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Biomedical subjects

K Shimada

Publications and source records attributed to K Shimada.

At least 1,225 records · Page 68Linked to original sources
PubMed1988

Gene rearrangements of T cell receptor beta and gamma chains in HTLV-I infected primary neoplastic T cells.

Rearrangements of T cell receptor beta and gamma chain (T beta and T gamma) genes were analyzed by Southern blot method in samples from 30 patients with adult T cell leukemia (ATL) and 17 patients with non-ATL T cell neoplasms. The DNA probes used were the constant and joining region of T beta gene and the joining region of T gamma gene. Rearranged bands of T beta gene on one or both allelic chromosomes were detected in all neoplastic T cells, even those of smoldering ATL, in which only a small percentage of peripheral blood T cells were detected as leukemic. T gamma gene was rearranged in the cells of all but one patient, the exception being one ATL patient. In order to test whether any given variable region (V) of T beta gene was expressed in ATL cells, two functionally rearranged V beta sequences of ATL were compared with a V beta sequence from T cells acute lymphoblastic leukemia cells. No significant homologies were noted among the three deduced gene product amino acid sequences, confirming that T beta molecules of ATL cells contained no specific structures in common. The observed heterogeneity of T beta and T gamma gene rearrangements in ATL cells further supported these findings.

Amino Acid Sequence↗
PubMed1988

Monoclonal hybridoma anti-cardiolipin antibodies from SLE mice.

To determine whether the anti-cardiolipin antibodies are identical with the lupus anticoagulant and other antibodies to phospholipids and DNA, we prepared monoclonal hybridoma autoantibodies to cardiolipin from SLE-prone MRL/lpr mice and characterized their specificity. Using a somatic cell hybridization technique, we established three hybridoma clones which produce antibodies to cardiolipin (CAL-1: IgG2b, k, CAL-2: IgM, k and CAL-3: IgM, k). These hybridoma antibodies preferentially reacted with cardiolipin and phosphatidylserine, weakly reacted with phosphatidylinositol, but not with other phospholipids such as phosphatidylcholine, sphingomyelin, phosphatidylethanolamine and VDRL antigen. Two hybridoma anti-cardiolipin antibodies bound to ssDNA and were found to act as the lupus anticoagulant when mixing activated partial thromboplastin time with cephalin. These autoantibodies may prove to be good tools for elucidating mechanisms of thrombosis, thrombocytopenia, fetal loss and other related manifestations found in patients with systemic lupus erythematosus.

Animals↗
PubMed1988

[Clinical statistics on outpatients, inpatients and operations in 1986].

Statistical studies were made on 1,637 outpatients, 568 inpatients and 563 operative procedures at our department in 1986. The most frequent diseases among the outpatients were urogenital infections followed by anomalies, tumors and stones. The major diseases among the inpatients were hypospadias, vesicoureteral reflux, benign prostatic hypertrophy, bladder tumor and congenital urethral stenosis. A total of 563 operations were performed. The five major operations were hypospadia repair, optic internal urethrotomy, transurethral resection of prostate, ureterocystoneostomy and percutaneous nephrolithotripsy.

Adolescent↗
PubMed1988

IgG subclass distribution of anticardiolipin antibody in patients with systemic lupus erythematosus.

IgG subclass distributions of anticardiolipin (aCL), anti-ssDNA, and anti-dsDNA antibodies in sera of patients with systemic lupus erythematosus were determined by an enzyme linked immunoassay (ELISA) method, using mouse monoclonal antihuman IgG subclass antibodies. IgG aCL activity consisted mainly of the IgG1 subclass, and to some extent, the IgG3 subclass. Definite amounts of aCL activity were also detected in IgG2 in sera from 25% of the patients. Anti-ssDNA antibody activity was relatively equally distributed among IgG1, IgG2 and IgG3, but was poorly distributed in IgG4. In contrast, anti-dsDNA antibody activity consisted mainly of IgG1 and IgG3.

Antibodies, Antinuclear↗
PubMed1988

Myospherulosis in Japan. A report of two cases and an immunohistochemical investigation.

We report two cases of myospherulosis and offer review of the Japanese literature. Case 1 was a 41-year-old woman with cystic tumors under the fascia of the right major gluteal muscle. Case 2 was a 36-year-old man with subcutaneous cystic tumors in the right buttock. The characteristic saccular structures enclosing numerous small spherules were observed in the cysts. These spherules measured 5-7 micron in diameter and stained with Masson trichrome, Giemsa, Papanicolaou, and alizarin red S for hemoglobin. The myospherules also stained positively by the immunohistochemical method for hemoglobin. These findings support the contention that the spherules and parent bodies were derived from erythrocytes altered by foreign lipids or fat.

Adult↗
PubMed1987

Structural organization of the mouse mitochondrial aspartate aminotransferase gene.

Structural organization of the entire mouse mitochondrial aspartate aminotransferase (EC 2.6.1.1) gene was determined by analyzing the overlapping genomic clones obtained from a Charon 4A DNA library. The gene is 25 X 10(3) base-pairs long and contains ten exons interrupted by nine introns of various sizes. The 5' and 3'-flanking regions, the exact sizes and boundaries of the exon blocks including the transcription-initiation sites were determined. The 5' end of the gene lacks the prototypical 5' transcriptional regulatory sequence elements, such as TATA and CAAT boxes, but contains G + C-rich sequences, two putative binding sites for a cellular transcription factor, Sp1, and multiple transcription-initiation sites. Moreover, the sequences around the transcription-initiation sites are compatible with the formation of a number of potentially stable stem-loop structures. The leader sequence, which is essential for the transport of the protein into the mitochondria, is coded by the first exon and is separated from the mature protein by the first intron. The pyridoxal 5'-phosphate-binding domain, consisting of seven alternating beta-sheets and alpha-helical polypeptide strands, is separated by four introns present at the ends of alpha-helices. These genomic DNA structures suggest that the introns were not inserted into a previously uninterrupted coding sequence, but rather are products of evolution of the ancestral gene. However, a further correlation between the positions of introns relative to the well-defined structural domains of the mature protein was not obvious.

Animals↗
PubMed1987

Cloning and sequence analysis of cDNAs encoding mammalian cytosolic malate dehydrogenase. Comparison of the amino acid sequences of mammalian and bacterial malate dehydrogenase.

A cDNA clone, named ppcMDH-1 and covering a part of the coding region for the porcine cytosolic malate dehydrogenase (cMDH) mRNA, was isolated from a porcine liver cDNA library. Subsequently, mouse cMDH cDNA clones were isolated from mouse liver and heart cDNA libraries, using the ppcMDH-1 cDNA as a probe. The longest clone, named pmcMDH-5, was sequenced and the primary structure of the mouse cMDH deduced from its cDNA sequence showed that the mouse cMDH consists of the 334-amino acid residues. When the amino acid sequence of the mouse cMDH was compared with that of the porcine cMDH, they shared a 93% homology. On the other hand, the amino acid sequences of mouse cMDH and mitochondrial MDH (mMDH) showed about 23% overall homology. Surprisingly, comparison of the amino acid sequences among the mammalian and bacterial MDHs revealed that the homology between the mouse cMDH and thermophilic bacterial MDH, as well as the homology between the mouse mMDH and Escherichia coli MDH, markedly exceeds the intraspecies sequence homology between mMDH and cMDH from mice.

Amino Acid Sequence↗
PubMed1987

Sensitive ferrocene reagents for derivatization of thiol compounds in high-performance liquid chromatography with dual-electrode coulometric detection.

Three N-substituted maleimides possessing ferrocene as an electrophore were prepared and evaluated for pre-column derivatization of thiol compounds in high-performance liquid chromatography with dual-electrode coulometric detection. The utility of these reagents was investigated by employing N-acetyl-L-cysteine as a model compound. Among the three, N-(ferrocenyl) maleimide was the most favourable reagent with respect to reactivity, stability and electrochemical properties. The dual-electrode coulometric detection of the adduct showed high selectivity and sensitivity with a detection limit of 0.06 pmol. The proposed method is applicable to the determination of glutathione in biological specimens.

Adult↗
PubMed1987

Detection of toxoplasma IgM antibody by passive latex agglutination reaction.

Three major components (designated Sp-1, -2 and -3) of the microsomal pellet of Toxoplasma gondii (Tp) were isolated by Ultragel AcA 44 gel filtration chromatography from the microsomal pellet solubilized with detergents. Of these, Sp-2 proved to be most reactive with anti-Tp antibodies and its reactivity with IgM and IgG antibodies varied with the concentration at which it was used for sensitizing latex particles. Sp-2 antigen reacted with IgM antibody alone when latex particles were sensitized with less than or equal to 100 micrograms of this antigen/mg of particles, and its reactivity with IgG antibody appeared and increased progressively with increasing sensitizing concentrations of this antigen. Based on this finding, a method of direct measurement of anti-Tp IgM antibody in serum by passive latex agglutination has been developed. Polyacrylamide disc gel electrophoretic analysis of Sp-2 antigen in the presence of SDS revealed four constituents of 43, 35, 28 and 14 kDa. All these components reached with both IgM and IgG when tested by immunoblotting.

Animals↗
PubMed1987

Studies on steroids. CCXXIX. Separation and characterization of catechol oestrogen glucuronides in urine of pregnant women by high-performance liquid chromatography.

The separation and characterization of catechol oestrogen glucuronides in the urine of pregnant women by high-performance liquid chromatography with electrochemical detection is described. The urine samples from pregnant women were passed through Amberlite XAD-2 and Sep-Pak C18 columns and subsequented to ion-exchange chromatography on piperidinohydroxypropyl Sephadex LH-20 to isolate the oestrogen glucuronide fraction. The subsequent resolution into individual oestrogen glucuronides was achieved by high-performance liquid chromatography on a reversed-phase column. 2-Hydroxyoestrone 2-glucuronide and 4-hydroxyoestrone 4-glucuronide were identified on the basis of their behaviour in high-performance liquid chromatography with three different mobile phases. Derivatization of two glucuronides with 2-ferrocenylethylamine, followed by chromatographic separation and measurement of hydrodynamic voltammograms with an electrochemical detector was carried out for unequivocal identification. Enzymatic cleavage of the glucuronoside linkage followed by the identification of deconjugated catechol oestrogens by high-performance liquid chromatography with electrochemical detection further supported the structural assignment of these metabolites. The ratio between the amounts of 2-hydroxyoestrone 2-glucuronide and 4-hydroxyoestrone 4-glucuronide excreted in the urine of pregnant women was found to be ca. 5:1.

Chromatography, High Pressure Liquid↗
PubMed1987

Cloning and sequence analysis of cDNAs encoding mammalian mitochondrial malate dehydrogenase.

A cDNA clone, named ppmMDH-1 and covering a part of the porcine mitochondrial malate dehydrogenase (mMDH; L-malate:NAD+ oxidoreductase, EC 1.1.1.37) mRNA, was isolated from a porcine liver cDNA library with a mixture of 24 oligodeoxyribonucleotides as a probe. The sequences of the probe were deduced from the known sequence of porcine mMDH amino acid residues 288-293. ppmMDH-1 covered the coding region for porcine mMDH amino acid residues 17-314 and the 3' untranslated region. Subsequently, mouse mMDH cDNA clones were isolated from a mouse liver cDNA library with the ppmMDH-1 cDNA as a probe. One of the clones, named pmmMDH-1 and containing a cDNA insert of about 1350 base pairs, was selected for sequence analysis, and the primary structure of the mouse precursor form of mMDH (pre-mMDH) was deduced from its cDNA sequence. The sequenced coding regions for the porcine and mouse mMDH mRNAs showed about 85% homology. When the deduced amino acid sequence of the mouse pre-mMDH was compared with that of the porcine mMDH, they shared a 95% homology, and the mouse pre-mMDH yielded a leader sequence consisting of 24 amino acid residues and a mature mMDH, consisting of 314 amino acid residues. The leader sequence contained three basic amino acid residues, no acidic residues, and no hydrophobic amino acid stretch. The mouse mMDH leader sequence was compared with those of three other rodent mitochondrial matrix proteins.

Amino Acid Sequence↗