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Articles by H Hamada
Total Records ( 2 ) for H Hamada
  K Matsumoto , A Oki , T Satoh , S Okada , T Minaguchi , M Onuki , H Ochi , S Nakao , M Sakurai , A Abe , H Hamada and H. Yoshikawa

Polymorphisms in cytokine genes can influence immune responses to human papillomavirus infection, possibly modifying risks of cervical cancer. Using an amplification refractory mutation system-polymerase chain reaction method, we analyzed a single nucleotide polymorphism (A/G) at position –1082 in interleukin-10 promoter region in 440 Japanese women: 173 women with normal cytology, 163 women with cervical intraepithelial neoplasia and 104 women with invasive cervical cancer. The carrier frequency of interleukin-10 –1082 G alleles associated with higher interleukin-10 production increased with disease severity: 9.8% for normal cytology; 19.6% for cervical intraepithelial neoplasia; 29.8% for invasive cervical cancer (P for trend <0.001). Among cytologically normal women, human papillomavirus infections were more common in those who were positive for an interleukin-10 –1082 G allele (P = 0.04). In conclusion, our data suggest that interleukin-10 –1082 gene polymorphism may serve as a marker of genetic susceptibility to cervical cancer among Japanese women.

  T Shibata , S Nagao , H Tai , S Nagatomo , H Hamada , H Yoshikawa , A Suzuki and Y. Yamamoto

Human adult haemoglobin (Hb A), a tetrameric oxygen transfer haemoprotein, has been recognized as an excellent model for investigating the structure–function relationships in allosteric proteins, and has been characterized exhaustively from both experimental and theoretical aspects. Despite the detailed structural and spectroscopic information available for the protein, functional properties have not been as fully elucidated as expected, and hence have remained unexplored. A major drawback for the functional characterization of Hb A is the lack of experimental techniques which enable quantitative characterization of functional properties of the individual subunits of the intact protein. In this study, we have developed techniques for determining the equilibrium constant of the acid–alkaline transition, usually represented as the ‘pKa’ value, in the individual subunits of the met-forms of Hb A (metHb A) and human foetal haemoglobin (metHb F). The pKa values of the individual subunits of metHb A and metHb F have been shown to constitute novel and highly sensitive probes for characterizing the effects of structural changes of not only the interfaces between the subunits within the protein, but also the contact between haem and the protein in the haem pocket. In addition, haem replacement studies of the proteins revealed that the contact between the haem peripheral vinyl side chain and the protein in the haem pocket is important for maintaining the non-equivalence in the haem environment between the subunits of Hb A and Hb F, which could be relevant to the cooperative ligand binding of the proteins.

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