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

Thin sections in mouse mast cells and thymic cells are stained with cobalt thiocyanate a compound known to form insoluble complexes with organic bases. Chromatin, nucleolus, ribosomes and mast cell granules are contrasted. Different blockade reactions and enzymatic digestions indicate the staining corresponds to the basic protein amino-groups. The silver methenamine reaction stains the same cellular structures. However, the specificity control reactions show the staining mainly corresponds to protein sulphydryle groups and in a lesser extent to aldehyde and polyanions.
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PMID:Cobalt thiocyanate as a stain for basic proteins and other organic bases on thin sections. 7 73

We have previously reported that Tranilast, an anti-allergic agent, was rapidly taken into the cytoplasm of rat mast cells in vitro by means of light microscopic radioautography. The present study was performed at the electron microscopic level to elucidate the fine localization of this agent in the mast cells. The results revealed that the number of radioautographic silver grains in the cells increased by the incubation with 3H-labelled Tranilast for 0 to 60 min. and that many silver grains were localized on the specific granules, especially on the perigranular membranes. These results suggest that the mode of inhibitory action of mast cell degranulation by Tranilast is related to the specific localization of this agent on the perigranular membranes.
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PMID:Electron microscopic radioautographic study of the localization of an anti-allergic agent, Tranilast, in rat mast cells. 169 12

Mast cells are common in the thymic parenchyma of the European common frog, Rana temporaria. They are stained meta chromatically with toluidine blue and the majority of them are impregnated with silver during the argentaffin reaction. The latter phenomenon indicate that these cells store serotonin. At the ultrastructural level, mast cells contain specific granules with electron-dense and electron-lucent parts. The silver grains are located exclusively over the electron-lucent part of the mast cell granules indicating that serotonin is stored just in this compartment.
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PMID:Argentaffin mast cells in the thymus of the frog. 178 98

The ontogenic evolution of mast cells in the rat ventral prostate was studied using the Grimelius silver impregnation method. The mast cell density was highest during the pubertal period and later, it declined significantly with age. Most mast cells were identified in the fibrovascular stroma in close proximity to nerve fibers and blood vessels. The total number of mast cells seems to be constant when correlated with prostatic weight.
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PMID:Ontogeny of mast cells in the ventral prostate of the rat. 209 47

Peritoneal mast cells (PMC) and intestinal mucosal mast cells (IMMC) were purified from rats infected with the nematode Nippostrongylus brasiliensis. Overall protein constituents of both mast cell subtypes were analyzed by two-dimensional gel electrophoresis using either nonequilibrium pH gradient electrophoresis (NEPHGE) or isoelectric focusing (IEF) in the first dimension and SDS-PAGE (10%) in the second dimension followed by silver staining. PMC had seven dominant basic proteins (PB2-8; pI 9-9.5) with estimated molecular masses of 26 to 37 kDa, as well as 80 to 90 neutral or acidic proteins, most of which had pI 6 to 7.5 and estimated molecular masses of 20 to 100 kDa. All the basic proteins were granule-associated. Three basic proteins, PB6 (29 kDa), PB7 (28 kDa) and PB8 (RMCP I, 26 kDa), bound [3H]diisopropyl fluorophosphate (DFP), suggesting that they are serine proteases. However, only PB8 was reactive with antibodies to RMCP I. Another basic component (less than 14 kDa), perhaps a degradation product of PB6, PB7 or PB8, also bound [3H]DFP. By comparison, IMMC possessed nine basic proteins (IB1-9) and, in general, they were more acidic (pI about 8.5-9) than those of PMC. Four major basic proteins (IB6-9) were all 24 kDa but were slightly different in isoelectric points. These and another 46-kDa basic component (IB2) were reactive with antibodies to RMCP II and bound [3H]DFP. There were no other DFP-binding proteins in IMMC. In spite of remarkable differences between basic granule-associated proteins in PMC and basic proteins in IMMC, spots in the neutral-acidic range were for the most part similar in the two mast cell subsets, although quantitative differences were evident for some spots. Thus, rat mast cell populations from the peritoneal cavity and intestinal mucosa exhibit marked heterogeneity in their protein constituents with basic pI, including in their granule-associated proteins with serine protease activity.
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PMID:Mast cell heterogeneity: two-dimensional gel electrophoretic analyses of rat peritoneal and intestinal mucosal mast cells. 220

The binding protein for the K+-channel toxin dendrotoxin I was purified from a detergent extract of rat brain membranes. The purification procedure utilized chromatography on DEAE-Trisacryl, affinity chromatography on a dendrotoxin-I-Aca 22 column, and wheat germ agglutinin-Affigel 10 with a final 3800- to 4600-fold enrichment and a recovery of 8-16%. The high affinity (Kd, 40-100 pM) and specificity of the binding site are retained throughout the purification procedure. Analysis of the purified material on silver-stained NaDodSO4/polyacrylamide gel revealed three bands of Mr 76,000-80,000, 38,000, and 35,000. Interestingly, the binding site for 125I-labeled mast cell degranulating peptide, another putative K+-channel ligand from bee venom, which induces long-term potentiation in hippocampus, seems to reside on the same protein complex, as both binding sites copurify through the entire purification protocol.
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PMID:Purification and subunit structure of a putative K+-channel protein identified by its binding properties for dendrotoxin I. 245

Plasma extravasation responses to silver nitrate (AgNO3), histamine, 5-hydroxytryptamine (5-HT), bradykinin and prostaglandin E1 (PGE1) in the abdominal skin, hindpaw ankle joint and subplantar region of rats have been investigated using the Evans blue dye leakage technique. All substances tested produced plasma extravasation and combination of low doses (5 x 10(-10) mol) of either histamine or bradykinin with PGE1 (5 x 10(-10) mol) exhibited potentiation of responses of all regions. Responses to AgNO3 (1 x 10(-6) mol) were significantly reduced by the H1 receptor antagonist, mepyramine, only in the abdominal skin, but the H2 receptor antagonist metiamide reduced the responses at subplantar and ankle joint regions. Indomethacin significantly reduced the AgNO3 responses at the ankle joint only, but aprotinin reduced it at the other two regions. In rats pretreated with a combination of all antagonists the residual plasma extravasation response to AgNO3 was very small, indicating that the response could be almost totally accounted for by the combined actions of mast cell amines, kinins and prostanoids. The finding that prostanoids played a major role in the plasma extravasation response of the rat ankle joint to AgNO3 indicated that this model would be useful for the screening of non-steroidal anti-inflammatory drugs.
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PMID:Mediators of the plasma extravasation response to silver nitrate in the rat skin, subplantar region and ankle joint. 256 64

A 62-year-old male patient developed generalized argyria following the intake of silver-proteinacetyltannate (Targesin; approx. 60 g in 10 years) as treatment for gastric discomfort. On histological and ultrastructural examination of the skin, silver particles were found not only in the usual locations but also in the Schwann cell, the mast cell, and in smooth muscle cells. This corresponded to chemical analysis, proving the presence of this metal in the skin. In the blood, a level of 0.26 +/- 0.04 ppm silver was found. By means of an equation, attempts were made to demonstrate the reaction process involved in the formation of Ag2S as subjected to the photochemical effect of sunlight.
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PMID:[Argyria. A clinical, chemical analytic and micromorphologic study]. 342 29

The phosphate transport protein from beef heart mitochondria has been purified on a large scale by hydroxylapatite chromatography in the presence of sodium dodecyl sulfate and urea. As shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (silver stain), the pure phosphate transport protein preparation consists of two protein bands (alpha and beta, ratio 1:1) with similar mobilities (34 kDa) which display identical peptide maps if fragmented with either CNBr or HCl/dimethyl sulfoxide/HBr. The complete amino acid composition of phosphate transport protein is presented. Quantitative determination of N-terminal amino acids underlines the purity of the preparation and shows for alpha and beta the identical amino-terminals H2N-Ala-Val-Glu-Glu-Glx-Tyr-. Qualitative digestion shows that carboxypeptidase A is able to release at least three amino acids from the C termini of the alpha as well as the beta band of phosphate transport protein. The nature of these two protein bands is discussed. The sum of phosphate transport protein (alpha + beta) per total mitochondrial protein amounts to 2.3% or 1.4 nmol of phosphate transport protein (34 kDa) per nmol of cytochrome b.
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PMID:Mitochondrial phosphate transport. Large scale isolation and characterization of the phosphate transport protein from beef heart mitochondria. 674 42

In the intestinal mesentery of 40 white rats and 40 mongrel dogs by means of azure-eosin staining, silver impregnation, vital microscopy and certain histological methods, after left-sided cervical vagotomy it has been demonstrated that an increasing functional activity of mast cells is reached by: 1. increasing number of the mast cells; 2. increasing part of degenerating forms; 3. elevating part of the most active forms. As to the microcirculatory bed, a decreasing volume is observed at the expense of opening the arteriolo-venular anastomoses, a certain spasm of the microvessels and loosing of the capillary network. In the intervascular connective tissue, destabilization of the connective tissue elements is observed. Biomicroscopy reveals an accelerated time for the blood elements to get out of the vascular bed. The data obtained demonstrate that the postvagotomic reaction of the microcirculatory bed and its mast cell apparatus is limited with the innervation zone of the vagus nerve.
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PMID:[Microcirculatory bed and mast cells in vagotomy]. 715 12


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