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Biomedical subjects

S Shirahama

Publications and source records attributed to S Shirahama.

15 recordsLinked to original sources
PubMed1992

[The prevalence of diabetes mellitus and impaired glucose tolerance studied by 75 gram oral glucose tolerance test in a rural island population].

A mass health examination was performed to assess the glucose tolerance of inhabitants of the island of Ojika, in the Goto islands, Nagasaki prefecture Japan. There were 554 males and 820 females older than 34 years who participated in the mass health examination, a response rates of 42 percent and 52 percent for males and females respectively. Serum glucose levels after overnight fasting and at 2 hours after a 75 gram oral glucose tolerance were used with WHO criteria to classify individuals. Among these subjects, the prevalence of diabetes mellitus increased with age, with a prevalence of diabetes mellitus of around 10 percent in the older subjects. The prevalence for males was higher than that for females. Prevalences of impaired glucose tolerance were roughly in the 15-25 percent range and did not show clear differences among different age groups and sexes. From a questionnaire survey of all island inhabitants, it was considered that the degree of bias of the results was small, if any. The true prevalence for all the inhabitants may be a little larger than the observed prevalence of these subjects.

Adult↗
PubMed1991

Epidemic patterns of hepatitis type B virus (HBV) and human T lymphotropic virus type I (HTLV-I) in two ATL-endemic islands in Kyushu, Japan.

To evaluate the relationships between human T lymphotropic virus type I (HTLV-I) and hepatitis virus type B (HBV) infections, we compared both individual and geographical distributions of carriers of HTLV-I and HBV, and antibody positives to HBV in two ATL-endemic islands in Kyushu, Japan. The positive rates of antibodies to HTLV-I (anti-HTLV-I-Ab) in sera among healthy inhabitants older than 30 years of age were 27.5% (617/2,232) in Nakadohri, Goto Island and 24.0% (500/2,048) in Shimo-agata, Tsushima Island. The positive rates for surface antigen of hepatitis B virus (HBs-Ag) in sera among the same subjects were 6.4% and 2.5%, respectively. In Nakadohri, the age-adjusted positive rates of HBs-Ag and antibody to HBs-Ag (anti-HBs-Ab) in anti-HTLV-I-Ab positives (so-called HTLV-I carriers) differed little from those in negatives. In Shimo-agata, the geographical distribution of HBs-Ag positives (so-called HBV carriers) showed no positive association with that of HTLV-I carriers. These results did not support the positive correlations between HTLV-I and HBV infections among the general population in ATL-endemic areas in Japan.

Adult↗
PubMed1989

[The epidemiological study of hepatolithiasis in the Kamigoto district, Nagasaki where hepatolithiasis is high incidence].

Regional distribution, age, sex, type of disease and history of surgery of the biliary tract were examined in 134 patients with hepatolithiasis in the Kamigoto district. The ratio of patient to population was 1:126 in the region showing the highest incidence. When classified by age at establishment of the diagnosis, patient in their sixties comprised the largest portion in both sexes. The ratio of men to women was 1:1.2. When classified in accordance with the draft by Research Group for the Study of Hepatolithiasis, 103 cases (76.9%) were of the intrahepatic type, and 31 cases (23.1%) were of the intra-extrahepatic type. The stones were found in the right lobe in 58 patients (43.3%), the left lobe in 59 patients (44.0%) and the both lobes in 17 patients (12.7%). Forty-four patients (32.8%) had a history of surgery of the biliary tract. Ultrasonographic examination of the abdomen in junior high school students revealed hepatolithiasis in one. As a result, the intrahepatic type and the right lobe type are high frequency in this district, and epidemiological survey of the family history and the food habit in this district is necessary.

Adolescent↗
PubMed1987

Effects of lysine and glutamic acid or [corrected] Mg++ on the conformations of C3 and B, and the activation of the alternative complement pathway.

The conversion of C3 and B in the mixture of C3, B, D and Mg++ ions was inhibited in the presence of arginine and lysine, but not in the presence of glutamic acid and aspartic acid among other amino acids. Application of dialyzed plasma to a lysine-Sepharose column resulted in elution of B and a part of D in pass-through fractions, and C3 and the other part of D were retained in the column, subsequently eluted by increase in salt concentrations. C3, B and a part of D were eluted in pass-through fractions, and C3 and the other part of D were retained in the column, subsequently eluted by increase in salt concentrations. C3, B and a part of D were eluted in pass-through fractions when applied to glutamic acid-Sepharose. A highly purified D preparation appeared in the pass-through fraction of the lysine-Sepharose column, suggesting that D may form a complex in plasma. The intensity of intrinsic fluorescence of C3 decreased in the presence of arginine to the largest extent. Lysine affected the intensity less than arginine. Kd was calculated to be 0.42 mM for arginine and 0.55 mM for lysine in the interaction with C3. The intensity of intrinsic fluorescence of B decreased in the presence of aspartic acid and glutamic acid (Kd = 0.48 mM for aspartic acid and 0.24 mM for glutamic acid). Arginine or lysine affected the intensity of B less than those anionic amino acids. The presence of Mg++ ions resulted in a decrease in the fluorescence intensity of C3 and B.(ABSTRACT TRUNCATED AT 250 WORDS)

Binding Sites↗
PubMed1986

Inhibition by lysine and arginine of the conversion of C3 and B in the serum and a purified system.

When human serum was incubated at 45 degrees C for 30 min, C3 and B were converted to C3b and Bb. Molecular weights of purified C3 and B were shown not to change after incubation at 50 degrees C. Spectropolarimetry indicated that the secondary structures of C3 and B changed after incubation at higher temperature. The titration of SH groups in the C3 molecule showed the liberation of an SH group. These results show that the alternative complement pathway is activated at raised temperatures without known activators such as zymosan or lipopolysaccharide (LPS). This may be due to the accelerated interaction of conformationally changed components of the alternative pathway such as C3 and B. Using this system, effects of various substances on the interaction of C3 and B in serum and the purified system were investigated. The addition of arginine and lysine resulted in the inhibition of the conversion of C3 and B in the serum at elevated temperature. Other amino acids such as anionic amino-acids and NaCl did not influence the conversion. In the purified system, only arginine and lysine prevented the conversion of C3 and B, when C3, B and D were incubated in the presence of Mg++ and amino-acids. Since lysine and arginine did not inhibit the enzymatic activity of D, these data suggest that arginine and lysine prevent the interaction of C3 and B in the serum at elevated temperatures.

Animals↗
PubMed1985

Inhibition by various peptides of the activation of C1, the first component of complement, and the interaction of C gamma 2 domain of IgG with C1q.

Three groups of peptides were synthesized, each of which was proposed to be a part of the C1q binding sites of the C gamma 2 domain of IgG. They were: Trp(277)-Tyr-Val-Asp-Gly (WYVDG), Thr(289)-Lys-Pro-Arg (tuftsin) and Gly(316)-Lys-Glu-Tyr-Lys (GKEYK) or portions of these peptides. Assays included CH50, consumption of serum complement induced by heat-aggregated IgG, C1 hemolysis and an enzyme immunoassay that directly measures interaction between C1q and IgG. Peptides near Gly(316) such as GKEY, GKE or EYK inhibited CH50 and heat-aggregated IgG-induced consumption of serum complement. WYVDG also inhibited CH50, with 50% inhibition at 2.05 mM, which was more than the concentrations of peptides near Gly(316) at 50% inhibition. Tuftsin was only slightly inhibitory in both systems. Results of C1 hemolysis indicated that dipeptides composed of two aromatic amino acids, especially Trp-Tyr, were more inhibitory than dipeptides of which one residue was an aromatic amino acid. Peptides such as EYK, GKEY or GKE were very inhibitory, and tuftsin was far less inhibitory than these peptides in C1 hemolysis. Results of enzyme immunoassay also showed that dipeptides composed of two aromatic amino acids were more inhibitory than dipeptides of which one residue was aromatic amino acid. WYVDG was most inhibitory in enzyme immunoassay, but tuftsin, EYK, GKEY GKE and KE were less effective.

Binding Sites↗
PubMed1985

Conformational changes of complement components C3 and B induced at higher temperature.

When purified C3 or B of human complement was incubated at various temperatures for 30 min, B lost most of its antibody combining capability at 46 degrees C, and C3 lost it at higher than 50 degrees C. When C3, heated B, D and Mg++ ions were incubated, there was a precipitous decrease in C3 conversion in the presence of heated B between 44 and 46 degrees C. No C3 conversion was observed in the presence of B heated at 50 degrees C. When C3 heated higher than 50 degrees C was incubated with B, D and Mg++ ions, C3 conversion decreased dramatically, but B was converted almost normally, suggesting that B could be complexed with heated and conformationally altered C3 and cleaved by D. The fluorescence intensity of heated C3 excited at 288 nm gradually decreased between 44 and 46 degrees C. The fluorescence 288 nm gradually decreased between 44 and 46 degrees C. The fluorescence intensity of C3 was slightly increased by 1-anilino-8-naphthalene sulfonate (ANS) at 50 degrees C and significantly increased at 56 degrees C, while ANS enhancement of fluorescence of B began at 46 degrees C and was significant at 50 degrees C, indicating that the surface of B and C3 became hydrophobic between 44 and 46 degrees C, and 46 and 50 degrees C, respectively. These results suggest that conformations of C3 and B have low melting points at which they change confirmations drastically.

Anilino Naphthalenesulfonates↗
PubMed1985

Enzyme immunoassay of C1q and its application to the detection of C1q antigens in urine.

A highly sensitive enzyme immunoassay for the determination of C1q, a subcomponent of the first component of complement, C1, was developed to determine C1q in body fluid. Anti-C1q F(ab')2 fragments were immobilized on silicone rubber and after the interaction of anti-C1q with C1q, Fab' fragments of anti-C1q coupled with beta-D-galactosidase were added. The amounts of C1q were measured by enzymatic activity of beta-D-galactosidase to cleave 4-methylumbelliferyl-D-galactoside. A calibration curve of C1q indicates that C1q could be determined in the range of 0.3 ng/ml-1 mg/ml, the optimal range being 1-100 ng/ml. While C1q was not detectable in the urine of healthy volunteers, C1q could be determined in the urine of patients with renal diseases. The highest level of C1q detected was 31.8 ng/ml in urine of chronic nephritis.

Complement Activating Enzymes↗
PubMed1979

IgM anti-IgM cold lymphocytotoxins to B cells.

Cytotoxic antibodies to B lymphocytes have been shown to be IgM. They are not absorbed by red blood cells and therefore not absorbed by red blood cells and therefore not directed against the I antigen of red cells. They are also not inhibited by mannose, as are certain natural cytotoxins against lymphocytes. Methods for producing purified eluates of IgM anti-IgM antibodies are given. These antibodies are postulated to be immunoregulative by acting on B lymphocytes.

Absorption↗
PubMed1979

A simple, rapid micro-latex fixation test.

A micro-latex fixation test (LFT) for the determination of rheumatoid factor (RF) is presented. Its advantages compared to similar tests are greater precision, simplicity, increased sensitivity, lower cost, reproducibility and adaptibility to large-scale testing. Micro-LFT titres are presented from a wide range of sample populations. The majority of normal samples show measureable titres whereas rheumatoid patients show high titres. A large sampling of pre- and post-transplant sera from kidney patients was studied and the micro-LFT titres were in the range of normal persons. The transplant sera were tested for lymphocytotoxic antibodies and no correlation was observed with the micro-LFT titres.

Adult↗