JOURNAL OF THE KYORIN MEDICAL SOCIETY

[title in Japanese]

Article type: Cover
1999 Volume 30 Issue 3 Pages Cover9-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.Cover9

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[title in Japanese]

Article type: Cover
1999 Volume 30 Issue 3 Pages Cover10-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.Cover10

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Influence of Hyperthermia on the Contents of HSP, Fas, p53, p21, and pRB in Cytosol of Methyl Cholanthrene-induced Fibrosarcoma (Meth A) Cell Transplanted to BALB/c Mice

Hiroshi FURUYA

Article type: Article
1999 Volume 30 Issue 3 Pages 241-252
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.241

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In order to clarify the mechanism of the growth suppression of tumor induced by hyperthermia, the contents of stress protein, apoptosis-associated protein, and suppressive oncogene products, were determined in the cytosol fraction of methyl cholanthrene-induced fibrosarcoma (Meth A) cell, which was transplanted to BALB/c mice, by an enzyme-immuno dot-assay. The tumor-bearing mice were treated at 42±0.5℃ for 10 min once a week for three weeks. The results indicate that the hyperthermic treatment decreased the tumor growth rate and evoked a change in these protein contents in the cytosol. Among them, the contents of suppressive oncogene products, such as p53 and p21 were decreased in the cytosol fraction during the coarse of the treatment. This suggests that hyperthermia decreases the phosphorylation rate of pRB protein inducing active form of the protein.

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The Time Course of Bone Metabolic Markers in Untreated Female Wistar Rats

Shigeki OHMORI

Article type: Article
1999 Volume 30 Issue 3 Pages 253-260
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.253

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I studied the time course of bone metabolic markers in untreated female Wistar rats between 3 and 24 months of age. I used 20 untreated female Wistar rats for longitudinal study and 140 rats for cross-sectional study, totaling 160 rats. Items examined were osteo-calcin (OC), bone alkaline phosphatase (bone ALP), tartrate-resistant asid phosphatase (TrAcP), hydroxyproline (Hyp), pyridinoline (Pyr) and deoxypyridinoline (D-Pyr). In longitudinal study the levels of each bone metabolic marker reached the maximums in 3-month-old rats, then decreased thereafter. Levels of OC, bone ALP, Hyp and Pyr reached the minimums at 18 months of age. In cross-sectional study, the levels of each bone metabolic marker also reached the maximums in 3-month-old rats. Levels of OC, bone ALP, and Hyp reached the minimums at 16 months of age, while those of Pyr and D-Pyr reached the minimums at 24 months of age of rats. In female Wistar rats, bone turnover was most energetic around 3 months of age and lowest around 18 months of age. These results were similar to change in the levels of OC, bone ALP, Pyr and D-Pyr observed in female humans, who show markedly higher levels in infancy and rapidly decreased levels thereafter.

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The Mechanism of the Effect of Adrenocorticosteroid Hormone upon Pediatric Patients with Bronchial Asthma as Evidenced by Serum ECP Level and its Release from Eosinophilic Cells

Nobuo ISHIGAKI

Article type: Article
1999 Volume 30 Issue 3 Pages 261-269
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.261

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I studied 12 pediatric patients with status asthmaticus with intravenous administration of either hydrocortisone sodium succinate (HCSS) or prednisolone (PS) and determined serum eosinophil cationic protein (ECP) level before and 2 hours after injection along the course of the attack. Serum ECP level significantly decreased in 2 hours after injection of corticosteroids (HCSS or PS) and went up again in 24 hours. An in vitro mixing of PS into the blood from patients with status asthmaticus before or after its coagulation disclosed that PS inhibits the ECP release from the eosinophilic cells only when it is given before coagulation. Besides, HCSS inhibited the release of ECP from eosinopilic cells in a dose depended fashion. It seemed to inhibit the ECP release at the concentration of 1μg/ml but inhibited significantly at 5μg/ml. These results clearly indicate that corticosteroids immediately and dose dependently inhibits ECP release from eosinophilic cells before coagulation of blood.

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Synthesis of Adenosine 5'-[β-imidazolidate]diphosphate 2',3'-cycIic carbonate to Enable Probing of Phosphate Group-accepting Asp Residue of the P-type ATPase : Binding the Synthesized Compound to the ATP-binding Sites of Na^+, K^+-ATPase and Ca^<2+>-ATPase

Susumu MIKKAICHI

Article type: Article
1999 Volume 30 Issue 3 Pages 271-281
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.271

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I developed a plan to establish a fluorescent probe of the phosphate group-accepting Asp residue of the P-type ATPase. This type of probing requires the Asp residue to be activated. One compound expected to activate the Asp residue is adenosine 5'-[β-imidazolidate]diphosphate 2',3'-cyclic carbonate (ImADP-cc), which I synthesized in proportion to published procedures as a reference. The resultant compound was assayed for ATPase activity in order to determine if it bound to the ATP-binding site, leading to the activation of Asp residues of Na^+, K^+-ATPase and Ca^<2+>-ATPase, which are P-type ATPases. The ATPase was incubated at 23℃ with synthesized ImADP-cc in the presence of various ligands. After 1h, the incubation mixture was centrifuged, and then the residual ATPase activity was measured. The results indicated that Na^+, K^+-ATPase was inactivated by ImADP-cc in the presence of NaCl. Ca^<2+>-ATPase was also inactivated by ImADP-cc in the presence of CaCl_2. However, in the presence of ATP, these ATPases were not inactivated by ImADP-cc. Thus, the present results suggest that ImADP-cc binds to the ATP-binding site under appropriate conditions, leading to activation of the Asp residues of Na^+, K^+-ATPase and Ca^<2+>-ATPase.

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages 283-446
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.283

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages 447-469
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.447

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages 470-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.470_1

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages 470-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.470_2

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages 470-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.470_3

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages App8-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.App8

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages App9-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.App9

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[title in Japanese]

Article type: Appendix
1999 Volume 30 Issue 3 Pages App10-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.App10

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[title in Japanese]

Article type: Cover
1999 Volume 30 Issue 3 Pages Cover11-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.Cover11

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[title in Japanese]

Article type: Cover
1999 Volume 30 Issue 3 Pages Cover12-
Published: September 30, 1999
Released on J-STAGE: February 13, 2017

DOIhttps://doi.org/10.11434/kyorinmed.30.Cover12

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