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Biomedical subjects

S Hara

Publications and source records attributed to S Hara.

At least 577 records · Page 32Linked to original sources

[A case of bilateral testicular infarction without spermatic torsion].

A case of bilateral testicular infarction without spermatic torsion in a 39-year-old man is presented. Eighty cases of testicular infarct or necrosis, including this case, have been reviewed in the Japanese literature and the pathogenesis, clinical features, diagnosis and treatment of this disease are discussed.

Adult↗

[Total pelvic exenteration for primary and locally recurrent rectal cancer].

Thirteen patients with advanced carcinoma of the lower colon and no evidence of extrapelvic metastasis were submitted to total pelvic exenteration with urinary diversion. The operative mortality rate was 7.7%. Determinate 5-year survival rate of 40% was achieved. Local recurrence of rectal cancer following abdominoperineal resection is rarely amenable to limited resection. Six patients with deeply invading recurrent lesions had pelvic exenteration combined with sacral resection. This procedure seems a reasonable treatment for palliation and the chance of cure in selected patients. CT examination of the pelvis is very valuable for the early detection and localization of recurrence.

Adult↗

[2 cases of renal cell carcinoma on long-term hemodialysis].

Two cases of renal cell carcinoma on maintenance dialysis for chronic renal insufficiency are reported. The first case, a 40-year-old man, complained of hematuria after 9.3 years of dialysis. Nephrectomy was done and small renal cell carcinoma with acquired cystic disease of the kidney were observed. The second case, a 48-year-old man, was found to have renal cell carcinoma after 2.5 years of dialysis by means of routine examination without any symptoms. The kidney showed carcinoma with small cystic areas and four adenomas. Usefulness of routine examination with echogram is stressed for management of hemodialysis.

Adult↗

[Effects of KC-404 on bronchial anaphylactic reactions].

The effects of 3-isobutyryl-2-isopropylpyrazolo [1,5-a] pyridine (KC-404), a new anti-allergic agent with a unique mode of action, on bronchial anaphylactic reactions were investigated in guinea pigs and rats. The inhibitory effects of orally administered KC-404 on systemic anaphylactic reaction caused by intravenous antigen and on anaphylactic bronchoconstriction caused by inhaled antigen in guinea pigs actively sensitized with egg albumin were observed at doses of 100 mg/kg and 10 mg/kg, respectively. When these animals were pretreated with diphenhydramine and atropine before antigen challenge, the inhibitory effects of KC-404 were markedly enhanced; doses as low as 0.25 to 0.5 mg/kg p.o. were effective in this situation. In guinea pigs similarly sensitized as above, KC-404 injected i.v. after the maximum development of antigen-induced constriction of airways resulted in a rapid dilatation. KC-404 was about 100 times as potent as aminophylline in this respect. KC-404 inhibited passive anaphylactic bronchoconstriction in rats mediated by an IgE antibody at an oral dose of 2.5 mg/kg. The inhibitory effect of KC-404 (10 mg/kg) persisted for at least 6 hr. These results indicate that KC-404 is orally effective in inhibiting anaphylactic bronchoconstrictions mediated by IgE as well as IgG antibodies. Furthermore, KC-404 is suggested to be able to control the SRS-A-induced component of bronchospasm.

Administration, Oral↗

Concerning the use of empirical methods for determining the molecular weight of a small glycopeptide cleaved from bovine rhodopsin.

The molecular weight of a glycopeptide cleaved enzymatically from bovine rhodopsin was investigated by a variety of techniques, such as gel filtration, sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the presence and absence of urea, and gel filtration in 6 M guanidinium chloride after reduction and carboxymethylation. Great variation in the estimation of the molecular weight between the several techniques was observed. When compared to an estimate of 9000 based on amino acid analysis and considerations of its carbohydrate content, values ranging between 4500 and 18,000 were obtained by the other methods. Thus, while the molecular weight of the glycopeptide remains unresolved, the resultant ambiguity in evaluating this property may exemplify the limitations inherent in applying empirical methods to the determination of the molecular weight of small glycopeptides.

Animals↗

Characterization of lecithin:cholesterol acyltransferase from human plasma: II. Physical properties of the enzyme.

The physical properties of purified human plasma lecithin:cholesterol acyltransferase (LCAT) were investigated by techniques including analytical ultracentrifugation, ultraviolet spectroscopy, electrofocusing, and circular dichroism. The partial specific volume of LCAT was determined by sedimentation equilibrium ultracentrifugation experiments in H2O and D2O solutions (0.702 ml/g). The Mr was 67,000 by sodium dodecyl sulfate (SDS)-gel electrophoresis and 60,000 by sedimentation equilibrium ultracentrifugation. The discrepancy between the two sets of data presumably arose from the glycoprotein nature of the enzyme. Studies of the ultraviolet spectrum indicated that LCAT contained 6.5% (w/w) tyrosine which corresponds to approximately 18 tyrosine residues/mol of LCAT (polypeptide Mr 45,000). Spectrophotometric titration of the ionizable phenolic side chains indicated that nearly all the tyrosine residues were buried at neutral pH while they became gradually exposed at higher pH. The apparent pK of this transition was about 12.0 contrasted with 9.8, the apparent pK of ionization of the free tyrosyl groups.

Centrifugation, Density Gradient↗

Amino acid sequence of a heat-stable enterotoxin isolated from enterotoxigenic Escherichia coli strain 18D.

A heat-stable enterotoxin produced by a strain of enterotoxigenic Escherichia coli 18D was purified by ion-exchange and reversed-phase high-pressure liquid chromatography. The amino acid sequence of the purified toxin was determined by Edman-degradation and a combination of fast atom bombardment mass spectrometry and carboxypeptidase digestion to be Asn-Thr-Phe-Tyr-Cys-Cys-Glu-Leu-Cys-Cys-Asn-Pro-Ala-Cys-Ala-Gly-Cys-Tyr.

Amino Acid Sequence↗

Relapse of androgen-dependent tumour of mouse (Shionogi Carcinoma 115) after castration and oestrogen treatment.

To elucidate relapse of hormone-dependent tumour, mice bearing androgen-dependent carcinoma (SC 115) underwent castration or received oestrogen treatment. Since SC 115 consisted of two types of cells, androgen-sensitive round cells and -insensitive spindle-shaped cells, changes in the ratio of the cellular population were examined. After castration, spindle-shaped cells increased temporarily as the tumour regressed, then the round cells increased significantly along with an increase in size of the tumour. Oestrogen treatment did not influence the population. Androgen dependency and the growth rate of round cells were generally preserved in the next generation. Therefore, relapse may occur by an increase in the number of androgen-sensitive round cells.

Androgens↗

The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. I. Enzyme preparation, properties and kinetics: characterization of the glycopeptide product.

An enzyme system has been detected in the bovine retinal pigmented epithelium (RPE) which carries out the degradation of rhodopsin. The substrate for these studies was bovine rhodopsin labeled by in vitro techniques with [3H]-glucosamine or [3H]-mannose, the former being the derivative most extensively examined. Labeled rhodopsin was purified by adsorption and affinity chromatography followed by preparative isoelectric focusing. Cell-free preparations from bovine RPE cleaved rhodopsin to a single glycopeptide. The pH optimum for the reaction was about 3.5. The apparent Km for rhodopsin was about 5 microns. Rhodopsin was cleaved about 55% under saturating conditions, the limited extent of reaction due primarily to its partial inactivation for use as a substrate during the course of the reaction. Inhibition by cleavage products was not observed. Among several tissues which were examined, the RPE was the most active in rhodopsin-cleaving activity. Although stable as a crude extract, the activity of the rhodopsin-cleaving enzyme, as well as the bovine serum albumin (BSA)-cleaving enzyme (cathepsin-D) were rapidly lost upon purification by DEAE-Sephacel and pepstatin-Sepharose. Differences in relative specific activity among tissues as well as differential patterns of purification suggest that the rhodopsin-cleaving enzyme and the BSA-cleaving enzyme of the RPE may not be the same. Using N-retinylopsin as a substrate for the rhodopsin-cleaving enzyme, it was shown that the regions of the cleavage products containing vitamin A were not associated with the glycopeptide. Some of the properties of the product were examined. Its response to ion exchange resins, susceptibility to further cleavage by pronase, amino acid analysis, solubility properties, isoelectric point, and binding by concanavalin A (conA)-Sepharose, were consistent with the product being described as an acidic glycopeptide. The glycopeptide was reactive with the antibody prepared against bovine rhodopsin, and retained the full antigenicity of the intact molecule. This enzyme system may be one of the means whereby the RPE participates in maintaining the physiological concentration of rhodopsin which is synthesized in the retina and catabolized in the RPE.

Amino Acids↗

The enzymatic cleavage of rhodopsin by the retinal pigment epithelium. II. The carbohydrate composition of the glycopeptide cleavage product.

The carbohydrate groups present in the glycopeptide cleaved from purified [3H]-GlcNAc-rhodopsin by an enzyme from the retinal pigment epithelium were analyzed in terms of the size of the oligosaccharide chains, the sequence of the sugars and their anomeric linkages. These analyses were performed also on intact rhodopsin and an enzyme control. The oligosaccharides were cleaved from the peptide by means of hydrazinolysis. After reduction with NaB3H4, the oligosaccharides, purified by paper electrophoretic and paper chromatographic means, were digested sequentially with exoglycosidases, and the resultant digestion products examined by high-resolution gel filtration on Bio-Gel P-4 (-400). The size, sequence and anomeric configuration of the constituents of the oligosaccharides present in the glycopeptide were essentially identical to those present in intact purified rhodopsin, indicating the retention by the glycopeptide of the sugar chains of the intact molecule.

Animals↗

The value of transrectal ultrasonography in preoperative assessment for transurethral prostatectomy.

Transrectal ultrasonography was done in 19 healthy men and 236 patients with benign prostatic hyperplasia to elucidate the pathomorphology of the prostate and to determine preoperative prostatic size in patients who underwent transurethral prostatectomy. We found that the ultrasonographic examination allowed for an accurate estimation of the prostatic weight and a good assessment of the completeness of resection of the prostatic adenoma.

Humans↗

Amino acid sequences of two trypsin inhibitors from winged bean seeds (Psophocarpus tetragonolobus (L)DC.).

The trypsin inhibitor (WTI-1) purified from winged bean seeds is a Kunitz type protease inhibitor having a molecular weight of 19,200. WTI-1 inhibits bovine trypsin stoichiometrically, but not bovine alpha-chymotrypsin. The approximate Ki value for the trypsin-inhibitor complex is 2.5 X 10(-9) M. The complete amino acid sequence of WTI-1 was determined by conventional methods. Comparison of the sequence with that of soybean trypsin inhibitor (STI) indicated that the sequence of WTI-1 had 50% homology with that of STI. WTI-1 was separated into 2 homologous inhibitors, WTI-1A and WTI-1B, by isoelectric focusing. The isoelectric points of WTI-1A and WTI-1B were 8.5 and 9.4, respectively, and their sequences were presumed from their amino acid compositions.

Amino Acid Sequence↗

Characterization of lecithin-cholesterol acyltransferase from human plasma. 3. Chemical properties of the enzyme.

The polypeptide molecular weight of lecithin-cholesterol acyltransferase (LCAT) (45000) was obtained by deducting the weight of carbohydrate moiety (25%, w/w) from the total molecular weight of 60000. LCAT was found to have a relatively high content of glutamic acid, aspartic acid, glycine, and leucine residues and four half-cystines. The carbohydrate content was found to be about 25% (w/w): hexoses, 13%; hexosamines, 6.2%; and sialic acid, 5.4%. The total number of 408 amino acid residues per mole and the mean residue weight of 110.3 were found. From fluorescence spectroscopy analysis, 6-7 mol of tryptophan were found per mole of LCAT in 10 mM phosphate (pH 7.4). However, when LCAT was digested by the mixture of chymotrypsin and pronase the tryptophan residues increased to 10-11 mol/mol of LCAT, which agrees well with data obtained previously by ultraviolet absorption spectroscopy. A partial specific volume of 0.707 mL/g was determined by compositional analysis. Human LCAT was found to have a relatively high extinction coefficient (E1%1cm) of 21 at 280 nm and neutral pH. Two residues of cysteine per mole of LCAT were estimated both in the presence or absence of sodium dodecyl sulfate by titration with 5,5'-dithiobis-2-nitrobenzoic acid. The enzyme showed a lower tendency to staining with Coomassie blue R-250 than bovine serum albumin. The enzyme was rapidly inactivated by diisopropyl fluorophosphate (DFP), regardless of whether the free sulfhydryl were blocked or not. The enzyme was also irreversibly inhibited by cysteine above concentrations of 1 mM.(ABSTRACT TRUNCATED AT 250 WORDS)

Amino Acids↗