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T Ikuta

Publications and source records attributed to T Ikuta.

At least 73 records · Page 4Linked to original sources
PubMed1989

[Statistical analysis of new out-patients in the Department of Medicine, Fukuoka Dental College Hospital. 10: From January 1 to December 31, 1987].

To clarify the common diseases of new out-patients, a retrospective study was made in 1.523 out-patients, who visited our department from January 1 to December 31, 1987. Of 1,523 out-patients, 3,513 diseases were diagnosed in 1,350 patients and the others were normal subjects who visited the department for obtaining health certificates. Of these 3,513 diseases, 1,220 (34.7%) were respiratory diseases including upper respiratory infections, 471 (13.4%) were gastrointestinal diseases, 396 (11.3%) were renal and urinary tract diseases, 371 (10.6%) were liver and biliary tract diseases including pancreas diseases, 354 (10.1%) were cardiovascular diseases, 257 (7.3%) were allergic, muscle, bone and connective tissue diseases, 206 (5.9%) were neurologic diseases, 153 (4.4%) were metabolic diseases, 46 (1.3%) were endocrine diseases and 39 (1.1%) were hematologic diseases. Of these 1,523 out-patients 20 (1.5%) patients were positive for HBs antigen.

Adolescent↗
PubMed1988

Direct determination of usual (Caucasian-type) and atypical (Oriental-type) alleles of the class I human alcohol dehydrogenase-2 locus.

Two types of alleles exist in the human alcohol dehydrogenase-2 (ADH2) locus. The usual ADH12 allele is common in Caucasians, while the atypical ADH22 allele is predominant in Orientals. The ADH22 produces the beta 2 subunit, which is catalytically far more active than the beta 1 subunit produced by the ADH12 gene. The racial difference in alcohol-related problems could be related to the genetic differences in ADH and other ethanol-metabolizing enzymes. In order to examine the possibility, a method for determining ADH2 genotypes was developed. Two 21-base synthetic oligonucleotides, one complementary to the usual ADH12 allele and the other complementary to the atypical ADH22 allele, were used as specific probes for in-gel hybridization analysis of human genomic DNA from peripheral blood. Under appropriate hybridization conditions, these two probes can hybridize to their specific complementary alleles and, thus, allow the genotyping of the ADH2 locus. Genotypes of the ADH2 locus of 49 unrelated Japanese individuals were determined. The frequency of the atypical ADH22 gene was found to be 0.71 in the Japanese population examined.

Alcohol Dehydrogenase↗
PubMed1986

mRNA for the three human alcohol dehydrogenase subunits: size heterogeneity and developmental changes.

Human alcohol dehydrogenase consists of three types of subunits (alpha, beta, and gamma) which are governed by three separate loci. mRNA components for the three subunits were examined by Northern blot hybridization, using a common cDNA probe and specific oligonucleotide probes. A marked size heterogeneity of beta mRNA, ranging from 1.6 kb to 5.2 kb (of which the 2.4-kb and 3.5-kb were major), was observed in the adult liver. The mRNA for the gamma subunit was homogeneous (about 1.6 kb), and that for the alpha subunit contained a major 1.6-kb and a minor 4.3-kb component. The amount of mRNA was much lower (approximately 10% of adult) and the mRNA was less heterogeneous in the infant liver; i.e., an alpha mRNA (1.6 kb) and two beta mRNAs (a major 1.6 kb and a minor 3.5 kb), and no detectable gamma mRNA. The short beta mRNA, with 1.6 kb, could not be hybridized with a non-coding cDNA fragment that originated from the 3'-end of the 2.6 kb beta cDNA. The observed multiple ADH mRNAs, with a common coding region and different 3'-untranslated regions, are generated by utilization of multiple polyadenylation signals. The selection of polyadenylation signals and the rate of transcription of the three ADH loci are developmentally regulated. The 4.3-kb-long mRNA, which was hybridized with both a- and beta-specific probes, could be related to the previously cloned "fused beta-alpha" cDNA.

Adult↗
PubMed1986

Human lymphocytes synthesize C-reactive protein.

We obtained evidence for the synthesis and secretion of C-reactive protein (CRP) by peripheral mononuclear cells in culture. Human mononuclear cells isolated from peripheral blood, after depletion of platelets, were cultured in glutamine-depleted RPMI 1640 supplemented with [3H]glutamine in the presence of 10-O-tetradecanoyl-phorbol-13-acetate (TPA). Anti-CRP antiserum was added to the culture medium, and the resultant immunoprecipitate was analyzed in SDS-polyacrylamide gel electrophoresis (SDS-PAGE). The immunoprecipitate consisted of CRP, heavy and light chains of IgG, and only the CRP protein band had radioactivity, indicating that CRP was synthesized by mononuclear cells. In the populations of mononuclear cells, T-cell preparations mainly synthesized CRP, under stimulation of a factor derived from activated monocytes. Studies using the inhibitors of phospholipid metabolism suggested that generation of the monocyte factor was relevant to metabolites of an arachidonate cascade.

B-Lymphocytes↗
PubMed1986

Human glucose-6-phosphate dehydrogenase: primary structure and cDNA cloning.

The X-chromosome-linked glucose-6-phosphate dehydrogenase (D-glucose-6-phosphate:NADP+ oxidoreductase, EC 1.1.1.49) of humans and other mammals consists of a subunit with a molecular weight of about 58,000. The enzyme plays a key role in the generation of NADPH, particularly in matured erythrocytes, and the genetic deficiency of the enzyme is associated with chronic and drug- or food-induced hemolytic anemia in humans. The enzyme was purified to homogeneity from human erythrocytes. The complete amino acid sequence of the subunit, consisting of 531 amino acid residues, was determined by automated and manual Edman degradation of tryptic, chymotryptic, thermolytic, and cyanogen bromide peptides obtained from the enzyme. Based on the amino acid sequence data thus obtained, a 41-mer oligonucleotide with unique sequence was prepared. Two cDNA libraries constructed in phage lambda gt11--i.e., a human liver cDNA library and a human hepatoma Li-7 cDNA library--were screened with the synthetic nucleotide probe. Two positive clones, lambda G6PD-19 and lambda G6PD-25, were obtained from the hepatoma library. lambda G6PD-19 contained an insertion of 2.0 kilobase pairs (kbp), and encoded 204 amino acid residues that were completely compatible with the COOH-terminal portion of the enzyme. The insertion of the clone had a 3' noncoding region of 1.36 kbp. The other clone, lambda G6PD-25, had an insertion of 1.8 kbp and encoded 362 amino acid residues of G6PD. Southern blot analysis of DNA samples obtained from cells with and without the human X chromosome indicated that the cDNA hybridizes with a sequence in the X chromosome.

Amino Acid Sequence↗
PubMed1986

Three human alcohol dehydrogenase subunits: cDNA structure and molecular and evolutionary divergence.

Class I human alcohol dehydrogenase (ADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1) consists of several homo- and heterodimers of alpha, beta, and gamma subunits that are governed by the ADH1, ADH2, and ADH3 loci. We previously cloned a full length of cDNA for the beta subunit, and the complete sequence of 374 amino acid residues was established. cDNAs for the alpha and gamma subunits were cloned and characterized. A human liver cDNA library, constructed in phage lambda gt11, was screened by using a synthetic oligonucleotide probe that was matched to the gamma but not to the beta sequence. Clone pUCADH gamma 21 and clone pUCADH alpha 15L differed from beta cDNA with respect to restriction sites and hybridization with the nucleotide probe. Clone pUCADH gamma 21 contained an insertion of 1.5 kilobase pairs (kbp) and encodes 374 amino acid residues compatible with the reported amino acid sequence of the gamma subunit. Clone pUCADH alpha 15L contained an insertion of 2.4 kbp and included nucleotide sequences that encode 374 amino acid residues for another subunit, the alpha subunit. In addition, this clone contained the sequences that encode the COOH-terminal part of the beta subunit at its extended 5' region. The amino acid sequences and coding regions of the cDNAs of the three subunits are very similar (approximately 93-95% identity). A high degree of resemblance is observed also in their 3' noncoding regions. However, distinctive differences exist in the vicinity of the Zn-binding cysteine residue at position 46--i.e., Cys-Gly-Thr in the alpha, Cys-Arg-Thr in the wild-type beta 1, Cys-His-Thr in the Oriental-type beta 2, and Cys-Arg-Ser in the gamma, reflecting the differences in their kinetic properties. Based on the cDNA sequences and the deduced amino acid sequences of the three subunits, their structural and evolutionary relationships are discussed.

Alcohol Dehydrogenase↗
PubMed1985

Influence of acute-phase proteins on the activity of natural killer cells.

The effects of alpha 1-antitrypsin (alpha 1-AT), alpha 1-acid glycoprotein (alpha 1-AGP), and haptoglobin (Hp), the main constituents of alpha-globulin and which belong to acute-phase proteins, on NK activity were examined using K562 cells as the NK target cells. Among the three proteins, alpha 1-AT and alpha 1-AGP had inhibitory effects on NK activity for "fast target" K562 cells. The alpha 1-AT preparations having the same protein concentration and a different trypsin inhibitory capacity (TIC) had an equal effect. Although alpha 1-AT and alpha 1-AGP equally reduced the NK activity, the mechanism involved in the reduction differed, in that the effect of alpha 1-AT directed toward NK cells reduced their binding capacity with the target cells. alpha 1-AGP probably interacts with a cytotoxic factor secreted from NK cells following effector-target interaction. These studies suggest that each of the acute-phase proteins, which increase following inflammation, inhibits NK cell function by two distinct mechanisms.

Albumins↗
PubMed1985

Molecular cloning of a full-length cDNA for human alcohol dehydrogenase.

We have cloned a full-length cDNA coding for human alcohol dehydrogenase (ADH; alcohol:NAD+ oxidoreductase, EC 1.1.1.1) from a human liver cDNA library constructed in phage lambda gt11. The library was screened by using a rabbit antibody against human ADH as a first probe, by the modified method of Young and Davis [Young, R. A. & Davis, R. W. (1983) Proc. Natl. Acad. Sci. USA 80, 1194-1198]. Mixed 14-mer synthetic oligonucleotides encoding Asp-Asp-His-Val-Val and Gln-Cys-Gly-Lys-Cys were used as a second probe. These amino acid sequences are considered to be common in all three subunits (alpha, beta, and gamma) controlled by the ADH1, ADH2, and ADH3 loci. Ten lambda gt11 recombinants of 35 positive plaques obtained by antibody screening contained inserted cDNAs of 1.5-2.4 kilobase pairs and were found to exhibit positive signals by hybridization with synthetic probes. One of them, with an inserted cDNA of 1631 base pairs, contained a sequence that encodes 374 amino acid residues of the human beta 1 subunit, a chain initiation codon, a chain termination codon, and additional 3' and 5' untranslated regions. A complete amino acid sequence of the human beta 1 subunit was deduced from the cDNA.

Alcohol Dehydrogenase↗
PubMed1985

Evaluation of a new bronchodilator, Formoterol, using biochemical parameters.

The authors administered orally 40, 60 and 80 micrograms of Formoterol which was developed as a new bronchodilator and 4 mg of Salbutamol which is considered to be a beta 2-selective drug, to healthy adults. Pulse rate, blood pressure and blood levels of cyclic GMP, free fatty acid, cyclic AMP, glucose and lactic acid were measured in order to evaluate efficacy and dosage of Formoterol and to compare efficacy of this drug with that of Salbutamol. As a result, it is considered that Formoterol has a strong dose dependent beta 2-effect with 40 micrograms of Formoterol almost as high as 4 mg of Salbutamol in beta 2-effect. In addition, Formoterol has almost no alpha-effect and its beta 1-effect can be considered negligible in the doses of 60 micrograms and 80 micrograms.

Adult↗
PubMed1984

Selective IgA deficiency: analysis of Ig production in vitro.

The cellular basis of the pathogenesis of selective IgA deficiency (SIgAD) was investigated by examining surface immunoglobulin (SmIg) and in vitro pokeweed mitogen (PWM)-stimulated immunoglobulin (Ig) synthesis and by assaying in combination the counterpart lymphocytes from individuals with SIgAD and healthy donors. Peripheral blood lymphocytes (PBL) from 14 individuals with SIgAD synthesized normal amounts of IgG and IgM but did not synthesize normal amounts of IgA. Functional defects of lymphocytes for IgA synthesis were classified into four types: (i) B-lymphocyte dysfunction, (ii) increased function of suppressor T lymphocytes (Ts), (iii) decreased function of helper T lymphocytes (Th), and (iv) B-lymphocyte dysfunction and increased Ts function. The cells bearing SmIgG, SmIgM, and SmIgD were demonstrated at normal percentage ratios in all cases by immunofluorescent staining. The cells bearing SmIgA were at normal percentage ratios in the cases of T-lymphocyte dysfunction, while in the cases of B-lymphocyte defect SmIgA-bearing cells were reduced.

Adult↗