attenuates the bronchoconstrictor response to adenosine 5'-monophosphate (AMP) in asthmatic subjects. 758 76

We examined the staining characteristics and degranulation of mast cells in bronchial biopsy specimens taken by fiberoptic bronchoscopy from 13 stable asthmatic patients and eight normal nonsmoking subjects. Specimens were fixed in periodate-lysine-paraformaldehyde, embedded in glycol methacrylate, and stained with toluidine blue (2%) for 30 min (pH 2.7) and 7 days (pH 0.5). The number of mast cells in the epithelium and in the lamina propria was counted under light microscopy. In addition, the distribution of mast cells with different granule contents, arbitrarily defined as degranulated or partly degranulated and fully granulated, was estimated at the two levels. In asthmatic subjects, the number of mast cells in the epithelium after either staining method was significantly higher compared with that in control subjects. The number of mast cells in the lamina propria, but not in the epithelium, was significantly higher after 7 days compared with 30-min toluidine blue stain both in asthmatic (135.6/mm2 versus 74.8/mm2; p < 0.001) and control subjects (121.5/mm2 versus 71.5/mm2; p < 0.01). There was evidence of a progressive mast cell degranulation when moving toward the airway lumen in both groups. However, degranulation was more evident in asthmatic subjects. In both groups, granulated mast cells were absent in the epithelium, whereas in the lamina propria granulated mast cells were approximately one-third of total in asthmatic and two-thirds of total in normal subjects. These observations suggest that mast cells in human bronchial mucosa are heterogeneous with respect to histochemical characteristics. They provide evidence that degranulation of mast cells occurs in both asthmatic and normal subjects and that degranulation is greater in asthmatics.
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PMID:Histochemical characteristics and degranulation of mast cells in epithelium and lamina propria of bronchial biopsies from asthmatic and normal subjects. 768 Jan 88

Tryptase-like activity has previously been identified biochemically in gingival homogenates and gingival crevicular fluid (GCF) using substrates linked to the 7-amino-4-trifluoromethyl coumarin (AFC) leaving group. In the present study, activity was demonstrated histochemically in tissue sections with analogous 4-methoxy-2-naphthylamide (MNA) substrates. Z-Ala-Ala-Lys-MNA and D-Val-Leu-Arg-MNA were the most sensitive substrates. Comparison of staining patterns with the MNA substrates and toluidine blue indicated that enzyme activity was localized to mast cell secretory granules. Most stained cells were in the lamina propria, but a few were in the epithelium. The number of stained cells was somewhat greater in inflamed tissue from chronic periodontitis patients than in healthy tissue from controls. However, hardly any staining was seen in inflamed granulomatous tissue. Using high-salt buffer containing heparin, it was possible to extract enzyme activity from tissue sections for biochemical analysis with corresponding AFC substrates. Inhibitors gave similar results in the biochemistry and histochemistry. The inhibitor response and pH profile of the enzyme were the same as that found earlier with gingival homogenates and GCF and were again consistent with mast cell tryptase. The enzyme may have a role in the pathology of chronic periodontitis.
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PMID:Comparative histochemical and biochemical studies of mast cell tryptase in human gingiva. 769 9


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