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Biomedical subjects

T Hatayama

Publications and source records attributed to T Hatayama.

138 records · Page 8Linked to original sources
PubMed1977

Nucleotide sequence of a region in 23-S RNA adjacent to peptidyl transferase catalytic center of Escherichia coli ribosomes.

N-Iodoacetylphenylalanyl-tRNAPhe was used as an affinity label to localize the RNA components intimately involved in the catalytic center of Escherichia coli ribosomes. This analogue could alkylate the specific region of 23-S RNA that waslocated within 2000 nucleotides from the 3' terminus of the molecule. Sequence analysis revealed that the alkylation by the active substrate (N-iodoacetylphenylalanyl-tRNAPhe) was directed to 5'-terminal adenosine residue of a heptanucleotide, A-U-U-U-U-A-Gp, which seemed to be derived from a heptadecanucleotide, U-U-A-A-A-A-A-C-A-C-A-U-U-U-U-A-Gp, in the original 23-S RNA. The significance of the unique sequence in the ribosomal functions is discussed.

Acyltransferases↗
PubMed1975

Affinity labeling of the ribonucleic acid component adjacent to the peptidyl recognition center of peptidyl transferase in Escherichia coli ribosomes.

N-Iodacetylphenylalanyl-tRNA was used as an affinity label for localizing the RNA components intimately related to the peptidyl transferase activity of Escherichia coli ribosomesmthis analogue could specifically alkylate a unique nucleotide chain of 23-S RNA. The alkylation was strongly enhanced by poly(U), and was dependent on the presence of both 50- and 30-S subunits; Chloramphenicol inhibited the reaction, wheras blasticidin S stimulated it. The alkylated RNA base was found to be adenine. The nucleotide chain attacked by N-iodoacetylphenylalanyl-tRNA seemed to be localized at or near to the peptidyl recognition center of peptidyl transferase.

Acyltransferases↗
PubMed1975

Identification of the 30 S protein adjacent to peptidyl transferase catalytic center of Escherichia coli ribosomes.

Iodoacetylphenylalanyl-tRNAPhe was used as an affinity label to localize the ribosomal components involved in the peptidyl transferase catalytic center of Escherichia coli ribosomes. When labeling was carried out at pH 5.0, the affinity label could specifically label the ribosomal components which comprise the catalytic center. Analysis of ribosomal proteins which had reacted with the affinity label revealed that a 30 S subunit protein, S 20, was located at or near to the ribosomal binding site of the 3'-terminus of aminoacyl- or peptidyl-tRNA.

Acyltransferases↗
PubMedDate not supplied

Secretory IgA in saliva and academic stress.

Several reports have proposed that the concentration of secretory immunoglobulin A (S-IgA) in saliva is an indicator of psychological stress. With this in mind, we decided to examine it in 10 second year medical student volunteers at Kawasaki Medical School course between May 4 and July 13, 2000 and discussed the relationship between S-IbA and the stress from academic examinations. Saliva was collected three times (on rising, at forenoon, and at bedtime) every Thursday. During this period, sporadic academic examinations were held twice and term end examination occurred during the last two weeks. Results showed the concentration of S-IgA significantly higher at the on rising time-point than at the other two time-points. There was also a tendency for the S-IgA level in saliva to be higher on the day before academic examinations and during them and lower on the days between these examinations. In addition, daily variations in the S-IgA concentration sometimes seemed to be disturbed by other academic stress. Therefore it may be possible to use this measurement to monitor psychological stress in students and workers.

Adult↗
PubMedDate not supplied

Reduced function of CD4+25+ regulatory T cell fraction in silicosis patients.

The quality and quantity of CD4+25+ regulatory T cells (Treg) in silicosis patients (SIL) were examined and compared with results from healthy donors (HD) because SIL often develop autoimmune diseases along with pulmonary disorders. Peripheral blood mononuclear cells from 57 SIL and 50 HD were analyzed for Treg. Treg frequency and clinical parameters were subjected to a factor analysis. Treg and CD4+25- T cells (Tneg) from five HD and five SIL, sorted by flow-cytometer, were used for functional assays of Treg, the expression pattern of Treg specific genes (FoxP3, GITR and CTLA-4) and activation-related genes (CD122 and CD123). Although the actual frequency of Treg did not differ between SIL and HD, the age-corrected level was reduced in SIL. The factor analysis showed that Treg frequency was positively associated with the serum level of IL-2. The inhibitory effect of Treg on Tneg activation was decreased when the Treg:Tneg ratio was 1:1/4 to 1/2. In addition, Treg dominancy of FoxP3 and CTLA-4 expression and Tneg dominancy of CD132 expression found in HD were lost in SIL. These results indicated that the Treg fraction in SIL may be substituted with chronically activated T cells due to recurrent exposure to silica, resulting in a reduction in the frequency and function of Treg. Since the reduction of Treg may precede the clinical manifestation, as silicosis may be a pre-clinical status for autoimmune diseases, control of Treg function using cell and/or gene therapy may be a good way to manage autoimmune disease.

Aged↗
PubMedDate not supplied

Role of heat-shock proteins in the induction of thermotolerance in Chinese hamster V79 cells by heat and chemical agents.

To examine the involvement of heat shock proteins in the induction of thermotolerance in Chinese hamster V79 cells, thermotolerance was induced by heating of the cells at 42 degrees C for 4 h or at 44 degrees C for 20 min, or by treatment of the cells with 50 microM sodium arsenite for 3 h or 20 micrograms/ml puromycin for 4 h. Under unstressed conditions V79 cells synthesized constitutively three major heat-shock proteins, hsp70, hsp85 and hsp105. On exposure to conditions under which thermotolerance was induced, the synthesis of constitutive hsp70, hsp85 and hsp105 increased, but the inducible form of hsp70 was not synthesized, indicating that this inducible form was not necessary for the induction of thermotolerance. Although the amounts of heat-shock proteins synthesized in the cells that acquired thermotolerance were not always more than those synthesized constitutively in unstressed cells, the stressed cells synthesized heat-shock proteins (especially hsp70) preferentially over other proteins. As the level of hsp70 in the thermotolerant cells was almost the same as that in unstressed cells, the specific accumulation of hsp70 seemed not to be required for the acquisition of thermotolerance. From these findings it seemed likely that, for the induction of thermotolerance in V79 cells, hsp70 preferentially synthesized during or after the stress has an important function. Or the synthesis of heat shock proteins may not be important, and constitutively synthesized heat-shock proteins acquire a specific function during or after the stress.

Animals↗
PubMedDate not supplied

Characteristic synthesis and redistribution of 70 kd heat shock protein in thermotolerant Chinese hamster V79 cells.

Upon exposure to heat shock the increased rate of hsp70 synthesis decreased more rapidly in thermotolerant V79 cells than in the non-thermotolerant cells. However, the levels of hsp70 in the thermotolerant cells at 12 h after a heat shock were almost the same as those in the non-thermotolerant cells. On the other hand, the migration of hsp70 from cytoplasm to nucleoli after a heat shock was very rapid in both thermotolerant and non-thermotolerant cells, but hsp70 in the nucleoli disappeared faster in the thermotolerant cells than in the non-thermotolerant cells, and this coincided with the faster decline of hsp70 synthesis in the thermotolerant cells. For the characteristic distribution of hsp70, protein synthesis was not required. Furthermore, the induction and expression of thermotolerance by the cells were little affected by the inhibition of protein synthesis. Thus, the synthesis of hsp70 itself seemed not to be essential for the induction and expression of thermotolerance of the cells, although hsp70 may be essential for thermoresistance of cells. The rapid decrease of hsp70 synthesis and the rapid disappearance of hsp70 from the nucleoli after a heat shock may be essential for the expression of thermotolerance of the cells.

Animals↗