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Articles by A Saito
Total Records ( 2 ) for A Saito
  K Sato , T Sato , J Furuse , H Kasugai , M Konishi , T Kosuge , A Saito , Y Sasaki , K Takasaki and T. Okusaka
  Objective

The aim of this study was to explore why patients accepted or declined to participate in a randomized clinical trial, which was subsequently discontinued because of a low recruitment rate.

Methods

Forty-one patients were invited to participate in a randomized clinical trial that aimed to compare local ablation therapies and surgery to treat small asymptomatic hepatocellular carcinomas. These patients were then asked to answer a questionnaire that assessed patient perception and reasons for accepting or declining to enroll in the randomized clinical trial. When patients had a strong preference for a specific treatment, the questionnaire assessed why, how and when they had chosen it.

Results

The response rate was 6/6 (100%) and 30/35 (86%) for the participant and non-participant groups, respectively. Among the 30 non-participants, 23 had a strong preference for local ablation therapies, which was less invasive and offered shorter hospitalization. Patient preference for a specific treatment often stemmed from their consultations with a clinician who referred them to a specialist hospital. Patients without strong preference for a specific treatment participated in the randomized clinical trial because of altruistic motivations.

Conclusion

When new treatments that are innovative and less burdensome become widespread, they are difficult to compare with standard therapy utilizing a well-designed randomized clinical trial. Consequently, when an innovative treatment is developed, investigators should consider designing a randomized clinical trial as early as possible.

  K Suga , A Saito , T Tomiyama , H Mori and K. Akagawa
 

In this study, we examined the interaction of Syntaxin 5L (Syx5L), a Syx5 isoform that has an N-terminal extension containing a di-arginine ER-retrieval motif, with presenilin (PS) and its effects on the processing of β-amyloid precursor protein (βAPP). Similar to Syx5, Syx5L bound to PS1 holoprotein but not to its N- or C-terminal fragments. Unlike Syx5, Syx5L overexpression did not cause marked accumulation of intracellular βAPP holoprotein, and did not inhibit amyloid β peptide (Aβ) secretion. Analyses using deletion mutants of Syx5L revealed that, in addition to the difference in the intracellular localization between the isoforms, the presence of the N-terminal extension in Syx5L was critical for suppressing its inhibition of βAPP processing. Treatment of cells that overexpressed Syx5L with brefeldin A, an inhibitor of transport from the ER to the Golgi compartments, resulted in substantial accumulation of intracellular βAPP holoprotein and reduction in the secretion of Aβ. Although Syx5 and Syx5L share lengthy regions of amino acid identity, they appear to play distinct roles in modulating the metabolism and trafficking of βAPP in the early secretory compartment.

 
 
 
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