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Biomedical subjects

K Hori

Publications and source records attributed to K Hori.

At least 163 records · Page 9Linked to original sources
PubMed1996

[Utility of predeposit autologous blood donation by switch back method combined with recombinant human erythropoietin in gynecological surgery].

To apply recombinant human (rh)erythropoietin (EPO) to predeposit autologous blood donation (P.A.B.D.) in cancer patients clinically, (1) we tested the effects of rh-EPO on 2 ovarian cancer cell lines in vitro at first, then, (2) studied the effect of the rh-EPO for switch back (SB) method that is a variant of P.A.B.D. clinically. Rh-EPO (0.068-68U/ml) caused no significant and reproducible stimulation of clonal growth to SHIN-3 (derived from serous cyst adenocarcinoma) and MN-1 (derived from mucinous cyst adenocarcinoma). Twenty-five cases were studied. The change in the hemoglobin concentration (delta Hb) was -0.43 +/- 1.38g/dl (mean +/- SD) and the change in the total amount of hemoglobin (total delta Hb) which is calculated on the basis of whole blood volume was 111.5 +/- 53.2g/body in 16 cases with rh-EPO. The delta Hb and total delta Hb were -3.25 +/- 0.78g/dl and 30.1 +/- 41.7g/body in 9 cases without rh-EPO. The rh-EPO combined cases were significantly increased in both delta Hb and total delta Hb (p < 0.05, unpaired student t test). We therefore conclude that it would be very beneficial to use rh-EPO combined with the SB method in P.A.B.D. for high maximum surgical blood order schedule (MSBOS) cases such as gynecological malignancies.

Adult↗
PubMed1996

[Pre-emptive analgesia from intravenous administration of opioid: no effect with pentazocine].

The influence of timing of administration of preoperative pentazocine on pain and analgesic requirements after surgery was studied in 46 patients undergoing total abdominal hysterectomy. Twenty-three patients received thiamylal 5 mg.kg-1 on induction of anesthesia, followed by pentazocine 30 mg or 60 mg before surgical incision (group A). Twenty-three control patients received pentazocine 30 mg or 60 mg, 5 min after abdominal incision (group B). The visual analogue scales for pain 24 h after operation were 6.0 cm at 30 mg dose in group A or 5.3 cm at 60 mg dose in group A and 5.7 cm at 30 mg dose in group B or 4.7 cm at 60 mg dose in group B. There were no differences in the visual analogues scales. Pentazocine consumption in the first 24 h after surgery was 67.5 mg at 30 mg dose in group A or 52.5 mg at 60 mg dose in group A and 70.9 mg at 30 mg dose in group B or 51.8 mg at 60 mg dose in group B. We conclude that postoperative pentazocine consumption and pain scores are no different when pentazocine is given before or after skin incision for abdominal hysterectomy and that there is no clinically useful pre-emptive analgesic effect with these doses of pentazocine.

Adult↗
PubMed1996

[Experience with surgery for synchronous double cancer of rectum and lung detected after long-term follow-up for pneumoconiosis].

A 60-year-old man has been followed up for pneumoconiosis for 7 years. He was admitted to our hospital because of melena. He was undergone a colonofiberscopy and was diagnosed as rectal cancer. We performed anterior resection of the rectum (Stage I). About 5 months after the first operation, abnormal shadows of the both lungs were growing in size. Bronchoscopic examination revealed adenocarcinoma, we performed left upper lobectomy (Stage I) and this case was judged a synchronous double cancer.

Adenocarcinoma↗
PubMed1995

Comparative studies of human recombinant 74- and 54-kDa L-histidine decarboxylases.

We have expressed and characterized human recombinant 74-kDa (rHDC74) and 54-kDa (rHDC54) L-histidine decarboxylases (HDCs) in Sf9 cells. By immunoblot analysis, rHDC74 and rHDC54 were shown to be localized predominantly in the particulate and soluble fractions, respectively. rHDC74 exhibited histamine-synthesizing activity equivalent to that of rHDC54. The existence of 74- and 54-kDa HDCs was also confirmed in the particulate and supernatant fractions of the cell lysate, respectively, from the human basophilic leukemia cell line KU-812-F. The ratio of HDC activity to immunoreactivity was similar for the two forms of the enzyme. The specific activity of purified rHDC54 (1.12 mumol/mg/min) was comparable to those of HDCs from other mammalian tissues or cells. The purified rHDC54 was eluted as a monomer form from a Superdex-200 column; the molecular mass of the enzyme was approximately 54 kDa on SDS-polyacrylamide gel electrophoresis without 2-mercaptoethanol. The HDC activity of rHDC54 significantly decreased on dialysis against buffer without pyridoxal 5'-phosphate; addition of pyridoxal 5'-phosphate to the dialysate readily increased in the enzyme activity to the original activity. Taken together, these results suggest that human HDC functions as both 74- and 54-kDa forms having equivalent HDC activity, which are localized in the particulate and soluble fractions, respectively, and that the latter form exhibits its activity as a monomer form.

Animals↗
PubMed1995

Analysis of the in vitro translation product of a novel-type Drosophila melanogaster aldolase mRNA in which two carboxyl-terminal exons remain unspliced.

Drosophila melanogaster generates three different types of aldolase mRNAs from a single gene by selective usage of the triplicate exons 4 (4 alpha, 4 beta, and 4 gamma), which encode three different isozymes having respective carboxyl termini. We have found the presence of a novel-type mRNA (named alpha beta) in which two final exons, 4 alpha and 4 beta, were retained unspliced. Herein, a cDNA clone containing the alpha beta sequence was inserted into pINIII and expressed in an Escherichia coli system. The product, which exhibited aldolase activity, was found to be isozyme alpha from the primary structure and the enzymological properties, with the 4 alpha sequence alone being present as the carboxyl terminus. In tissues of D. melanogaster, the production of mRNA encoding exon 4 alpha is known to be restrained to a low level. This may be understood by the fact that the aldolase gene of this species does not have a typical poly(A) signal at the 3' end in exon 4 alpha. Instead, the transcript-encoding exons, 4 alpha and 4 beta, might be produced when AATATA, which resides downstream of the coding frame in exon 4 beta, is recognized as a poly(A) signal during RNA processing.

Alternative Splicing↗
PubMed1995

The plastid aldolase gene from Chlamydomonas reinhardtii: intron/exon organization, evolution, and promoter structure.

Genomic clones encoding the plastidic fructose-1,6-bisphosphate aldolase of Chlamydomonas reinhardtii were isolated and sequenced. The gene contains three introns which are located within the coding sequence for the mature protein. No introns are located within or near the sequence encoding the transit-peptide, in contrast to the genes for plastidic aldolases of higher plants. Neither the number nor the positions of the three introns of the C. reinhardtii aldolase gene are conserved in the plastidic or cytosolic aldolase genes of higher plants and animals. The 5' border sequences of introns in the aldolase gene of C. reinhardtii exhibit the conserved plant consensus sequence. The 3' acceptor splice sites for introns 1 and 3 show much less similarity to the eukaryotic consensus sequences than do those of intron 2. The plastidic aldolase gene has two tandemly repeated CAAT box motifs in the promoter region. Genomic Southern blots indicate that the gene is encoded by a single locus in the C. reinhardtii genome.

Amino Acid Sequence↗
PubMed1995

Septo-hippocampal cholinergic system under the discrimination learning task in the rat: a microdialysis study with the dual-probe approach.

To investigate regulation of the septo-hippocampal cholinergic system by dopaminergic inputs to the septum in rats which performed a discrimination learning task, an in vivo microdialysis method with the dual-probe approach was used. Rats were trained to discriminate between lamp-on and -off states under an operant-type learning procedure. After stable discriminative behavior was established, dialysis probes were implanted into the hippocampus and the lateral septum area of each rat. The concentration of dopamine (DA) in the septum rapidly increased within 20 min after the beginning of a learning session. However, another group of rats trained on a similar but non-discriminative task showed no such increase. The concentration of acetylcholine (ACh) in the hippocampus was significantly enhanced during the learning session and rapidly returned to the basal value after the session, but showed a delayed and diminished increase in the non-discrimination group. These results suggest that DAergic inputs to the septum may be involved in control of the septo-hippocampal cholinergic system which is of importance for discrimination learning behavior.

3,4-Dihydroxyphenylacetic Acid↗
PubMed1995

New gene, nel, encoding a M(r) 93 K protein with EGF-like repeats is strongly expressed in neural tissues of early stage chick embryos.

A new gene, nel, was isolated from a 9-day-old chick embryonic cDNA library. The gene encodes a protein of 835 amino acids (93,407 M(r)) consisting of two hydrophobic domains presumed to be the signal and transmembrane sequences, a histidine rich domain, two repeats of a cysteine rich structure similar to the C-terminal domain of von Willebrand factor, five EGF-like repeats, and again two repeats of the cysteine rich sequence similar to the C-terminal domain of von Willebrand factor in the presumed cytoplasmic domain. The expression of the nel gene was studied by Northern blot and in situ hybridization analyses of chick embryos. The mRNA of the gene was found in all tissues of 10- and 17-day-old embryos by Northern blot hybridization. Among the tissues examined, the level in the brain was highest and increased with age. After hatching, gene expression was retained in the brain at about the same level found in old embryos, increased in the retina, and disappeared from the other tissues. In situ hybridization with a nel gene probe revealed that the gene was strongly expressed in neural tissues such as brain, spinal cord, and dorsal root ganglia of early embryos. Gene expression was observed in the mantle layer of the neurepithelium of the brain and of the spinal cord. Gene expression in early embryos was not restricted to the neural tissues, but was also detected in the cells around cartilage, myocardium, lung mesenchymal cells, and in the liver, etc. One band of about 4.5 Kb mRNA was detected in all tissues and stages by Northern blot hybridization analysis. The possible function of the gene is discussed.

Amino Acid Sequence↗
PubMed1995

Effect of leukotriene C4D4 antagonist on colonic damage induced by intracolonic administration of trinitrobenzene sulfonic acid in rats.

We examined the effects of eicosanoid antagonists on colonic damage induced by trinitrobenzene sulfonic acid (TNB) in a rat inflammatory bowel model. TNB (30 mg) dissolved in 0.25 ml of 50% ethanol, was given intrarectally. The appropriate doses of ONO-1078 (a leukotriene C4D4 antagonist), ONO-4057 (a leukotriene B4 antagonist), and OKY-046 (a thromboxane A2 synthetase inhibitor) were given to obtain the same blood level, either 4 h before (pre-treatment model) or 24 h after (the post-treatment model) the administration of TNB (n = 8 in all groups). Drugs were given once daily for 6 days through a gastric feeding tube. Autopsy was performed on the 7th day. Colonic damage was assessed in terms of colonic damage scores, and myeloperoxidase (MPO) activity and eicosanoid concentrations in colonic tissues were measured. Compared with the group given TNB alone, the colonic damage score was reduced to 10% in the pre-treatment model with ONO-1078, but the score was not reduced in other groups, MPO activity was not changed in any group. The concentration of leukotriene C4 was reduced with ONO-1078 treatment, in both pre- and post-treatment models. These results demonstrated that a leukotriene C4D4 antagonist reduced colonic inflammation; however, its anti-inflammatory effect was limited in this colitis model.

Animals↗
PubMed1995

Poststreptococcal glomerulonephritis with the nephrotic range of proteinuria.

In order to characterize the clinical features in poststreptococcal glomerulonephritis (PSGN) in relation to the range of proteinuria, 27 patients with PSGN were divided into 3 groups according to the amount of urinary protein excretion; Group I: with proteinuria over 3.5 g/day (n = 8), Group II: with proteinuria between 1.0 and 3.4 g/day (n = 9) and Group III: with proteinuria less than 1.0 g/day (n = 10). Bed-rest was ordered until proteinuria decreased to less than 1.0 g/day. The serum creatinine levels in Group I were significantly higher than in Group III both on admission and at discharge, although the duration of hospitalization was longer in the former than in the latter group. Furthermore, the durations of proteinuria and hypocomplementaemia were longer in the former than in the latter. In addition, the former showed a higher systolic blood pressure and a greater expanded extracellular fluid volume expressed as body weight change during hospitalization. However, none of the patients in this study demonstrated any persistent proteinuria or renal function impairment. In conclusion, bed-rest in the acute phase of PSGN might improve the short-term prognosis of PSGN.

Adult↗
PubMed1995

Variation of growth rate of a rat tumour during a light-dark cycle: correlation with circadian fluctuations in tumour blood flow.

To determine whether tumour growth is influenced by circadian variations in tumour tissue blood flow, we measured changes in area doubling time of tumours (Sato lung carcinoma) within transparent chambers and changes in tissue blood flow of rat subcutaneous tumour during a light-dark cycle. Rats were subjected to an artificial light-dark cycle with light from 7 a.m. to 7 p.m. Tumour doubling times (TDTs) during the dark and the light spans were 33.5 +/- 11.9 h (n = 38, 20 rats) and 70.6 +/- 36.9 h (n = 39, 20 rats) respectively. The former was significantly shorter than the latter (P < 0.001). In addition, the larger the tumour became, the longer was the TDT during the light span (P < 0.05). Tumour tissue blood flow during the night (10 p.m.-4 a.m.) was approximately 1.5 times greater than that during the day (10 a.m.-4 p.m.). The time during which tumours actively grow and that during which tissue blood flow in tumours increases coincided. These results strongly suggest that tumour tissue blood flow is a determining influence on tumour proliferative activity and that tumour growth is influenced by circadian variations in tumour tissue blood flow.

Animals↗
PubMed1995

Three conserved glycine residues in valine activation of gramicidin S synthetase 2 from Bacillus brevis.

The translated product from the gene fragment containing the second and third domains of gramicidin S synthetase 2 was purified to an essentially homogeneous state. It showed valine- and ornithine-activating activity and the second domain was proved to be the valine-activating domain. Three mutant genes from Bacillus brevis Nagano, BI-3, E-4, and E-5 strains, which encode defective valine-activating domains of gramicidin S synthetase 2, were sequenced. By comparison with the wild-type gene, single point mutations of guanine to adenine were found at the three conserved glycine codons; the 5303rd guanine in BI-3, the 5378th guanine in E-4, and the 4967th guanine in E-5, which corresponded to codon changes of the 1768th glycine to glutamic acid and the 1793rd and the 1656th glycine to aspartic acid. Loss of valine-adenylation activity by mutation at the 1656th glycine proved the direct participation of the TSGT/STGXPKG motif in the adenylation reaction, and suggests that this glycine residue with the conserved lysine residue of the motif forms the phosphate-binding loop for ATP-binding. The 1793rd glycine is a member of the YGXTE motif which was also conserved among adenylate-forming enzymes except acetyl-CoA synthetases. The 1768th glycine residue appears to maintain the conformation of the active site for aminoacyl adenylation since this residue is retained among the adenylate-forming enzymes, though flanking regions are not conserved. These results suggest that these glycine residues are essential for adenylate formation in the antibiotic peptide synthetase family and some other adenylate-forming enzymes.

Amino Acid Isomerases↗
PubMed1995

Structures of cDNAs encoding the muscle-type and non-muscle-type isozymes of lamprey fructose bisphosphate aldolases and the evolution of aldolase genes.

Nearly full-length cDNA clones for muscle-type and non-muscle-type aldolase mRNAs were cloned from lambda gt10 cDNA libraries constructed from skeletal muscle and liver mRNAs of lamprey (Entosphenus japonicus). The cDNA-M8 has 2,240 bp carrying an open reading frame of 1,089 bp which encodes 362 amino acids without the amino terminal methionine, while the cDNA-L3 is 1,761 bp in length and has an open reading frame of 1,092 bp, which encodes 363 amino acids without the methionine. We designated the cDNA clones M8 and L3 as the muscle-type and non-muscle-type aldolase cDNAs, respectively. The entire amino acid sequences deduced from cDNA-M8 and -L3 show a high degree of identity to one another (76%) and also to vertebrate aldolases A (74-76%), B (68-70%), and C (71-76%) and Drosophila melanogaster aldolases alpha, beta, and gamma (66-67%). Northern blot analyses using the 3'-noncoding sequences of cDNA-M8 and -L3 as hybridization probes indicated that the muscle-type mRNA is expressed mainly in the skeletal muscle, heart muscle, brain, and some other tissues, but probably not in liver, while the non-muscle-type mRNA is expressed mainly in the liver and also in brain and other tissues, except for the heart muscle. Phylogenetic analyses showed that both muscle-type and non-muscle-type aldolases of lamprey resemble one another and might share a common ancestor with vertebrate aldolases A and C, but they are not direct ancestors of vertebrate aldolases.

Amino Acid Sequence↗
PubMed1995

Drosophila melanogaster aldolase: characterization of the isozymes alpha, beta, and gamma generated from a single gene.

Three isozymic forms, alpha, beta, and gamma, of Drosophila melanogaster aldolase are produced from a single gene by alternative usage of the triple exons 4 (4 alpha, 4 beta, and 4 gamma) [Shaw-Lee et al. (1992) J. Biol. Chem. 267, 3959-3967; Kim et al. (1992) Mol. Cell. Biol. 12, 773-783; Kai et al. (1992) J. Biochem. 112,677-688]. The expression plasmids for the respective isozymes were transfected into Escherichia coli cells, and the isozymes alpha and beta were purified to homogeneity by a simple procedure, though isozyme gamma was only partially purified. These isozymes are active towards two substrates, fructose-1,6-bisphosphate (Fru-1,6-P2) and fructose-1-phosphate (Fru-1-P), with a preference for Fru-1,6-P2 over Fru-1-P, but they have different kcat/Km values towards these two substrates; isozyme alpha shows the highest value for Fru-1,6-P2. These isozymes show similarity in optimal pHs, thermal stability, and Km values for both Fru-1,6-P2 and Fru-1-P. They are composed of four identical subunits of 40 kDa, forming a tetramer with a molecular weight of approximately 160 kDa. The three isozymes are different in primary structure only at the carboxyl-terminal region encoded by the respective exon 4. Therefore, this region should be primarily responsible for the distinct characteristics of these isozymes.

Amino Acid Sequence↗
PubMed1995

Copy-dependent and position-independent expression of rat aldolase A gene.

In order to understand the molecular mechanisms of the temporal and spatial differences of gene expression in higher organisms, rat aldolase A gene carrying two distinct promoters was introduced into fertilized eggs and the resulting transgenic mice were analyzed. The transgene expression is tissue-specific and is developmentally regulated. In addition, the expression is regulated in a copy-dependent manner irrespective of where the transgene is integrated, suggesting that a mechanism excluding the effect of the integration site exists within the transgene itself. To explore the conformational change of this gene in the genome, the DNase I hypersensitive sites of the gene were examined. Three sites (DHS-1,2, and 3) were identified upstream and downstream of the gene and these sites were retained in the transgene as well as in the gene observed endogenously.

Animals↗
PubMed1995

Actin-actin contact: chemical cross-linking between actin and the 2.6-kDa peptide from subdomain 4 of actin.

Previously, we demonstrated that the 2.6-kDa peptide extending from Arg177 to Tyr198 in subdomain 4 of rabbit skeletal actin bound to actin itself, inhibited the elongation of actin filament, and severed F-actin. The corresponding segment in actin, therefore, is thought to contain the most critical actin-actin contact [Hori, K. and Morita, F. (1992) J. Biochem. 112, 401-408; Hori, K., Itoh, T., Takahashi, K., and Morita, F. (1994) Biochim. Biophys. Acta 1186, 35-42]. In this paper, we report on the binding site in actin for the 2.6-kDa peptide studied by using a zero-length cross-linker, 1-ethyl-3(3-dimethylaminopropyl)carbodiimide (EDC). We conducted limited digestion of actin cross-linked with the 125I-labeled 2.6-kDa peptide with various proteases, and developed peptide maps. The cross-linked region of the 2.6-kDa peptide was found to be within the region of Ala114 to Glu167 in actin by identifying the radioactive peptide fragments. The region was further restricted by isolation of radioactive peptide from alpha-chymotryptic digest of the cross-linked actin. The binding site of the 2.6-kDa peptide was finally assigned to be within the 24 amino acid segment from Ala144 to Glu167, which lies in subdomain 3 of actin. Using computer graphics, actin-actin contact provided by the two segments was suggested to be along the left-handed genetic helix of actin filament.

Actins↗
PubMed1995

Purification and properties of branched chain amino acid aminotransferase from gramicidin S-producing Bacillus brevis.

The branched chain amino acid aminotransferase [EC 2.6.1.42] was purified to a homogeneous state from a gramicidin S-producing strain of Bacillus brevis. The enzyme had a molecular weight of about 93,000 and consisted of two identical subunits, each with a molecular weight of about 47,000. One pyridoxal phosphate is bound per subunit. In addition to branched chain amino acids, the enzyme uses L-phenylalanine and L-tryptophan as the amino donor, indicating that B. brevis branched chain amino acid aminotransferase has a broad substrate specificity for the amino donor. The enzyme utilized 2-oxoglutarate as the amino acceptor. The purified enzyme exhibits its absorption maxima at 332 and 427 nm at neutral pH.

Bacillus↗