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Biomedical subjects

M Mio

Publications and source records attributed to M Mio.

64 records · Page 4Linked to original sources
PubMed1985

Inhibitory effect of lysophosphatidylcholine on the histamine release from rat peritoneal mast cells.

Histamine release from isolated rat peritoneal mast cells induced by compound 48/80 (0.5 microgram/ml) or antigen-antibody reaction was inhibited by lysophosphatidylcholine in a dose-dependent fashion at concentrations up to 4 microM. Within the same range of concentration, lysophosphatidylcholine exhibited a membrane-stabilizing action on the model membrane systems decreasing the permeability of lipid bilayer and the fluidity of liposomal membrane in the liquid crystalline state. At concentrations higher than 8 microM, lysophosphatidylcholine damaged the cell membrane and subsequently histamine was released. It was assumed that lysophosphatidylcholine may act as an endogenous membrane stabilizer inhibiting histamine release in normal mast cells.

Animals↗
PubMed1984

Permeability increase in black lipid membrane induced by compound 48/80.

When compound 48/80, a potent histamine liberator, was added in the aqueous phase facing the black lipid membrane, the conductivity of the membrane was remarkably increased. Although valinomycin displayed a distinct selectivity for K+ movement, such selection for ionic permeability was not observed in the case of compound 48/80.

Animals↗
PubMed1984

Effect of N-methylation of phosphatidylethanolamine on the fluidity of phospholipid bilayers.

The effect of N-methylphosphatidylethanolamine on phase transition and the fluidity of the liposomes made of dipalmitoylphosphatidylcholine or phosphatidylethanolamine was studied by the steady-state fluorescence polarization method and differential scanning calorimetry. N-methylation of phosphatidylethanolamine caused a decrease of fluidity of liposomes made of dipalmitoylphosphatidylcholine, but had little effect on dipalmitoylphosphatidylethanolamine. The liposomes prepared with both phosphatidylcholine and N-methylphosphatidylethanolamine and also phosphatidylethanolamine and N-methylphosphatidylethanolamine could be composed of solid solution and exhibited symmetric phase diagram.

Animals↗
PubMed1983

Analgesic activity of certain tripeptide-beta-phenethylamide analogs.

Studies of the analgesic effect of tripeptide-beta-phenethylamides are described, and their structure-activity relationship is discussed. SD-25, which has a methyl group at R2, and a hydroxymethyl group at R3 of beta-phenethylamide, was the most potent one of the 8 analogs tested.

Analgesia↗
PubMed1983

Histamine release inhibition and prevention of the decrease in membrane fluidity induced by certain anti-allergic drugs: analysis of the inhibitory mechanism of NCO-650.

NCO-650 exerted a dose-dependent inhibition of histamine release from isolated rat mast cells without affecting the Ca-uptake and intracellular cAMP levels. When the membrane stabilizing action of NCO-650 was investigated with the liposomes prepared by various phospholipids with or without cholesterol, it became clear that compound 48/80 decreases the order parameter of liposomes and NCO-650 inhibits the decrease of order parameter. Histamine release from histamine-containing liposomes was brought about by compound 48/80 at concentrations higher than 0.5 micrograms/ml, and pretreatment of the liposomes with NCO-650 inhibited histamine release due to compound 48/80. The incorporation of NCO-650 in the liposomes was effective in abolishing the phase transition of the lipid bilayer membranes from crystalline gel to liquid crystalline phases, and decreased the phase transition temperature. Those changes in the lipid bilayer membranes correspond to those displayed by incorporation of cholesterol in the liposomes. An increase of permeability of lipid membrane by compound 48/80 may be due to partial loosening of the lipid order; NCO-650 rigidified the liposome membrane and as a result of this, it decreased histamine release.

Animals↗
PubMedDate not supplied

Role of microtubules on Ca2+ release from the endoplasmic reticulum and associated histamine release from rat peritoneal mast cells.

In order to study the role of cytoskeletons on histamine release from mast cells, the effects of cytoskeleton-inhibiting agents were investigated. Since neither colchicine, vinblastine nor cytochalasin D was effective in inhibiting the IP3 formation, it is possible that neither microtubules nor microfilaments of rat peritoneal mast cells participate in the initial membrane events of the histamine release. However, both colchicine and vinblastine, but not cytochalasin D, were effective in inhibiting Ca2+ release from the intracellular Ca store. It was accordingly suggested that the microtubules, rather than microfilaments, are intimately related to the Ca2+ releasing process from the endoplasmic reticulum. The fluorescence intensity of the mast cells stained with FITC-labeled anti-tubulin antibody reflects the amount of tubulin polymers inside the cell, and colchicine treatment decreased the fluorescence intensity, indicating that colchicine is effective in depolymerizing the microtubules of rat mast cells. By contrast, the amount of tubulin polymer in the mast cells increased by compound 48/80, indicating that the rearrangement of microtubules took place in the mast cells, leading to histamine release. When permeabilized mast cells were exposed to potassium antimonate solution, microtubules attached themselves to the endoplasmic reticulum and many Ca antimonate dots were observed. From the present results, it was concluded that microtubules play an important role in the processes leading to Ca2+ release from the intracellular Ca store and subsequent histamine release.

Animals↗
PubMedDate not supplied

Ca uptake and Ca releasing properties of the endoplasmic reticulum in rat peritoneal mast cells.

In order to study the characteristics of the intracellular Ca store of mast cells, organelles of rat peritoneal mast cells were fractionated. The binding of 45Ca was at its peak in the fractions where the highest activity of glucose-6-phosphatase, the marker enzyme for the endoplasmic reticulum (ER), was measured. The ER-rich fraction exhibited an ATP-dependent uptake of 45Ca and this uptake was inhibited by pretreatment with ATPase inhibitors such as LaCl3 or Na3VO4. When inositol 1,4,5-trisphosphate (IP3) was added to a medium containing the 45Ca-loaded ER fraction, it caused a dose-dependent release of 45Ca at concentrations higher than 0.5 microM, while inositol 1-monophosphate and inositol 1,4-bisphosphate were not effective even at higher concentrations. The results of a binding assay using 3H-labeled IP3 indicated that there exist two kinds of IP3 binding site in the ER: one is of high affinity but low capacity while the other is of low affinity and high capacity. IP3-induced 45Ca release was dose-dependently inhibited by pretreatment with c-AMP. The present study supports the assumption that the intracellular Ca store associated with histamine release from the mast cell is the ER.

Adenosine Triphosphate↗
PubMedDate not supplied

Role of endoplasmic reticulum, an intracellular Ca2+ store, in histamine release from rat peritoneal mast cell.

By means of the Ca-antimonate precipitation technique, it was revealed that Ca2+ accumulates in the endoplasmic reticulum (ER) of rat peritoneal mast cells. The ER of rat mast cells was isolated using Percoll density gradient centrifugation, and its characteristics were studied. Although the uptake of 45Ca into the ER was enhanced by adenosine 5'-triphosphate (ATP) at concentrations lower than 2 mM, at higher concentrations ATP induced 45Ca release from the ER, suggesting that bidirectional translocation of Ca2+ takes place in the ER membrane. When apyrase was added to the reaction mixture to decompose all ATP molecules, the amount of 45Ca in the ER was decreased, indicating that ATP is necessary to retain Ca2+ in the ER. Not only inositol 1,4,5-trisphosphate (IP3) but also guanosine 5'-triphosphate (GTP) was effective in releasing Ca2+ from the ER at concentrations higher than 2 microM, while guanosine 5'-[gamma-thio]-triphosphate (GTP-gamma S), a non-hydrolysable analogue of GTP, was not effective. This may indicate that a hydrolysis of GTP is necessary for Ca2+ release from the ER. Intracellular Ca2+ blockers such as 8-(N,N-diethylamino)octyl-3,4,5-trimethoxybenzoate (TMB-8) and dantrolene sodium were effective in inhibiting Ca2+ release from ER induced by IP3. The Ca2+ release due to IP3 was also inhibited by flunarizine, a Ca2+ channel blocker, and by oxatomide, an antiallergic drug. Since these two compounds are diphenylpiperazine derivatives, it is suggested that a diphenylpiperazine moiety may be effective in inhibiting Ca2+ release from the ER.

Adenosine Triphosphate↗
PubMedDate not supplied

Substance P-induced histamine release from rat peritoneal mast cells and its inhibition by antiallergic agents and calmodulin inhibitors.

Substance P-induced histamine release and Ca2+ release from the intracellular Ca store of rat peritoneal mast cells were inhibited by both antiallergic drugs and microtubule inhibiting agents. It was found that in the case of antiallergic compounds, histamine release inhibition may be intimately related to the inhibition of Ca2+ release from the intracellular store in which the microtubules play an important role. When mast cells were pretreated with either theophylline or dibutyryl cAMP, the inhibition of histamine release was closely related to the inhibition of Ca2+ release from the intracellular Ca store. Calmodulin inhibitors were also effective in inhibiting histamine release from mast cells induced by substance P. The inhibitory potencies of calmodulin inhibitors on histamine release from mast cells were closely correlated with those exerted on calmodulin activity.

Animals↗