[Changes in plasma lipoprotein-X (LP-X) in patients with cholestasis. Mechanism of LP-X formation].
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Biomedical subjects
Publications and source records attributed to Y Muto.
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A prognostic flowmetric study on 80 reconstructed arteries of the lower extremity was carried out to assess the flow wave patterns detected using a bidirectional doppler flowmeter. In 21 of 80 arteries, changes in the flow wave pattern were noted. For 10 of 21 affected arteries, an immediate arteriography revealed localized stenotic lesions at the distal anastomosis, in a short segment of the implanted autogenous vein graft or at the proximal host artery. Immediate repairs for the lesions were successfully performed by a minor surgery in 8 of 10 cases and the flow wave pattern reverted to normal. Two were not successful as the occlusion was complete before attempting the repair. The remaining 11 are now under conservative management as these patients refused further surgery. The ultrasonically driven flow wave pattern proved to be a useful indicator to assess the patency of the reconstructed peripheral artery to detect possible stenosis and thereby to take proper corrective measures and hence prevent a late occlusion.
Femoral arterio-venous (A-V) differences of blood free amino acids and plasma ammonia (NH3) were simultaneously determined after an overnight fast in 16 patients with decompensated liver cirrhosis in the absence and presence of encephalopathy, as compared with those in 8 control subjects. In spite of increased releases of phenylalanine (Phe) and tyrosine (Tyr) from the peripheral tissue, releases of isoleucine (Ile) and leucine (Leu) as well as alanine (Ala) were found to be significantly reduced in decompensated liver cirrhosis, particularly in the presence of hepatic encephalopathy. Furthermore, NH3 was found to be significantly taken up by the skeletal muscle of these patients, and a positive correlation was observed between arterial NH3 level and the A-V differences of Leu, of Ile and of Ala. These findings strongly suggest that net degradation (or utilization) of branched-chain amino acids (in particular, Leu and Ile) is enhanced in the muscle for detoxication of ammonia (i.e., glutamine synthesis) by supplying the carbon skeleton and energy in cirrhosis of the liver.
Among the clinical isolates of Serratia marcescens, non-pigmented cells appeared more frequently from pigmented, drug-resistant strains than from pigmented, drug-sensitive strains. Transfer of R plasmid from Escherichia coli to pigmented strains caused spontaneous loss of pigment producibility, whereas such spontaneous loss never occurred in fresh cultures of drug-sensitive strains. The non-pigmented strain was a better recipient of R plasmid from E. coli than was the pigmented strain. R plasmid was transferred from the non-pigmented strain to the pigmented strain at a higher frequency than from E. coli to the pigmented strain. The results of the present investigation suggest that transfer of R plasmid may be one of the reasons for the significant increase of non-pigmented, drug-resistant strains of S. marcescens in nature.
Changes in the levels of liver cellular aetinol- and retinoic acid-binding proteins were studied after partial (about 70%) hepatectomy for 14 days in the rat. It was found that a novel binding protein designated F-type appears transiently in liver cytosol 3 days after the operation. The appearance of this protein coincides with the peak level of the alpha 1-fetoproteain. In contrast, cellular retinoic acid-binding protein was detected only the first day after hepatectomy, whereas no significant change was observed in the level of the cellular retinol-binding protein during the entire observation period. [3H]Retinol or [3H]retinoic acid complexed with serum retinol-binding protein injected intravenously into vitamin A-deficient rats 1 day after the hepatectomy was recovered 5 min or 20 min later bound specifically to cellular retinol- or retinoic acid-binding protein, respectively. The results presented here strongly suggest that each of the three cellular retinoid-binding proteins plays a distinct role in cell proliferation and differentiation.
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A study was conducted to investigate the in vitro binding affinity of new synthetic polyprenoids to cellular retinoid-binding proteins. Among 10 synthetic polyprenoic acid derivatives, 3,7,11,15-tetramethyl-2,4,6,10,14 hexadecapentaenoic acid (compound 1) was found to have the strongest binding affinity to cellular retinoic acid-binding protein (CRABP) from rat testis. As regards the chemical structure of the polyprenoic acids, it was found that suitable carbon chain length and double bond arrangement are both essential for binding affinity to CRABP. Moreover, compound I displayed a binding affinity to cellular retinoid receptors obtained from precancerous tissues such as mouse skin papillomas and rat liver hyperplastic nodules experimentally induced.
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A case of Exulceratio simplex (Es) was reported. Fair sized arteries were present in submucosal layer of fundus of the stomach from which massive arterial hemorrhage occurred due to the erosion caused by two small mucosal defects.
Two immunologically similar, probably identical, binding proteins for vitamin D and its metabolites (DBP1 and DBP2) were isolated separately from rat serum after approximately 180-fold purification by novel procedures using Blue Sepharose CL-6B chromatography. The freshly purified DBP1 and DBP2 each showed a single band of protein on polyacrylamide gel electrophoresis, and had alpha-mobility, although DBP1 moved slightly faster than DBP2. DBP1 and DBP2 had the same molecular weight, which was estimated as approximately 54,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric points of DBP1 and DBP2 were estimated as 4.9 and 5.0, respectively, from the results of isoelectric focusing experiments. DBP1 and DBP2 both appeared to have one binding site for 25-hydroxyvitamin D3 per molecule of protein, with apparently similar association constants at 4 degrees C of 5--7 x 10(9) M-1. The amino acid compositions of DBP1 and DBP2 were also determined and compared. A monospecific antiserum against rat DBP2 was prepared in a rabbit and was used for immunological studies of rat DBP. On double immunodiffusion, anti-DBP2 antiserum produced precipitin lines of complete reaction-of-identity against the purified DBP1, the purified DBP2, and rat whole serum. There was no immunological cross-reactivity between rat DBP and sera from man, dog, and rabbit, but mouse serum showed a pattern of partial identity with rat DBP. When rat serum samples were analyzed by immunoelectrophoresis using anti-DBP antiserum, three patterns of precipitin line were observed: a pattern showing the existence of only DBP1, designated as DBP 1-1; a pattern showing the existence of only DBP2, designated as DBP 2-2; and a pattern showing the existence of both DBP1 and DBP2, designated as DBP 2-1. Using single radial immunodiffusion assay for rat serum DBP, the mean (+/- S.D.) serum DBP concentrations were found to be 461 +/- 59 microgram/ml in adult male rats and 328 +/- 16 microgram/ml in adult female rats, and the difference was significant (p < 0.001). In molar terms, DBPs are present in normal rat serum in large excess relative to vitamin D and its metabolites, and most of the serum DBP, therefore, circulates as apo-DBP, not containing a bound molecule of vitamin D or of its metabolites. The immunoprecipitation studies of DBP in rat serum showed that DBPs were common main transport proteins for naturally occurring vitamin D and its metabolites, and that DBP played some, but not a principal, role in the transport of synthetic 1 alpha-hydroxyvitamin D3.
The inhibitory effects of beta-sitosterol on intestinal cholesterol absorption were studied by means of a dual isotope plasma ratio method (in vivo), which is a new technique for the measurement of cholesterol absorption, as well as a ligated-loop method (in situ). The results obtained were as follows: 1. The absorption of beta-sitosterol itself was significantly less than cholesterol. Cholesterol was selectively absorbed from rat intestine. 2. When 100 to 1,000 microgram of beta-sitosterol were added to the dose solution containing 10 microgram of cholesterol, cholesterol absorption by the in vivo experiment decreased with the increae of additional beta-sitosterol. 3. A similar inhibitory effect of beta-sitosterol was observed by the in situ ligated-loop method. These results suggest that beta-sitosterol actually inhibits cholesterol absorption in the physiological state of an animal.
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