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Articles by N Yamaguchi
Total Records ( 2 ) for N Yamaguchi
  T Shimada , N Yamaguchi , N Nishida , K Yamasaki , K Miura , S Katamine and H. Masuzaki
  Objectives

The squamous cell carcinoma antigen is considered the most accurate serologic tumor marker for uterine cervical carcinoma. However, serum squamous cell carcinoma antigen levels were found to correlate significantly with clinical severity of atopic dermatitis and chronic renal failure. The present study was conducted in patients with human papillomavirus 16 DNA-positive uterine cervical cancer to determine the plasma level of human papillomavirus 16 DNA and the diagnostic values of plasma human papillomavirus DNA in these patients.

Methods

Forty-three human papillomavirus 16-positive patients with cervical intraepithelial neoplasia or uterine cervical squamous cell carcinoma were recruited in this study. The diagnosis was cervical cancer in 20 patients, high-grade squamous intraepithelial lesions in 21, low-grade squamous intraepithelial lesions in 1 and negative for intraepithelial lesion or malignancy in 3 patients. Before any treatment, blood samples were collected from all patients. For analysis of human papillomavirus DNA in plasma of patients with cervical cancer, quantitative polymerase chain reaction fluorescent assay for human papillomavirus 16 was performed using human papillomavirus 16 primers and SYBR Green dye using the LightCycler 480 SW1.5 apparatus.

Results

Plasma human papillomavirus 16 DNA was detected in only 30.0% of the patients with human papillomavirus 16-positive cervical cancer and in none of normal controls. The copy number of plasma human papillomavirus 16 DNA was higher in patients with invasive cancer than in those with cervical intraepithelial neoplasia (CIN3), micro-invasive cancer and in normal individuals.

Conclusions

These results indicated that the plasma human papillomavirus DNA level could be potentially used as a marker of low-invasive cervical cancer tumors in patients with normal squamous cell carcinoma antigen levels before treatment.

  Y Mezaki , N Yamaguchi , K Yoshikawa , M Miura , K Imai , H Itoh and H. Senoo
 

Hepatic stellate cells (HSCs) are the major site of retinoid storage, and their activation is a key process in liver fibrogenesis. We have previously shown that expression of the retinoic acid receptor alpha (RAR) is upregulated in activated rat HSCs at a posttranscriptional level and that these RAR proteins showed a speckled distribution in the cytosol, despite their possession of a nuclear localization signal (NLS). In this report, we further characterize these cytosolic RAR proteins by using exogenously expressed RAR protein fragments or mutants tagged with a green fluorescent protein. Substitution of four amino acids, 161–164 from lysine to alanine, abolished the NLS. Exogenously expressed RAR protein fragments containing an NLS were localized exclusively in the nuclei of activated rat HSCs and never colocalized with the endogenous RAR proteins in the cytosol, suggesting that the NLS of endogenous RAR proteins is masked. Biochemical analysis showed that 65% of RAR proteins in activated HSCs were insoluble in a mixture of detergents. The insolubility of RAR proteins makes it difficult to identify RAR proteins in activated HSCs. Therefore, we propose that insoluble, speckled cytosolic distribution of RAR proteins represents a new marker of HSC activation. (J Histochem Cytochem 57:687–699, 2009)

 
 
 
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