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Biomedical subjects

Y Maeda

Publications and source records attributed to Y Maeda.

At least 1,009 records · Page 56Linked to original sources

1H-NMR study of the effect of synthetic polymers on the fluidity, transition temperature and fusion of dipalmitoyl phosphatidylcholine small vesicles.

The interaction of water-soluble polymers with dipalmitoyl phosphatidylcholine small vesicles and the effect on vesicle fusion were studied by means of 1H-NMR spectrometry. The motion of dipalmitoyl phosphatidylcholine molecules decreased on interaction with the polymers and was detected as a change in the signal intensity. The interaction behavior of polymers is very sensitive to the chemical structure of the applied polymers. Poly(styrene sulfonic acid) and poly(ethylene glycol) decreased the motion of the choline methyl group, predominantly through coulombic and hydrophobic interaction forces, respectively. For example, in the case of the poly(styrene sulfonic acid)-containing system, the signal intensity of the choline methyl group was decreased about 15% while those of the hydrophobic methylene and terminal methyl groups were scarcely decreased by the addition of polymer to a final concentration of 4.0 x 10(-2) unit mol/l. These polymers are considered to interact with the surface of the vesicle membrane. On the other hand, poly(L-glutamic acid) and poly(N-vinyl-2-pyrrolidone) decreased the signal intensities of not only the choline methyl group, but also those of the hydrophobic methylene and terminal methyl groups. This result suggests that part of these polymers might be incorporated into the hydrophobic region of the vesicle membrane. Addition of the non-ionic polymers inhibited vesicle fusion considerably. This effect was explained by the stabilization of dipalmitoyl phosphatidylcholine vesicles by complexation with these polymers.

Kinetics↗

Trends in heterozygosity in the process of producing inbred strains of Japanese quail.

Trends in heterozygosity in the process of producing inbred strains of Japanese quail were examined through the characterization of protein polymorphisms based on gene freqencies of 7 polymorphic loci. The average heterozygosity (Ho) at generation 1 was 0.472 and it decreased with increasing inbreeding coefficient (F) to 0.214 at generation 5 when F was 0.594. In all generations, the observed heterozygosities of the surviving families tended to be higher than those of the families that did not survive. The frequency of heterozygotes of the Es-4 locus in surviving families was higher than that of the extinct families in each generation and the difference became conspicuous in generation 4. These results suggest that a heterozygote advantage of Es-4 locus is revealed by inbreeding.

Animals↗

A modulator which converts activated estrogen receptor to a biologically inactive aggregated form.

The in vitro nuclear binding of rat uterine estrogen-receptor complexes has been studied. Heating cytosol from mature rat uterus at 25 C for various times in the presence of 0.15 M KCl resulted in a transient increase in nuclear binding activity, followed by irreversible loss of this activity. The molecular state of these complexes heated at 25 C in the presence of 0.15 M KCl was determined using Sephadex G-200 chromatography and sucrose density centrifugation at high ionic strength (0.4 M KCl). Gel filtration resulted in steroid-binding activity in the void volume. Sucrose density gradient analysis revealed a broad peak, ranging from approximately 5-20S. When cytosol was heated at 25 C in the presence of 10 mM molybdate to block the temperature-induced activation of receptor, nuclear binding ability was easily recovered by dialysis, while heating already activated estrogen receptor in the presence of 0.15 M KCl and 10 mM molybdate caused irreversible loss of nuclear binding ability. When cytosols prepared from immature rats (19-23 days old) were heated at 25 C in the presence of 0.15 M KCl, only a minimum loss of nuclear binding ability was shown. The radioactive peak in a high salt sucrose density gradient appeared almost exclusively in the 5S region. However, the addition of receptor-free mature uterine cytosol to estrogen-receptor complexes from immature rat uterus caused a marked loss of nuclear binding utility, with a resultant receptor aggregation, whereas rat liver cytosol had no effect on this reaction. Furthermore, heating liver glucocorticoid receptor did not cause a loss of nuclear binding ability even in the presence of receptor-free adult rat uterine cytosol. These observations suggest that there is a factor(s) in rat uterus which recognizes only activated estrogen receptor and induces receptor aggregation and a rapid loss of the nuclear binding ability of receptor in a KCl concentration- and temperature-dependent manner. Preliminary characterization indicates that this factor is macromolecular in nature and resistant to RNase and trypsin treatment, but labile at 100 C.

Animals↗

Prostaglandin metabolism in experimental cerebral vasospasm.

Experimental cerebral vasospasm was produced in the canine basilar artery by an intracisternal injection of fresh autogenous arterial blood, and prostaglandins generated in spastic and nonspastic arteries were assessed by thin-layer chromatography. Prostaglandins synthesized in normal arteries were 6-keto-prostaglandin (PG)F1 alpha, PGF2 alpha, PGE2, and PGD2; 6-keto-PGF1 alpha was the most abundant prostaglandin. The study of platelet aggregation suggested that prostacyclin (PGI2)-like activity was manufactured by the normal basilar artery. At 5 minutes after the intracisternal blood injection, no significant changes were evident in syntheses of prostaglandins generated by spastic artery. However, PGE2 synthesis was significantly increased in spastic artery 2 days after the intracisternal blood injection, and 6-keto-PGF1 alpha and PGF2 alpha synthesis and PGE2 synthesis were significantly decreased and increased, respectively, in spastic artery 6 days after the intracisternal blood injection. No significant changes were found in syntheses of 6-keto-PGF1 alpha, PGF2 alpha, and PGE2 manufactured by nonspastic arteries at any stage. Formation of thromboxane B2 was not detected in normal, spastic, or nonspastic arteries.

Animals↗