Search Results

You are looking at 1 - 4 of 4 items for

  • Author or Editor: N. Fujii x
  • Refine by Access: All Content x
Clear All Modify Search


In this work, we determined the levels of trace metals in protein fractions isolated from rock oysters by neutron activation analysis (NAA) and particle induced X-ray emission (PIXE). Proteins were extracted from mantles and hepatopancreases of rock oysters and fractionated by size-exclusion high performance liquid chromatography (HPLC). The protein fractions from mantles and hepatopancreases are found to be abundant in Fe, Cu, Zn, Mn, Pb, and Ag. HPLC profiles of Fe, Cu, Zn, and Ag indicate that those elements are bound to proteins extracted from mantles and hepatopancreases.

Restricted access


We have investigated the concentrations of REEs in fern leaves collected indifferently to the fern species from 9 sampling sites in Japan using INAA. The results indicated a large variation in the values obtained between fern leaves. In the present investigation we applied the same analytical method on the samples (Blechnaceae, a kind of fern, mature and developing leaves were collected from the same plant) restrictively gathered from the University Forests in Ashiu, Kyoto University. It was demonstrated that the variations in the REE concentrations decreased by one to two order of magnitude, and that the REE contents in developing leaves were also one to two orders of magnitude lower than those in mature leaves. It can be considered that fern accumulates REEs with their growth stages.

Restricted access
Journal of Radioanalytical and Nuclear Chemistry
Authors: M. Koyama, J. Takada, K. Kamiyama, N. Fujii, J. Inoue, K. Issiki, and E. Nakayama


In order minimize the possible contamination during storing and pre-treatment of such pure samples as ice and snow collected in Antarctica, trace elements in experimental tools such as bottles, beakers, tubings and filters were determined by neutron activation analysis. By using well certified tools, ice and snow samples from Antarctica and high mountains in China and in Japan were analyzed. Relative concentrations of volatile elements such as Zn, Cd, As, Sb or Ag to Al or Fe which are major components in the earth crust were found to be 10 to 1000 times higher than in the ordinary soil for the samples from Antarctica and Mt. Naimonanyi in China.

Restricted access
Physiology International
Authors: M. Nakamura, N. Satoh, H. Tsukada, T. Mizuno, W. Fujii, A. Suzuki, S. Horita, M. Nangaku, and M. Suzuki



Acid-base transport in renal proximal tubules (PTs) is mainly sodium-dependent and conducted in coordination by the apical Na+/H+ exchanger (NHE3), vacuolar H+-adenosine triphosphatase (V-ATPase), and the basolateral Na+/HCO3 - cotransporter. V-ATPase on PTs is well-known to play an important role in proton excretion. Recently we reported a stimulatory effect of insulin on these transporters. However, it is unclear whether insulin is involved in acid-base balance in PTs. Thus, we assessed the role of insulin in acid-base balance in PTs.


V-ATPase activity was evaluated using freshly isolated PTs obtained from mice, and specific inhibitors were then used to assess the signaling pathways involved in the observed effects.


V-ATPase activity in PTs was markedly enhanced by insulin, and its activation was completely inhibited by bafilomycin (a V-ATPase-specific inhibitor), Akt inhibitor VIII, and PP242 (an mTORC1/2 inhibitor), but not by rapamycin (an mTORC1 inhibitor). V-ATPase activity was stimulated by 1 nm insulin by approximately 20% above baseline, which was completely suppressed by Akt1/2 inhibitor VIII. PP242 completely suppressed the insulin-mediated V-ATPase stimulation in mouse PTs, whereas rapamycin failed to influence the effect of insulin. Insulin-induced Akt phosphorylation in the mouse renal cortex was completely suppressed by Akt1/2 inhibitor VIII and PP242, but not by rapamycin.


Our results indicate that stimulation of V-ATPase activity by insulin in PTs is mediated via the Akt2/mTORC2 pathway. These results reveal the mechanism underlying the complex signaling in PT acid-base balance, providing treatment targets for renal disease.

Restricted access