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Biomedical subjects

T Takano

Publications and source records attributed to T Takano.

At least 541 records · Page 30Linked to original sources
PubMed1987

Current status of prehospital care of patients with acute myocardial infarction in Tokyo: analysis of 3-year experience with coronary care unit network.

To clarify the current status of prehospital care of patients with acute myocardial infarction (AMI) in the Tokyo metropolitan area, the availability of the coronary care unit (CCU) network during the past 3 years (January 1982 through December 1984) was analyzed, examining: final diagnosis, circumstances at the onset of AMI, course of transportation to CCU, time elapsed before admission, severity of AMI, and prognosis of patients. Of 6,939 patients admitted to CCU by means of the CCU network, 2,408 patients (34.7%) had AMI. The patient's decision time was, on the average, 12 hr 3 min, longer when the course of transportation to CCU was more complicated. The fatality for AMI was 17.2%. Causes of death were pump failure in 52.8%, arrhythmias in 62.8% and mechanical failure such as cardiac rupture in 8.5%. Patients with complicated AMI were admitted earlier and had a higher fatality than those without complications. Thus, community oriented programs are required to more fully inform the population at risk of AMI to shorten the patient's decision time, and more effective means to treat patients with pump failure and to prevent the development of pump failure need to be established.

Aged↗
PubMed1986

Secretion activities of Bacillus subtilis alpha-amylase signal peptides of different lengths in Escherichia coli cells.

The B. subtilis alpha-amylase promoter and signal peptide are functional in E. coli cells. DNA fragments coding for signal peptides with different lengths (28, 31, 33 and 41 amino acids from the translation initiator Met) were prepared and fused with the E. coli beta-lactamase structural gene. In B. subtilis cells, the sequences of 31, 33 and 41 amino acids were able to secrete beta-lactamase into the surrounding media, but the 28 amino acid sequence was not. In contrast, all of the four sequences were able to export beta-lactamase into the periplasmic space of E. coli cells. Thus, the recognition of the B. subtilis alpha-amylase signal peptide in E. coli cells seems to be different from that in B. subtilis cells.

Amino Acid Sequence↗
PubMed1986

Similarity of lysosomal H+-ATPase to mitochondrial F0F1-ATPase in sensitivity to anions and drugs as revealed by solubilization and reconstitution.

Lysosomal H+-translocating ATPase (H+-ATPase) was solubilized with lysophosphatidylcholine and reconstituted into liposomes (Moriyama, Y., Takano, T. and Ohkuma, S. (1984) J. Biochem. (Tokyo) 96, 927-930). In this study, the sensitivities of membrane-bound, solubilized and liposome-incorporated ATPase to various anions and drugs were measured in comparison with those of similar forms of mitochondrial H+-ATPase (mitochondrial F0F1-ATPase) with the following results. (1) Bicarbonate and sulfite activated solubilized lysosomal H+-ATPase, but not the membrane-bound ATPase or ATPase incorporated into liposomes. All three forms of mitochondrial F0F1-ATPase were activated by these anions. (2) All three forms of both lysosomal H+-ATPase and mitochondrial F0F1-ATPase were strongly inhibited by SCN-, NO3- and F-, but scarcely affected by Cl-, Br- and SO2-4. (3) The solubilized lysosomal H+-ATPase was strongly inhibited by azide, quercetin, 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl), 4-acetamido-4'-isothiocyanatostilbene-2,2'-disulfonic acid (SITS), 4,4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS) and oligomycin. Its sensitivity was almost the same as that of mitochondrial F0F1-ATPase. Neither membrane-bound ATPase nor ATPase incorporated into liposomes was affected appreciably by these drugs. These results indicate that the sensitivity to anions and drugs of lysosomal H+-ATPase depends on the form of the enzyme and that the sensitivity of the solubilized lysosomal H+-ATPase is very similar to that of mitochondrial F0F1-ATPase. On the other hand, the two ATPases differ in their sensitivity to N-ethylmaleimide and pyridoxal phosphate: only the mitochondrial ATPase is inhibited by pyridoxal phosphate whereas only the lysosomal ATPase is inhibited by N-ethylmaleimide.

Animals↗
PubMed1986

Studies on fine structure and location of lipids in quick-freeze replicas of atherosclerotic aorta of WHHL rabbits.

The fine structure of intracellular and extracellular lipids in the atherosclerotic aorta of Watanabe-heritable hyperlipidemic (WHHL) rabbits was demonstrated by a quick-freeze etching technique. Many lipid droplets, with and without a membrane, were observed in the foam cells. Membrane-free droplets were observed as onion-like structure with a concentric lamellar structure surrounded by 10 nm filaments. Droplets surrounded by a limited membrane probably correspond to lipid-laden lysosomes. In the extracellular connective tissue space, marked accumulation of lipids with a vesicular structure was seen among collagen fibers. The appearance of these lipids was similar to that of lipids in lysosomes of foam cells.

Animals↗
PubMed1986

Monoclonal antibodies recognizing lipid-laden cells and extracellular regions with lipid-deposits in atherosclerotic aorta.

Monoclonal antibodies against lipid-laden cells and against extracellular regions of lipid-deposits in atherosclerotic aorta were prepared. Mice were immunized with a delipidated homogenate of atherosclerotic aorta of Watanabe-heritable hyperlipidemic rabbits. Hybridomas were obtained by fusion and cultured in hypoxanthine, aminopterin and thymidine selection medium. Specific antibodies were selected by indirect immunohistochemical staining of frozen sections of atherosclerotic aorta. Nine clones that produced antibodies that stained the atherosclerotic intima exclusively were selected and cloned by limiting dilution. Finally two clones (FCR1a/201F, FCR1b/904B) producing antibodies specific to lipid-laden cells and one clone (EMR1a/212D) producing an antibody specific to regions with lipid deposits in the extracellular matrix were established. These monoclonal antibodies may help in understanding how lipids accumulate in atherosclerosis.

Animals↗
PubMed1986

High-resolution cytogenetic studies in patients with Prader-Willi syndrome.

We investigated 24 patients with Prader-Willi syndrome by the high-resolution banding technique. Their history and clinical findings were also examined in some detail. Twelve had interstitial deletion of 15q; del(15) (q11.2q13) in 11 cases and del(15) (q11.2q12) in one case. Six revealed normal karyotypes at about 500-850 bands per haploid-set level. In an additional six cases, no deletion was detected. However, we took the results as tentative, as the observed karyotypes were at the 400-bands level. During the course of this study, it was realized that a small deletion in the proximal 15q could be easily overlooked when a mitotic spread around 400-bands or less per haploid-set level was used. There was no distinct difference in the clinical features of patients with interstitial deletion and those with a normal karyotype. Two cases in the latter group lacked some of the typical features of the former group, e.g. poor fetal vigor, neonatal feeding difficulty, hypotonia, and delayed motor development.

Adolescent↗
PubMed1986

Molecular cloning, DNA nucleotide sequencing, and expression in Bacillus subtilis cells of the Bacillus macerans cyclodextrin glucanotransferase gene.

The gene for cyclodextrin glucanotransferase from Bacillus macerans was cloned in an Escherichia coli bacteriophage, lambda D69, and was recloned in a Bacillus subtilis plasmid, pUB110. Starting from an ATG initiation codon, a unique reading frame was shown to extend for 2,142 base pairs (714 amino acids). The nucleotide sequence revealed that the enzyme is composed of two identical subunits.

Amino Acids↗
PubMed1986

Transcellular transport of lipoprotein through arterial endothelial cells in monolayer culture.

To study the mechanism of lipoprotein transport through arterial endothelial cells, porcine endothelial cells were cultured on gelated type I collagen supported by a dacron sheet, and the transport of low density lipoprotein (LDL) labeled with rhodamine B isothiocyanate (RB-LDL) through the cells was measured. Light and scanning electron microscopy showed that the cells on the gel were confluent. There was little RB-LDL transport through the endothelial monolayer at 0 degrees C. RB-LDL transport through the monolayer at 37 degrees C was dose-dependent saturable at 0.4 mg protein/ml. The transport was energy-dependent, since its rate was affected by temperature and was inhibited by a combination of 2-deoxyglucose (50 mM) and NaN3 (10 mM). RB-LDL was shown not to be degraded during transport.

Animals↗
PubMed1986

Transcellular transport of fluorescein dextran through an arterial endothelial cell monolayer.

Transcellular transport of fluorescein dextran (FD) of various molecular weights (4K, 10K, 20K, 70K and 150K daltons) through porcine arterial endothelial cells cultured on a type I collagen gel supported by a dacron sheet was studied and compared with the transport of low density lipoprotein labeled with rhodamine B (RB-LDL) described previously (Hashida et al., Cell Struct. Funct. 11, 31-42, 1986). The rate of FD transport through the monolayer depended on the size of the FD. FD transport was not temperature-dependent and was not a saturable process. Our findings show that FD transport differs from RB-LDL transport which is temperature- and dose-dependent. The mechanism of the transport of FD is compared with that of RB-LDL.

Animals↗