CHIBA Hirofumi

写真a

Affiliation

School of Medicine, Department of Respiratory Medicine and Allergology

Job title

Professor
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Education 【 display / non-display 】

  • 　
    -
    1999

    Sapporo Medical University  

  • 　
    -
    1999

    Sapporo Medical University  

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Degree 【 display / non-display 】

  • 博士（医学）

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Professional Memberships 【 display / non-display 】

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    日本内科学会 日本呼吸器学会

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Affiliation 【 display / non-display 】

  • Sapporo Medical University   School of Medicine, 3rd Dept.of Internal Medicine   Instructor  

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Research Interests 【 display / non-display 】

  • 内科学

  • 呼吸器学

  • 生化学

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Misc 【 display / non-display 】

  • Surfactant protein gene expressions for detection of lung carcinoma cells in peripheral blood

    O Yamamoto, H Takahashi, M Hirasawa, H Chiba, M Shiratori, Y Kuroki, S Abe

    RESPIRATORY MEDICINE ( W B SAUNDERS CO LTD )  99 ( 9 ) 1164 - 1174  2005.09

    　View Summary

    Background: Inflow of tumor cells to circulation is an essential step for metastasis of primary tumors. To know its state may contribute to therapeutic strategy. However, methodology to detect lung carcinoma cells floating in peripheral blood has not been established. Pulmonary surfactant protein (SP)-A, SP-C and Clara cells-10 kd protein (CC10) are specific to the lung and often expressed in primary lung carcinomas. We evaluated the worth of these gene expressions for the detection of carcinoma cells in peripheral blood. Methods: The expressions in 5 ml of venous blood were tested by RT-PCR. Ninety-nine patients with non-small cell lung carcinoma (NSCLC) and 17 with small cell lung carcinoma (SCLC) were compared to 13 with secondary lung tumor, 48 with nonmalignant respiratory diseases and 19 healthy volunteers. Results: The mRNA expressions of SP-A and SP-C were completely specific to NSCLC when compared to SCLC and secondary lung tumors. All of the healthy volunteers and patients with non-malignant respiratory diseases showed negative for these mRNA expressions, except for one sample. The positive rate of SP-A, SP-C and CC10 mRNA in patients with NSCLC was 33.3%, 14.1%, 3.3%, respectively. The rates of SP-A and SP-C mRNA were higher than that (11.1%) in CEA mRNA. The increased positive rate of mRNA of SP-A and SP-C was significantly dependent on the clinical stage and the existence of distant metastasis. Conclusion: These results demonstrate that the detection of mRNA of SP-A and SP-C would give clinicians valuable information suggesting the presence of blood-floating carcinoma cells as a step toward metastasis. (C) 2005 Elsevier Ltd. All rights reserved.

    DOI

  • Reduction of bleomycin induced lung fibrosis by candesartan cilexetil, an angiotensin II type 1 receptor antagonist.

    Thorax   59   31 - 8  2004

    DOI

  • Elevated serum surfactant protein A and D in a case of acute eosinophilic pneumonia.

    Masaru FUJII, Hiroshi TANAKA, Masami KAMEDA, Masanori FUJII, Shintaro TANAKA, Kensuke OHASHI, Hirofumi CHIBA, Hiroki TAKAHASHI, Shosaku ABE

    Intern Med   43 ( 5 ) 423 - 426  2004

    DOI PubMed CiNii

  • [The environmental risk factors for COPD--tobacco smoke, air pollution, chemicals]

    Nippon Rinsho   61   2101 - 6  2003

  • Human surfactant protein D (SP-D) binds Mycoplasma pneumoniae by high affinity interactions with lipids

    H Chiba, S Pattanajitvilai, AJ Evans, RJ Harbeck, DR Voelker

    JOURNAL OF BIOLOGICAL CHEMISTRY ( AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC )  277 ( 23 ) 20379 - 20385  2002.06

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    Increasing evidence now identifies surfactant protein D (SP-D) as an important element of the innate immune system of the lung. In this study, we examined the interactions of rat and human SP-D with the human pathogen, Mycoplasma pneumoniae. Rat and human SP-D bound the organism with high affinity in a reaction that required Ca2+ and was inhibited by EGTA. Membranes derived from the organism bound the proteins in a similar manner, except the rat SP-D also exhibited a significant level of Ca2+-independent binding. Pretreatment of membranes with proteases did not alter the Ca2+-dependent SP-D binding of membranes by either protein. Mannose, glucose, maltose, and inositol, at millimolar concentrations, competed for human SP-D binding to the bacterial membrane. Lipids extracted from membranes and separated by two-dimensional thin layer chromatography bound human SP-D with high affinity in a Ca2+-dependent reaction. A tandem mutant of SP-D with E321Q and N323D substitutions, failed to bind M. pneumoniae lipids, directly implicating the carbohydrate recognition domain in the interaction. The interaction of rat and human SP-D with M. pneumoniae was unaffected by the presence of surfactant lipids and the hydrophobic surfactant proteins. These findings demonstrate that M. pneumoniae is likely to be recognized by SP-D in the alveolar environment and that primary determinants recognized on the organism are lipid components of the cell membrane.

    DOI PubMed CiNii

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Research Projects 【 display / non-display 】

  • サーファクタントプロテインの肺内局所免疫応答 マイコプラズマ感染

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