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)

1. The effects of intraperitoneal injections of actinomycin D on the temporal characteristics of the accumulation of the inflammatory exudate and cells into the peritoneal and pleural cavities were studied in male Sprague Dawley rats. 2. A measurable quantity of the exudate appeared in both cavities within 24 h and reached maxima in the peritoneal and pleural cavities on the fourth and third days, respectively. Thereafter, the accumulated volume of liquid decreased progressively in the peritoneal cavity but stayed more or less at about the same level in the pleural cavity until the sixth day. 3. The pooled peritoneal and pleural exudates contained neutrophils, macrophages, mast cell and eosinophils. The leucocyte infiltration occurred in two phases, the maximum cell numbers being found on the third and fifth days. A precipitous fall in the number of leucocytes occurred on the fourth day. Neutrophils and macrophages accounted for 85-95% of the total number of leucocytes. 4. The supernatant of the inflammatory exudate after centrifugation at 3,000 g contained histamine and the soluble lysosomal enzyme proteins, acid phosphatase and beta-glucuronidase until the sixth day following the initial dose of actinomycin D. 5. It is suggested that the release of lysosomal enzymes in the exudate, subsequent to leucocyte mobilization and the release of histamine from the mast cells, are probably involved in the genesis of inflammatory conditions induced by actinomycin D.
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PMID:Mobilization of leucocytes and subsequent release of histamine and lysosomal enzymes into the peritoneal and pleural cavities of rats by actinomycin D (dactinomycin). 5 Jan 58

Dipeptidyl aminopeptidase II (DAP II) was demonstrated cytochemically in rat peritoneal mast cells. The bright red reaction product in smears of peritoneal wash fluid tended to be localized in one to eight granules in the perinuclear region of the cell. This finding was confirmed at the electron microscopic level, where a small proportion of the granules, most often located near the nucleus, revealed electron opacity indicative of DAP II. Focal areas in the nuclear envelope densified by DAP II reaction product resembled reactive foci observed previously in the nuclear envelope of peritoneal macrophages. In mast cells exposed 1 to 2 hours to phosphate-buffered saline containing horseradish-peroxidase--coated colloidal gold, the spherules of gold were internalized and transported exclusively to the DAP II-reactive granules. Their content of endocytosed gold thus identified DAP II-reactive granules as secondary lysosomes of heterophagic nature. Mast cells induced to release their granules by stimulation with the divalent cation ionophore A23187 retained exclusively those granules possessing DAP II or acid phosphatase reactivity. This selective granule retention after ionophore exposure further differentiated granules with DAP II reactivity from the other non-reactive mast cell granules, presumably indicating a difference between the limiting membrane of granules that are converted to secondary lysosomes and the membrane of those that are not altered and persist as primary lysosomes. Demonstration of the DAP II reactivity in a minority of mast cell granules and of the heterophagic nature of these granules provides evidence that tissue mast cells in vivo function in endocytic activity by transporting material of extrinsic origin to some of their granules which are thereby transformed to heterophagic bodies or constitute previously existing heterophagosomes.
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PMID:The heterophagic granules of mast cells: dipeptidyl aminopeptidase II activity and resistance to exocytosis. 42 34

To clarify whether in vitro-cultured basophils have features of mast cells, basophils grown in semisolid and liquid culture were studied ultrastructurally and cytochemically and were compared with freshly isolated basophils and mast cells. Ultrastructurally, the cultured basophils had pleomorphic cytoplasmic granules, some of which were similar to mast cell granules. However, scroll formation, characteristic of mast cell granules, was not observed in cells grown in semisolid and liquid culture. Cytochemically, the reactivity patterns of acidic glycoconjugates in the cultured cells more closely resembled those of the freshly isolated basophils than of the mast cells. In addition, the basophils grown in liquid culture showed a more matured form and had stronger reactivity to glycoconjugates, acid phosphatase and peroxidase than did the cells grown in semisolid culture, suggesting that the liquid culture system was better for the basophil.
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PMID:Cultured human basophils with ultrastructural and ultracytochemical features of mast cells. 291 98

The ACTH influence upon the thymus may be a reliable model for stress involution. In this case, the cortical lymphocytic depletion is accompanied by mast cell accumulation and increased caliber of the blood vessels. The blood-thymus barrier which has an active role in involution shows an enriched transport activity of the endothelial cells, great enlargement of the basement membrane, increased macrophage activity within the perivascular space with elevated values of acid phosphatase activity, and thickening of the fibrillar network. The epithelioreticular cells show plenty of vacuoles in their cytoplasm, the mitochondria undergo swelling processes, and their cristae are diminished. The ultrastructural data show that lymphocyte depletion is carried out by macrophage-mediated lymphocytolysis. But by counting the peripheral blood cells an earlier mechanism is revealed; i.e. migration through the enlarged but more permeable blood-thymus barrier. The epithelioreticular cells do not seem to have an active, direct implication in any of the phenomena.
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PMID:Elements of structure and ultrastructure of the blood-thymus barrier in ACTH involuted thymus. 627 4

Rat mast cell granules contain a spectrum of enzymes as established by histochemical techniques and subcellular fractionation. However, 35% of the beta-glucuronidase, 30% of the beta-D-galactosidase, 14% of the beta-hexosaminidase and all of the acid phosphatase is not available for immunologic release from purified rat serosal mast cells, suggesting the presence of nonsecretory lysosomes containing these acid hydrolases. On the other hand, immunologic release of the majority of chymase, beta-hexosaminidase, beta-glucuronidase, beta-D-galactosidase, and arylsulfatase A occurs in parallel with histamine and thereby localizes these substances to the rat mast cell secretory granule. A molecular model of the secretory granule in the resting mast cell can now be constructed in which heparin proteoglycan is the granule matrix to which chymase and probably other proteins are ionically bound. Inhibition of chymase by serotonin stored in its active site and of chymase and acid hydrolases by their interaction with heparin probably occurs. Histamine is stored by ionic linkage to carboxyl groups of protein and heparin. Micromolar amounts of heparin glycosaminoglycans, histamine, serotonin, chymase, beta-D-hexosaminidase, beta-glucuronidase, and arylsulfatase A in secretory granules of 10(6) mast cells are 0.7--1.3 x 10(-3), 70--220 x 10(-3), 0.9--28 x 10(-3), 0.2--0.5 x 10(-3), 0.9--2.7 x 10(-6), 0.1--0.3 x 10(-6) and less than 8 x 10(-6), respectively. In addition, the total protein available for calcium ionophore-induced release from 10(6) rat mast cells is about 60 microgram, indicating that less than 50% of the granule protein can be accounted for. Recognition that mast cell secretory granules contain acid hydrolases indicates that they are modified lysosomes; their special intracellular and extracellular functions are dictated by the associated novel constituents and the stimulus for activation.
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PMID:Enzymes of the mast cell granule. 677 34

Lysosomal acid hydrolases were surveyed in elicited and non-elicited rat peritoneal macrophages to determine the types of enzymes present and optimal assay conditions. Adherent peritoneal cells (primarily macrophages) were cultured 24 hours prior to use. Intracellular distribution of enzymes was determined by differential centrifugation of whole cell homogenates into nuclear, cytoplasmic, and lysosomal fractions. The acid glycosidase, acid phosphatase, acid protease, and lysozyme were largely sedimentable in the lysosomal fraction. Much enzyme activity was latent, being activated by addition of Triton X-100. Chymotrypsin-like protease activity in cell fractions was apparently due to low level mast cell contamination. Elicited macrophages had elevated total cell protein as compared to non-elicited cells, but changes in intracellular enzyme levels were selective depending on the enzyme and the stimulus used to elicit macrophages. Thioglycollate-elicited cells showed elevations of most acid hydrolases compared to non-elicited cells, whereas enzyme levels in zymosan-elicited cells were similar to those in non-elicited cells. All elicited cells showed marked decreases in total cellular alpha-D-mannosidase and alpha-L-fucosidase compared to non-elicited cells. Intracellular lysozyme levels also varied between different rat strains. Cultured macrophages exhibited increasing intracellular levels and extracellular secretion of acid hydrolases, especially extracellular lysozyme (10-25 mug/10(6) cells/day), over 72 hours. No significant intra- or extracellular elastinolytic activity was detected.
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PMID:Selective modification of rat peritoneal macrophage lysosomal hydrolases by inflammatory stimuli. 710 74

Equilibrium sedimentation experiments of the native acid phosphatase indicate a dimer-tetramer dissociating nonequilibrating system with a dimer Mr = 180,000 g/mol. The hydrolysis of nitrophenylphosphate was used to determine the sedimentation coefficient of the active species. The s20,w value for the species which degrades nitrophenylphosphate is 13.52 +/- 0.46 S in 1% sucrose and 13.72 +/- 0.11 S in 1.3 M sodium chloride, corresponding to the Svedberg value of the tetramer species. Several lines of evidence are presented which, together with previous data, indicate that the Schizosaccharomyces pombe nonspecific acid phosphatase is composed of 4 identical or nearly identical polypeptide chains: a, equilibrium sedimentation analysis of the enzyme in denaturing agents indicates the presence of homogeneous material having Mr = 90,800 g/mol; b, digestion with carboxypeptidase A releases 0.82 mol of tyrosine/monomer molecular weight. Concomitant phosphatase inactivation occurred during the splitting off of the tyrosyl terminal residue. Furthermore, a unique NH2-terminal residue (histidine) was determined.
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PMID:Molecular properties and active form of nonspecific acid phosphatase from Schizosaccharomyces pombe. 721 63

The intralysosomal localization of the enzymes that catalyse inactivation of rat liver fructose-bisphosphate aldolase (D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase, EC 4.1.2.13) to a form with antigenic activity was demonstrated. The inactivating enzymes like all other lysosomal markers tested except acid phosphatase, were readily solubilized by hypotonic shock. The inactivating enzyme activity was inhibited by PMSF, TPCK, TLCK and leupeptin, but not by pepstatin. On partial purification of the inactivating activity from the lysosomal fraction by DEAE-Sephadex (A-50) and Sephadex G-100 column chromatographies, it was copurified with lysosomal carboxypeptidase A and cathepsin B (EC 3.4.22.1). Studies on its substrate specificity and sensitivity to inhibitors indicated that cathepsin B and carboxypeptidase A are responsible for almost all the aldolase-inactivating activity in the lysosomal fraction.
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PMID:Properties of fructose-1,6-bisphosphate aldolase inactivating enzymes in rat liver lysosomes. 726 Jan

To understand better the pathophysiology of random skin flaps, randomized skin flaps of human (3 cases) and guinea pig (53 cases) were investigated. Proximal (normal), proximomedial (viable), mediodistal (between viable and necrotic parts), and distal (necrosis) locations of the skin flaps were biopsied. Lipid peroxidase, hydrolytic enzymes of cytosol (Ca(2+)-dependent cysteine protease: calpain), and lysosome (acid phosphatase) of skin were used as markers. Measurements were taken of the flap blood flow; the numbers of capillaries, postcapillary venules, pericapillary arterioles, leukocytes, and mast cells per unit square of dermis. Apoptotic cells were identified by specific staining. Flaps were sampled at postoperative weeks 1 and 3 (human) and hours 1 and 6, and days 1 to 7 (guinea pig). The values for normal skin were regarded as the control. Obstruction (by leukocytes) of venous microvessels, rather than arterial microvessels, was the major cause of temporary hypoxia in the proximomedial location, constant hypoxia (venous stasis) in the mediodistal location, and ischemia in the distal location. Increases in the number of mast cells (mastocytosis) and microvessels (angiogenesis) were significant only in the viable parts of the flaps. This phenomenon and the rate of blood flow increased with time in viable locations (guinea pig). Epidermal necrosis, dermal fibrosis, and apoptosis were evident mostly in the mediodistal location. Elevated levels of leukocytes, lipid peroxidase, acid phosphatase, and calpain, combined with necrotic changes, were seen mostly in the distal skin location. There is a strong possibility that the following factors are involved: lipid piroxidation and hydrolysis in necrosis of the distal flap location after ischemia; constant hypoxia in fibrosis and apoptosis in the mediodistal location; and initial or temporary hypoxia in mastocytosis-induced angiogenesis in the viable location. The results presented here indicate that guidelines for further investigations include combined suppression of leukotaxis, lipid peroxidase, and hydrolysis, or the application of mast cell growth factors in an effort to salvage the flap maximally.
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PMID:Possible contributions of mastocytosis, apoptosis, and hydrolysis in pathophysiology of randomized skin flaps in humans and guinea pigs. 870 Sep 87

1,3-beta-D-glucans (glucans) are structural elements in the cell walls of yeast and fungi with immunomodulatory properties, mediated through their ability to activate macrophages. This study assessed the activation of cells of the peritoneal cavity between 3 and 90 days after i.p. injection of particulate yeast glucan differing in molecular weight (MW) and degree of (1,6)-linkages. Female QS mice, 7-9 weeks of age, were injected, i.p., with varying doses of low (< 5 x 10(5)), medium (1-2 x 10(6)) or high (> 3 x 10(6)) MW glucans, all with low (< 5%) beta-(1,6)-linkages, or high MW (> 3 x 10(6)) glucan with high 1,6-linkages (> 20%). All glucans induced a transient increase in the proportion of neutrophils and eosinophils and a reduction in mast cell numbers in the peritoneal cavity. Peritoneal macrophages showed an altered morphology, increased intracellular acid phosphatase, increased LPS-stimulated NO production and increased PMA-stimulated superoxide production. There were no significant changes in serum lysozyme levels. Most macrophage activities returned to control levels by 28 days post injection of 1, 3-beta-D-glucan. There was a trend for higher MW or (1,6)-linked, (1, 3)-beta-D-glucans to be more stimulatory. It was concluded that particulate yeast (1,3)-beta-D-glucan is an effective stimulator of immune function, the efficiency of which may be influenced by the MW and degree of (1,6)-linkages.
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PMID:The effect of molecular weight and beta-1,6-linkages on priming of macrophage function in mice by (1,3)-beta-D-glucan. 1054 Feb 5


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