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Biomedical subjects

F Kishi

Publications and source records attributed to F Kishi.

140 records · Page 8Linked to original sources
PubMed1979

Gene expression in vitro of colicin El plasmid.

Among eighteen polypeptides synthesized in vitro from colicin El plasmid, one of the major products with a molecular weight of 59,000 was identified as colicin El by its immunological property, molecular size, and biological activity. In addition to this polypeptide, seven other polypeptides reacted with colicin El antiserum. Using EcoRI-cleaved colicin El DNA, a 56,000 dalton polypeptide of truncated colicin El was synthesized, but no polypeptide that reacted with colicin El antiserum was produced from SmaI-cleaved colicin El DNA. This fact indicates that the direction of transcription of colicin El structural gene is from SmaI site to EcoRI site in vitro. The immunity protein of a molecular weight of 14,300 and a component of relaxation proteins of a molecular weight of 64,000 were deduced by comparing the results of the gene expression in vitro of one-half (pAO100) and a quarter (pAO2) of colicin El plasmid. The directions of transcription-translation in the genes on the plasmid were discussed. The colicin El plasmid appears to have at least three transcriptional units.

Colicins↗
PubMed1978

Effect of CO2 on carbonic anhydrase activity and isozyme levels in respiratory failure.

The activity and the isozyme B and C levels of red cell carbonic anhydrase was examined before and during CO2 inhalation in 18 patients with chronic respiratory failure. Carbonic anhydrase B and C levels did not change during 5 min breathing of high (8-9%) and low (3-5%) CO2 mixture. Carbonic anhydrase activity decreased in patients with combined hypercarbia (Paco2 greater than or equal to 45 mmHg) and hypoxemia (Pao2 less than or equal to 60 mmHg). This was accompanied by an increase in red cell K+ content, 2, 3-DPG and Hct/Hb. The activity did not change in patients with only hypoxemia. Carbonic anhydrase activity and plasma HCO-3 concentration were positively correlated (r = 0.4, P less than 0.05). A significant inverse correlation was also found between changes in red cell K+ content and those in carbonic anhydrase activity (r = - 0.42, P less than 0.05). These results indicate that 1), there is a dissociation between activity and isozyme levels in red cell carbonic anhydrase during the initial 5 min of CO2 breathing in patients with combined hypercarbia and hypoxemia, and 2), there seems a linkage exists between K+ movement across the red cell membrane and carbonic anhydrase activity.

Carbon Dioxide↗
PubMed1975

Changes in potassium content of erythrocytes during exercise in man.

Factors affecting erythrocyte K+ content and plasma electrolytes during light exercise were examined in 8 normal subjects and 27 patients with chronic obstructive lung disease. The patients were classified into bronchitis, emphysema and intermediate groups. Arterial blood was obtained during rest, after 2, 5, and 7 min. of exercise on a bicycle ergometer (30 km/h without mechanical brake), and at 10 and 20 min. during recovery for analysis of PO2, PCO2, plasma H+, Na+, K+, and Cl(-), erythrocyte K+ content and whole blood lactate. Plasma H+ increased significantly in all subjects after 2 min. of exercise and PCO2 rose in normal, bronchitis, and emphysema groups during exercise, whereas PO2 did not change significantly. Plasma K+ rose promptly after the beginning of exercise and remained at high values during exercise. The rapid rise in PCO2 was associated with a significant decrease of calculated erythrocyte K+ in patients with chronic bronchitis. Although changes in plasma H+ were dependent on both PCO2 and lactate, erythrocyte K+ changes were significantly related only to changes in PCO2. These results indicate that the decrease in erythrocyte K+ is mainly controlled by changes in arterial PCO2 during light exercise in patients with chronic bronchitis.

Adult↗
PubMedDate not supplied

Identification of natural resistance-associated macrophage protein in peripheral blood lymphocytes.

Natural resistance-associated macrophage protein gene (Nramp) was isolated from the gene locus Lsh/Ity/Bcg, which regulates macrophage activation for antimicrobial activity against intracellular pathogens. The deduced protein sequence encodes an integral membrane protein that has structural homology with known prokaryotic and eukaryotic transport systems. In the present study, a polyclonal antibody was raised with the synthetic peptide of the carboxy-terminal 17 amino acids of human Nramp. The protein product of the gene is apparently present in human peripheral blood lymphocyte (PBL) as a 60 kD a protein recognized by the antibody, which is consistent with the calculated molecular mass. Bacterial lipopolysaccharide or interferon-gamma did not appear to stimulate the level of Nramp expression in PBL.

Amino Acid Sequence↗
PubMedDate not supplied

Complete nucleotide sequence of human NRAMP2 cDNA.

The mouse Lsh/Ity/Bcg locus regulates macrophage activation for antimicrobial activity against intracellular pathogens, and the Nramp1 gene was isolated as its candidate. In the present study, a full length cDNA for human NRAMP2 has been isolated and characterized. Nucleotide sequence analysis reveals that the cDNA, 4142 bp in length, coded for a protein of 561 amino acid residues with a molecular weight mass of 61,456. Predicted amino acid sequence analysis of the NRAMP2 molecule indicates that NRAMP1 and NRAMP2 sequences share 64% identical residues overall, whereas only 21% at the NH2-terminal cytoplasmic domain, where the NRAMP1 molecule was associated with microtubules, was found to be identical. This suggests that the NH2-terminal region of the NRAMP2 molecule may have a particular function, different from that of the NRAMP1 molecule.

Amino Acid Sequence↗
PubMedDate not supplied

Specific detection and quantitation of SCC antigen 1 and SCC antigen 2 mRNAs by fluorescence-based asymmetric semi-nested reverse transcription PCR.

Squamous cell carcinoma antigen (SCCA) is expressed in normal squamous epithelia and malignant squamous cell tissues. The serum level of SCCA has been used to evaluate treatment efficacy, clinical course of disease, and recurrence. SCCA is produced by at least two genes (SCCA1 and SCCA2); both of them have been located on chromosome 18q21.3. It has been difficult to examine the expression levels of SCCA1 and SCCA2 mRNAs separately because of their high homology at nucleotide level. In the present study, asymmetric semi-nested reverse transcription PCR, based on the principle of fluorescence energy transfer, enabled to quantitate the copy numbers of both SCCA1 and SCCA2 mRNAs. Using this method, the expression levels of these mRNAs were evaluated in normal and malignant squamous tissues. The copy number of SCCA2 mRNA was higher in malignant tissues than in normal tissues, while those of SCCA1 mRNA did not significantly differ between normal and malignant tissues. These data indicate that specific quantitation of the expression level of SCCA2 mRNA may be useful for the diagnosis and management of patients with squamous cell carcinoma.

Antigens, Neoplasm↗