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Biomedical subjects

K Nagano

Publications and source records attributed to K Nagano.

At least 199 records · Page 11Linked to original sources
PubMed1987

[A combined treatment of interferon-alpha, 8 MHz radiofrequency hyperthermia and/or irradiation in a patient with advanced renal cancer].

A combined treatment of alpha interferon (INF), 8 MHz radiofrequency (RF) hyperthermia using Thermotron-RF Model 8 and/or irradiation was performed on a patient with advanced renal cancer. The patient was a 52-year-old male, who had received arterial embolization with a gelatin sponge and 60 mg of adriamycin for the right renal tumor in January, 1985. He was referred to our clinic in April, 1985. Computed tomography showed a right renal tumor, 120 x 105 x 80 mm. Histological examination revealed clear cell carcinoma of the right kidney. The tumor was unresectable because of the huge tumor size, invasion into the right lobe of the liver, multiple pulmonary metastases and severe dysproteinemia. From the beginning of May, 1985, administration of 3 x 10(6) units interferon-alpha (INF) daily and radiofrequency (RF)hyperthermia for one hour twice a week were started. By June 11, 1985, 10 sessions of RF-hyperthermia were performed. Thereafter, hyperthermia for the renal tumor was maintained once a week until June, 1986. From the middle of June, 1985, a gradual improvement of dysproteinemia and appetite loss, and a decrease of the right renal tumor size as well as disappearance of febrile attacks were attained. In November, 1985, mediastinal lymph node swelling developed. A combined therapy of RF-hyperthermia twice a week and irradiation with 2.0 Gy daily 5 times a week was started. A total of 14 sessions of RF-hyperthermia and 30 Gy of irradiation were delivered until January, 1986. Intratumoral temperature of the renal tumor reached 44.0 degrees C during the heating.(ABSTRACT TRUNCATED AT 250 WORDS)

Carcinoma, Renal Cell↗
PubMed1987

[Successful chemotherapy with adriamycin and methotrexate in a case of advanced transitional cell carcinoma of the ureter--a clinical application of subrenal capsule assay].

A case of advanced transitional cell carcinoma of the left ureter was treated with a combination of adriamycin and methotrexate. These drugs were selected using the subrenal capsule assay for which tumor tissues were obtained from a biopsy specimen of the left supraclavicular lymph node. Complete regression of left supraclavicular lymph node metastasis and 90% regression of para-aortic lymph node metastasis were obtained after four courses of the combination therapy. Subsequently, left total nephro-uretrectomy and retroperitoneal lymph node dissection were carried out. Pathological examination revealed the remains of tumor cells in the primary lesion and in the para-aortic lymph node. The tumor tissues obtained from the para-aortic lymph node were not susceptible to adriamycin and methotrexate. However, the tendency of the regression rates in the drug-treated groups was the same as that apparent before chemotherapy. Three courses of the same regimen as that given before surgery were then prescribed. The patient is currently alive with no evidence of disease. We therefore suggest the usefulness of the subrenal capsule assay for predictive chemosensitivity testing.

Antineoplastic Combined Chemotherapy Protocols↗
PubMed1986

Structure of the extra-membranous domain of the beta-subunit of (Na,K)-ATPase revealed by the sequences of its tryptic peptides.

Membrane bound dog kidney (Na,K)-ATPase was digested with trypsin. The peptides that were recovered in the supernatant were purified and sequenced. By comparing these results with the sequence of alpha- and human beta-subunits, the location of each of the peptides could be allotted. Both accessibility to trypsin and the facility of release into the water phase indicated that these peptides were derived from the exposed surface of the intact enzyme. The sequence, GXGXXG, reported in the Torpedo californica beta-subunit [(1986) FEBS Lett. 196, 315-319] was likely a mere coincidence with the sequence of the dinucleotide-binding site, since the last glycine was replaced by proline in the sequence of the dog beta-subunit. A disulfide bridge was found within a peptide derived from the beta-subunit. A possible model for the beta-subunit structure is proposed.

Amino Acid Sequence↗
PubMed1986

Molecular cloning and sequence analysis of human Na,K-ATPase beta-subunit.

We have isolated a cDNA clone for the beta-subunit of HeLa cell Na,K-ATPase, containing a 2208-base-pair cDNA insert covering the whole coding region of the beta-subunit. Nucleotide sequence analysis revealed that the amino acid sequence of human Na,K-ATPase exhibited 61% homology with that of Torpedo counterpart (Noguchi et al. (1986) FEBS Lett. in press). A remarkable conservation in the nucleotide sequence of the 3' non-coding region was detected between the human and Torpedo cDNAs. RNA blot hybridization analysis revealed the presence of two mRNA species in HeLa cells. S1 nuclease mapping indicated that they were derived from utilization of two distinct polyadenylation signals in vivo. Total genomic Southern hybridization indicated the existence of only a few, possibly one set of gene encoding the Na,K-ATPase beta-subunit in the human genome.

Amino Acid Sequence↗
PubMed1986

Primary structure of the beta-subunit of Torpedo californica (Na+ + K+)-ATPase deduced from the cDNA sequence.

DNA complementary to the Torpedo californica electroplax mRNA coding for the beta-subunit of (Na+ + K+)-ATPase has been cloned by screening a cDNA library with an oligodeoxyribonucleotide probe. Nucleotide sequence analysis of the cloned cDNA has revealed that this polypeptide consists of 305 amino acid residues (including the initiating methionine). The transmembrane topology and the potential N-glycosylation sites of this polypeptide are discussed.

Amino Acid Sequence↗
PubMed1986

Enzymatic synthesis and some properties of a model primitive tRNA.

A model primitive tRNA with the nucleotide sequence GGCCAAAAAAAGGCCp was synthesized using T4 RNA ligase. The nucleotide sequence of this newly synthesized oligonucleotide was confirmed by ladder analysis of several enzymatic digestion products. The secondary structure of the oligonucleotide was examined by comparison of the products of its digestion by single- and double-strand-specific nucleases with those of the digestion of the intermediate oligonucleotide GGCCAAAAAAAOH. The results indicated that the two GGCC segments of the 5' and 3' ends of the model tRNA may form base pairs in solution. The same conclusion was derived from the result of affinity-column chromatography of the model oligonucleotide. When 32pGGCCAAAAAAAGGCCOH was passed through a poly(U)-agarose column, about 70% of the applied sample bound to the poly(U)-agarose. In contrast, when the model oligonucleotide was passed through a poly(C)-agarose column, only 15% of the sample bound to the poly(C)-agarose. These results indicate that the newly synthesized oligonucleotide adopts a hairpin structure in solution. Two aspects of a potential biological activity of the synthetic model tRNA were examined. It was found that the oligonucleotide can bind to poly(U)-programmed 30S ribosomes and is recognized by Q beta replicase as a template for RNA synthesis.

Base Sequence↗
PubMed1986

The active site structure of Na+/K+-transporting ATPase: location of the 5'-(p-fluorosulfonyl)benzoyladenosine binding site and soluble peptides released by trypsin.

When the dog kidney Na+/K+-transporting ATPase (EC 3.6.1.37, formerly EC 3.6.1.3) was labeled with an ATP analogue, 5'-(p-fluorosulfonyl)benzoyladenosine (FSBA), there was a concomitant loss of ATPase activity. The presence of ATP protected the enzyme from both labeling and inactivation. The ATP-sensitive incorporation of FSBA is associated only with modification of the alpha subunit from which two labeled tryptic peptides were purified and sequenced. To establish any regions of the enzyme protruding from the membrane, the native Na+/K+-transporting ATPase from the electric ray, Torpedo californica, was treated with trypsin; and four peptides, which were released into the water phase, were purified and sequenced. A comparison of the peptide sequences with the deduced amino acid sequences of the DNA coding for the alpha subunit of T. californica and sheep kidney reveal the following. (i) FSBA-labeled peptides from the dog kidney enzyme are located in the central hydrophilic domain and show almost complete sequence homology with the same region in the alpha subunit from the electric ray and sheep kidney. Furthermore, the sequence homology of one of the two labeled peptides can be extended to the sarcoplasmic Ca2+-transporting ATPase and B subunit of Escherichia coli K+-transporting ATPase. (ii) Three trypsin-exposed peptides are found in the central hydrophilic domain, and one peptide is in the hydrophilic segment near the C terminus of the alpha subunit. (iii) The active center of Na+/K+-transporting ATPase is likely to be constructed from at least four different stretches in the primary sequence and, irrespective of the different specificity of cations, the various cation transport ATPases that form phosphorylated enzyme appear to have a common structure at the catalytic site for ATP hydrolysis.

Adenosine↗
PubMed1986

Primary structure of the alpha-subunit of human Na,K-ATPase deduced from cDNA sequence.

Clones carrying cDNA sequences for the alpha-subunit of the Na,K-ATPase from HeLa cells have been isolated. Nucleotide sequence analysis of the cloned cDNA has revealed the primary structure of this polypeptide, which consists of 1,023 amino acids. The alpha-subunit of the human Na,K-ATPase exhibited 87% homology with its Torpedo counterpart and 98% homology with its sheep counterpart. The six putative transmembrane segments M1-M6 showed higher conservation than the total segments. Total genomic Southern hybridization indicated the existence of at most two copies, possibly only one, of the gene encoding the Na,K-ATPase alpha-subunit in the human genome.

Amino Acid Sequence↗
PubMed1985

Protective effect of Na+ and K+ against inactivation of (Na+ + K+)-ATPase by high concentrations of 2-mercaptoethanol at high temperatures.

Purified dog kidney (Na+ + K+)-ATPase (EC 3.6.1.3) was inactivated with high concentrations of 2-mercaptoethanol at 50-55 degrees C. The inactivation was prevented by NaCl or KCl, with KCl being more effective than NaCl (the former ion being about one order more efficient under a typical set of experimental conditions). A disulfide bond in the beta-subunit of the enzyme protein was prevented from reductive cleavage by NaCl or KCl in accordance with protection of the enzyme activity. Choline chloride did not exert a significant protective effect over a similar concentration range. (Na+ + K+)-ATPase was also inactivated with high concentrations of 2-mercaptoethanol in the presence of low concentrations of dodecyl sulfate. This inactivation was also prevented by NaCl or KCl, with the latter being again more efficient than the former. These results indicate that Na+ and K+ bound to their respective ion-binding sites on the alpha-subunit exert a protective effect on a disulfide bond on the beta-subunit. This suggests some sort of interaction between the alpha- and the beta-subunits.

Animals↗