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Articles by Y Kikuchi
Total Records ( 3 ) for Y Kikuchi
  K Harada , H Matsuoka , N Fujimoto , Y Endo , Y Hasegawa , A Matsuo , Y Kikuchi , T Matsumoto and M. Inoue
 

The localization of the type-2 angiotensin II receptor (AT2) in the adrenal glands of rats, guinea pigs, bovines, and humans was examined at the mRNA and protein levels. PCR products for AT2 were detected in the adrenal cortices and adrenal medullae of all the mammals examined with an RT-PCR technique. Three different anti-AT2 antibodies (Abs), whose specificity was confirmed in our hands, recognized a 50-kDa protein in the adrenal glands of the four mammals, and this recognition was abolished by the preabsorption of an Ab with an antigen. Immunoblotting and immunohistochemistry revealed that the 50-kDa protein was expressed consistently and variably in the adrenal cortices and medullae of various mammals, respectively. We conclude that the 50-kDa AT2 is consistently expressed in the adrenal cortex in a wide variety of mammals. (J Histochem Cytochem 58:585–593, 2010)

  Y Kikuchi , M Nakaya , M Ikeda , K Narita , M Takeda and M. Nishi
 

Background The mental health of nurses is an important issue.

Aims To examine relationships between effort–reward imbalance (ERI) and depression and anxiety in nurses of a Japanese general hospital.

Methods A self-report survey was conducted among 406 nurses. Work stress was measured using a Japanese version of the ERI scale. Depression and anxiety were assessed by an item of the QOL-26. Logistic regression analysis was used to determine the independent contribution of the effort–reward ratios or overcommitment to the depressive state.

Results Both higher effort–money ratio and higher overcommitment significantly correlated with the depressive state (OR: 2.75; 95% CI: 1.34–5.66 and OR: 1.27; 95% CI: 1.15–1.41, respectively).

Conclusions These findings suggest that in addition to effort–money ratio, overcommitment at work is an especially important issue that may be able to be managed in health promotion services for nurses in general hospitals.

  T Igawa , H Tsunoda , Y Kikuchi , M Yoshida , M Tanaka , A Koga , Y Sekimori , T Orita , Y Aso , K Hattori and M. Tsuchiya
 

Thrombopoietin receptor agonist humanized VB22B single-chain diabody (hVB22B (scFv)2) was found to be expressed as a mixture of two conformational isomers, a single-chain diabody form and a bivalent scFv form, which had different VH/VL (variable region of the heavy chain/light chain) association patterns. The single-chain diabody form showed significantly higher biological activity than the bivalent scFv form and, when incubated at elevated temperatures, exhibited novel isomerization to the inactive bivalent scFv form. Therefore, therapeutic development of hVB22B (scFv)2 would require separation of the purified single-chain diabody form from the mixture of the two conformational isomers and also inhibition of isomerization into an inactive bivalent scFv form during storage. Novel VH/VL interface engineering in hVB22 (scFv)2, in which hydrogen bonding between H39 and L38 was substituted with electrostatic interaction to enhance the desired VH/VL association and inhibit the undesired VH/VL association, enabled selective expression of the desired conformational isomer without any reduction in biological activity or thermal stability. Moreover, VH/VL interface-engineered hVB22 (scFv)2 was completely resistant to isomerization. Because the hydrogen bonding interaction between H39 and L38 and the surrounding residues are highly conserved in human antibody sequences, VH/VL interface engineering could be generally applied to various (scFv)2 molecules for selective expression and inhibition of the isomerization of conformational isomers.

 
 
 
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