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Biomedical subjects

N Otsu

Publications and source records attributed to N Otsu.

6 recordsLinked to original sources
PubMed1991

[Aging effects on blood biochemical parameters in aged women: a longitudinal study using principal component analysis].

In order to examine the aging effects on blood biochemical parameters, 25 aged females (70 +/- 8 years old at the beginning of this investigation) were studied prospectively for 7 years. Biochemical parameters were measured in 1982, 1985, 1987, and 1989. Component scores were obtained by principal component analysis applied to all of these 100 data. The data of 13 biochemical parameters and 4 component scores were analyzed for aging, cohort, and time effects by utilizing 3 types of approach i.e., longitudinal, cross-sectional, and time-series. Positive aging effects were observed on blood urea nitrogen and 4th component score. Fourth component score had positive relations to blood urea nitrogen and total bilirubin, and a negative relation to total protein. This 4th component score increased with longitudinal age changes among all cohorts divided by decade, and it increased markedly over 70 years old. These results suggest that the aging effects on biochemical parameters are related with both the decrease in glomerular and hepatocellular functions and the increase in breakdown of tissue protein.

Aged↗
PubMed1990

[Immunoelectron microscopic studies on the localization of creatine kinase M in normal and ischemic myocardial cells].

The localization of creatine kinase M (CK-M) in both normal and acute ischemic canine myocardial cells was studied by immunoelectron microscopy using the anti-CK-M Fab'-horseradish peroxidase conjugate. Myocardial ischemia was induced by occlusion of the left anterior descending coronary artery for 15, 60, or 180 minutes. In the normal myocardial cells, CK-M was localized mostly in the A-band and some in the Z-line, M-line, sarcolemmal membrane, and membrane of sarcoplasmic reticulum. Most CK-M in the A-band appeared to associate with thick fibers. This finding strongly suggests that the CK associated with thick fibers may be the enzyme to rephosphorylate ADP produced by myosin ATPase. In 15 minutes of myocardial ischemia, CK-M showed only minimal changes in its location, i.e., almost similar to normal, indicating that the CK in the A-band still has the ability to couple with myosin ATPase. However, in 60 and 180 minutes of ischemia, the A-band CK dissociated markedly from thick fibers, diffused to the I-band and leaked out to the intercellular spaces. These results suggest that the dissociation and disappearance of the A-band CK from thick fibers induced by progress of myocardial ischemia disrupt the myocardial energy transport system via CK reaction, and lead to the irreversible injury of myocardial cells.

Adenosine Triphosphate↗
PubMed1989

Immunocytochemical localization of creatine kinase M in canine myocardial cells: most creatine kinase M is distributed in the A-band.

The localization of creatine kinase (CK) M in canine myocardium was immunocytochemically studied by a direct immunoperoxidase method. Specific antiserum against CK-M was produced in rabbits immunized with canine CK-MM. An anti-CK-M Fab'-horseradish peroxidase conjugate was prepared by the maleimide method. Frozen sections prepared from fixed canine myocardium were stained with the conjugate and observed by light and electron microscopy. In light microscopy of longitudinal sections, CK-M showed a cross-striated pattern consisting of distinct broad and narrow brown bands. Immunoelectron microscopy revealed that the regions of the broad and narrow brown bands corresponded to the A-band and the Z-line, respectively. Most CK-M in the A-band was associated with the thick fibers, and a small amount of CK-M was found in the M-line. These findings suggest that ATP regeneration from the ADP produced by myosin ATPase is related to the participation of this CK associated with the thick fibers rather than that of the M-line-bound CK. Creatine kinase M was also found in the sarcolemmal membrane, the membranes of the sarcoplasmic reticulum, and the mitochondrial outer and inner membranes. This report provides new information for understanding the physiological role of the phosphorylcreatine shuttle in the myocardial energy transport system.

Animals↗
PubMed1985

Abnormal lactate dehydrogenase isoenzyme in serum and tumor tissue of a patient with neuroblastoma.

Serum and tumor tissue of a patient with neuroblastoma contained an abnormal isoenzyme of lactate dehydrogenase (LDH; EC 1.1.1.27), which, on agarose gel electrophoresis, migrated between LDH-2 and LDH-3 with a mobility the same as that of the extra LDH isoenzyme found in normal human erythrocytes. On surgical removal of the tumor, the high total LDH activity (775 U/L) in the serum of the patient rapidly decreased to normal (70-220 U/L), and the abnormal LDH isoenzyme was no longer detected. The total LDH activity of the abnormal LDH isoenzyme per gram of hemoglobin in the tumor tissue was 26 times that of erythrocytes, suggesting that the abnormal isoenzyme originated mainly from the tumor cells themselves rather than the erythrocytes contained in the tumor tissue. This first report on the appearance of the abnormal LDH isoenzyme in a patient with neuroblastoma suggests that this abnormal LDH isoenzyme may have some significance as a marker enzyme for neurogenic tumors.

Abdominal Neoplasms↗