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

The 22076-Mr Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces abuls G effectively catalyses the transfer of the N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolysing penicillin into penicilloate at a very low rate. This protein consists of 212 amino acid residues in a single polypeptide chain. The N terminus is partially blocked as a result of the cyclization of the dipeptide Asn-Gly into anhydroaspartylglycine imide. The protein has been fragmented by cyanogen bromide into five fragments whose sequences have been determined via appropriate subcleavages with various proteases. The ordering of the cyanogen bromide peptide fragments has been carried out (a) by submitting the S-carboxymethylated protein to complete tryptic digestion and labelling the methionine-containing peptides thus obtained with iodo[14C]-acetamide, and (b) by submitting to limited tryptic digestion the S-[2-(4'-pyridyl)ethyl]-cysteine protein whose amino groups have been blocked by reaction with exo-cis-3,6-endoxo-delta 4-tetrahydrophthalic anhydride prior to digestion. The protein contains six cysteine residues in the form of three disulfide bridges. No homology is found by comparing this peptidase with other Zn2+-containing enzymes (carboxypeptidase A, thermolysin, carbonic anhydrase B and alcohol dehydrogenase) and several completely or partially sequenced, serine-containing D-alanyl-D-alanine-cleaving peptidases and Zn2+/serine-containing beta-lactamases.
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PMID:The complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G. 682 89

Although changes in proteolysis in muscle tissue are now well documented for a variety of physiological and pathological conditions, the mechanism of degradation of cellular protein during normal protein turnover remains to be elucidated. Data from several laboratories have suggested the involvement of alkaline serine proteinases. Recent studies have questioned these results, and demonstrated that the serine proteinases are of mast cell origin and are not present in muscle cells. The only proteinases to date that have been shown to be present in muscle cells and capable of degrading myofibrillar proteins are Ca2+-activated proteinase, cathepsin B, and cathepsin D. Recent interest and developing awareness of endogenous enzyme inhibitors in cells may unmask many new enzymes.
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PMID:Proteinases in cardiac and skeletal muscle. 698 69

Proteolytic enzyme activities were measured in skeletal muscle of Sprague-Dawley rats with streptozotocin-induced diabetes [tail vein injection of streptozotocin (100 mg/kg), under ether anesthesia]. Assay of rat muscle homogenates from diabetic rats revealed a significant increase in alkaline serine protease activity as compared to untreated control rats and diabetic rats given insulin. There were no significant changes in lysosomal cathepsin activities in diabetic muscle as compared to controls. Gel studies of myofibrils isolated from the three groups of rats, subjected to autolysis, revealed that the serine protease had copurified with the myofibrils. Treatment of rats with compound 48/80, which degranulates mast cells, abolished the alkaline protease activity. There was no serine protease activity associated with the myofibrils isolated from compound 48/80-treated rats. Results from this study indicate that serine proteases are not involved in muscle protein breakdown in diabetes and are of mast cell origin.
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PMID:Muscle proteolytic enzyme activities in diabetic rats. 703 84

An alkaline proteolytic activity from the smooth muscle of mouse small intestine has been separated and characterised. The activity sedimented after high-speed centrifugation, but was released into the soluble phase after treatment with 2.0 M KCl. The proteinase was found to be sensitive to salt concentration and the activity was maximal between 0.1-0.5 M NaCl/KCl and pH 9.5. This activity was completely inhibited by di-isopropylphosphoro fluoridate suggesting that it is a serine endopeptidase. The proteinase was identified as chymotrypsin-like due to the inhibition observed with the agents chymostatin, lima bean and soya bean trypsin inhibitor. These characteristics of the alkaline proteinase resemble the properties of the mast cell enzyme, chymase. The enzyme activity was measured in 48/80 treated animals and the mutant strain w/wv, which do not contain mast cells. No significant reduction in the enzyme activity was observed.
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PMID:Alkaline proteolytic activity from smooth muscle of mouse small intestine. 704 3

An unusual type of posttranslational modification has been observed in a rat brain in vitro system. It consists in leucine addition to a preformed protein in such a way that the added leucine is not located at either the NH2 or the COOH terminus of the acceptor protein. The incorporation reaction requires ATP, ATP-generating components and tRNA. It is inhibited by aurintricarboxylic acid but does not require the presence of ribosomes or GTP. The incorporated leucine has a free NH2 group, and it is not released by leucine aminopeptidase or carboxypeptidase A. It is linked to the acceptor protein through a bond that is too alkali labile and too hydroxylamine labile to be a peptide bond. The simplest interpretation of the results consists in proposing that an ester bond is formed between the leucine and the side chain of a serine, threonine, or tyrosine in the acceptor protein.
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PMID:Transfer ribonucleic acid dependent but ribosome-independent leucine incorporation into rat brain protein. 717 78

Based on the correlation between the kinetics and free energy of enzymatic reactions of hydrolysis (i. e. free energy linearity principle) for peptide and ester substrate hydrolysis by carboxypeptidase A, the identity of the catalytic mechanism for these substrates and the lack of formation of an activated enzyme intermediate with the C-terminal part of the hydrolyzed substrate were demonstrated. Using the energy linearity principle to the hydrolysis of specific peptide substrates by chymotrypsin, the nature of the activated enzyme intermediate with the C-terminal part of the substrate as a complex with a non-ionized product can be postulated. This accounts for the transpeptidation (according to the amino transfer type) of the peptides with an unprotected carboxylic group. It was concluded that the formation of the enzyme intermediate with the C-terminal part of the hydrolyzed substrate for all the three main classes of proteinases, i. e. serine, carboxylic and metal enzymes, occurs via different mechanisms.
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PMID:[Enzyme intermediates with the C-terminal products of substrate hydrolysis by carboxypeptidase A and chymotrypsin. Use of the free energy linearity principle]. 723 96

The neutral protease cathepsin G belongs to a family of hematopoietic serine proteases stored in the azurophil granules of the neutrophil granulocyte. To investigate the function of asparagine-linked carbohydrates in neutrophil serine proteases, we constructed a mutant cDNA, coding for human cathepsin G deficient of a functional glycosylation site, for use in a transgenic cellular model. Wild type and mutant cDNA were stably expressed in the rat basophilic/mast cell line RBL and in the murine myeloblast-like cell line 32D. Biosynthetic labeling, followed by immunoprecipitation, SDS-polyacrylamide gel electrophoresis, and fluorography, showed that carbohydrate-deficient cathepsin G was synthesized as a 29-kDa proform in both cell lines. The proform was proteolytically processed into a stable form with an apparent molecular mass of 27.5 kDa, indicating removal of the carboxyl-terminal prodomain. The mutant cathepsin G was enzymatically activated as determined by acquisition of affinity to aprotinin, a serine protease inhibitor. As for wild type cathepsin G, small amounts of the unprocessed form of the mutated enzyme were released from the cells, while the major part was transferred to a granular compartment as demonstrated by subcellular fractionation. Thus, neither processing leading to enzymatic activation nor granular sorting was obviously affected by the lack of oligosaccharides on the mutant cathepsin G. Our results therefore indicate that glycosylation is not essential for these processes. In addition to the previously utilized cell line RBL, we propose the 32D cell line as a suitable cellular model for transgenic expression of human neutrophil serine proteases.
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PMID:Human cathepsin G lacking functional glycosylation site is proteolytically processed and targeted for storage in granules after transfection to the rat basophilic/mast cell line RBL or the murine myeloid cell line 32D. 749 46

The effects of rat stem-cell factor (SCF) and interleukin-3 (IL-3), alone or in combination, on the in vitro growth and serine proteinase expression of rat serosal/connective-tissue mast cells (CTMC) or bone marrow-derived mast cells (BMMC) were examined. Rat SCF stimulated the growth of both CTMC and BMMC. IL-3 stimulated BMMC growth to a lesser extent than did SCF, whereas CTMC numbers did not increase in IL-3. However, SCF and IL-3 had synergistic effects on the growth of both BMMC and CTMC. SCF favoured the maintenance of rat mast cell proteinase-I (RMCP-I) in CTMC, but did not induce detectable production of RMCP-I in BMMC. In contrast, when IL-3 or lymph node-conditioned medium (LNCM) was added to SCF, a subpopulation of CTMC expressed and stored the soluble proteinase RMCP-II. In BMMC, the RMCP-II content of cells maintained in SCF was significantly less than that of cells maintained in IL-3 or LNCM. RMCP-II also appeared in the supernatants of BMMC, especially when BMMC numbers were increasing rapidly in SCF with or without IL-3 or LNCM. Thus, SCF and IL-3 can regulate the growth of rat BMMC and CTMC, as well as influence their production and release of proteinases.
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PMID:Effects of stem cell factor (kit-ligand) and interleukin-3 on the growth and serine proteinase expression of rat bone-marrow-derived or serosal mast cells. 750 83

Serine proteinases participate in many inflammatory events in the airway. We therefore screened perfusates of isolated rat tracheas for tryptic, elastolytic, and chymotryptic serine proteinases. Only chymotryptic activity, indicated by hydrolysis of the synthetic substrate N-succinylalanylalanylprolylphenylalanyl p-nitroaniline (AAPF), was consistently detected in these perfusates. Basal levels of chymotryptic activity were not increased significantly by electrical field stimulation (EFS) (mean change +/- SEM: -0.05 +/- 0.05 m o.d. units, n = 4) or by 10(-7) M substance P (SP) (+0.04 +/- 0.02 m o.d. units, n = 14). However, the mean change after the stimuli were jointly administered (0.17 +/- 0.06 m o.d. units, n = 12) was significantly greater than control or after EFS (P = 0.01, one-way ANOVA). The SP + EFS-induced chymotryptic activity was inhibited by PMSF, soybean trypsin inhibitor, and chymostatin and was associated with an increase in histamine concentration and immunoreactivity to rat mast cell proteases (RMCP), indicating that the activity is due to mast cell degranulation. However, the activity was not significantly decreased by pretreating rats with systemic compound 48/80. SP + EFS-induced chymotryptic activity peaked rapidly and was associated with modest histamine release and an immediate peak in immunoreactivity to RMCP II, a marker of mucosal mast cells. Immunoreactivity to RMCP I, a marker of connective tissue mast cells, also increased after SP + EFS, but this immunoreactivity was either delayed or more sustained and did not coincide with the peak of chymotryptic activity.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Chymotryptic activity in perfusates of isolated rat trachea: correlation with mucosal and connective tissue mast cell secretion. 752 16


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