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Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo.

Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Research Abstract Details 

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  • Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Abstract Text:

    kyung-ho jungKyung-Ho Jung,sung-hee songSung-Hee Song,jin-young paikJin-Young Paik,bong-ho kohBong-Ho Koh,yearn seong choeYearn Seong Choe,eun jung leeEun Jung Lee,byung-tae kimByung-Tae Kim,kyung-han leeKyung-Han Lee,kyung-ho jungKyung-Ho Jung,sung-hee songSung-Hee Song,jin-young paikJin-Young Paik,bong-ho kohBong-Ho Koh,yearn seong choeYearn Seong Choe,eun jung leeEun Jung Lee,byung-tae kimByung-Tae Kim,kyung-han leeKyung-Han Lee,

    Recent discoveries have identified endothelial cell-surface F(1)F(0) adenosine triphosphate (ATP) synthase as the key target for angiostatin (AST) action. As this enzyme is also present on tumor cells, we investigated whether radiolabeled AST may directly target cancer cell-surface ATP synthase in vitro and in vivo. METHODS: Cell-binding characteristics of (125)I-AST was evaluated on human umbilical vein endothelial (HUVE) and SNU-C5 colon carcinoma cells. The molecular target for binding was investigated with anti-ATP synthase antibodies and RGDyV. Biodistribution and imaging experiments were performed in mice xenografted with carcinoma and sarcoma tumors. Tumor localization of ATP synthase and exogenous AST was compared via double immunostaining. RESULTS: Both HUVE and SNU-C5 cells showed specific (125)I-AST binding that was dose-dependently inhibited by excess AST, with IC(50) values of 3.5 and 0.2 microM, respectively. Both cell types stained positive for ATP synthase and demonstrated an approximately 50% reduction in AST binding by antibodies against the alpha- and beta-subunit of the enzyme. (123)I-AST injected in mice allowed for the clear tumor visualization with significant tumor accumulation and uptake ratios. Immunostaining revealed a localization of exogenous AST to closely correlate to that of tumor-cell ATP synthase. CONCLUSIONS: AST can directly target tumor-cell ATP synthase, and AST imaging may thus be useful for monitoring tumor ATP synthase expression.

    Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Publishing Authors By Initials

    kh jungKH Jung,sh songSH Song,jy paikJY Paik,bh kohBH Koh,ys choeYS Choe,ej leeEJ Lee,bt kimBT Kim,kh leeKH Lee,kh jungKH Jung,sh songSH Song,jy paikJY Paik,bh kohBH Koh,ys choeYS Choe,ej leeEJ Lee,bt kimBT Kim,kh leeKH Lee,

    For similar abstracts research abstracts see: abstracts research

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    Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Journal Published:

    PUBLICATION TYPE: Research Support, Non-U.S. Gov

    Journal: Cancer biotherapy & radiopharmaceuticals

    VOLUME: 22

    Page Numbers: 704-12

    Journal Abbreviation: Cancer Biother. Radiopharm.

    ISSN: 1084-9785

    DAY: 5

    MONTH: Oct

    YEAR: 2007

    Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Information

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    LANGUAGE: eng

    NlmUniqueID: 9605408

    Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo. Keywords Mesh Terms:

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    Grant and Affiliation Information for Direct targeting of tumor cell F(1)F(0) ATP-synthase by radioiodine angiostatin in vitro and in vivo.

    AFFILIATION: Department of Nuclear Medicine, Samsung Medical Center, and Sungkyunkwan University School of Medicine, Seoul, Korea.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Cancer Biother Radiopharm

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