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Hiromi Ito - One of the best experts on this subject based on the ideXlab platform.

  • lectin inhibits Antigen Antibody Reaction in a glycoform specific manner application for detecting α2 6sialylated carcinoembryonic Antigen
    Proteomics, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

  • Lectin inhibits Antigen–Antibody Reaction in a glycoform‐specific manner: Application for detecting α2,6sialylated‐carcinoembryonic Antigen
    PROTEOMICS, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

  • lectin dependent inhibition of Antigen Antibody Reaction application for measuring α2 6 sialylated glycoforms of transferrin
    Journal of Biochemistry, 2013
    Co-Authors: Kyoka Hoshi, Hiromi Ito, Yoshinobu Kariya, Kiyomitsu Nara, Kana Matsumoto, Masamichi Nagae, Yoshiki Yamaguchi, Madoka Nakajima, Masakazu Miyajima, Hajime Arai
    Abstract:

    We developed a high-throughput Enzyme-linked immunosorbent assay (ELISA) for measuring α2,6-sialylated transferrin (Tf), based on inhibition of anti-Tf Antibody binding to α2,6-sialylated Tf by a lectin, Sambucus sieboldiana Agglutinin (SSA). The inhibition was not observed with other glycoforms, such as periodate-treated, sialidase-treated and sialidase/galactosidase-treated Tf, suggesting that the assay was glycoform specific. This finding was applied to an automated latex-agglutination immunoassay, using SSA lectin as an inhibitor (SSA-ALI). The concentration of α2,6-sialylated Tf measured by SSA-ALI in human cerebrospinal fluid was correlated with that of ELISA (r2 = 0.8554), previously developed for measuring α2,6-sialylated Tf.

Yasuhiro Hashimoto - One of the best experts on this subject based on the ideXlab platform.

  • lectin inhibits Antigen Antibody Reaction in a glycoform specific manner application for detecting α2 6sialylated carcinoembryonic Antigen
    Proteomics, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

  • Lectin inhibits Antigen–Antibody Reaction in a glycoform‐specific manner: Application for detecting α2,6sialylated‐carcinoembryonic Antigen
    PROTEOMICS, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

Yuehe Lin - One of the best experts on this subject based on the ideXlab platform.

  • microfabricated renewable beads trapping releasing flow cell for rapid Antigen Antibody Reaction in chemiluminescent immunoassay
    Analytical Chemistry, 2011
    Co-Authors: Guocheng Shao, Jun Wang, Wanjun Wang, Yuehe Lin
    Abstract:

    A renewable flow cell integrating a microstructured pillar-array filter and a pneumatic microvalve was microfabricated to trap and release beads. A bead-based immunoassay using this device was also developed. This microfabricated device consists of a microfluidic channel connecting to a beads chamber in which the pillar-array filter is built. Underneath the filter, there is a pneumatic microvalve built across the chamber. Such a device can trap and release beads in the chamber by “closing” or “opening” the microvalve. On the basis of the pneumatic microvalve, the device can trap beads in the chamber before performing an assay and release the used beads after the assay. Therefore, this microfabricated device is suitable for “renewable surface analysis”. A model analyte, 3,5,6-trichloropyridinol (TCP), was chosen to demonstrate the analytical performance of the device. The entire fluidic assay process, including beads trapping, immuno binding, beads washing, beads releasing, and chemiluminesence signal coll...

Kyoka Hoshi - One of the best experts on this subject based on the ideXlab platform.

  • lectin inhibits Antigen Antibody Reaction in a glycoform specific manner application for detecting α2 6sialylated carcinoembryonic Antigen
    Proteomics, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

  • Lectin inhibits Antigen–Antibody Reaction in a glycoform‐specific manner: Application for detecting α2,6sialylated‐carcinoembryonic Antigen
    PROTEOMICS, 2016
    Co-Authors: Hiromi Ito, Kyoka Hoshi, Fumihiko Osuka, Mitsukazu Gotoh, Takuro Saito, Hiroshi Hojo, Rei Suzuki, Hiromasa Ohira, Takashi Honda, Yasuhiro Hashimoto
    Abstract:

    Carcinoembryonic Antigen (CEA) is a glycoprotein marker, which is widely used for diagnosing various cancers, especially colon adenocarcinoma. In addition, CEA mediates homotypic adhesion of colon adenocarcinoma cells, which appears to favor hematogenous metastasis. CEA carries α2,6sialyl residues on its N-glycans whereas a normal counterpart, normal faecal Antigen-2, does α2,3sialyl residues, suggesting that cancer specific  α2,6sialylation on CEA may play a role for cell invasion and metastasis. Here we report a simple and rapid estimation of α2,6sialyled-CEA in detergent extracts from formalin fixed colon adenocarcinoma by “lectin inhibition”. In the lectin inhibition method, Sambucus sieboldiana Agglutinin (SSA) lectin, an α2,6sialic acid binder, was used as a glycoform specific inhibitor for Antigen-Antibody Reaction in ELISA. Detergent extracts from colon adenocarcinoma showed a fair amount of ELISA signal in the absence of SSA whereas the signal was markedly reduced (45∼74%) in the presence of SSA, suggesting that the extracts contains α2,6sialyled-CEA. The presence of α2,6sialyled-CEA in the extracts was confirmed by lectin microarray, in which SSA, Sambucus nigra agglutinin, and Trichosanthes japonica agglutinin I lectins were used as α2,6sialyl-binders. Thus lectin inhibition is a simple and rapid method for detecting α2,6sialyled-CEA even in crude detergent extracts from formalin-fixed adenocarcinoma tissue. This article is protected by copyright. All rights reserved

  • lectin dependent inhibition of Antigen Antibody Reaction application for measuring α2 6 sialylated glycoforms of transferrin
    Journal of Biochemistry, 2013
    Co-Authors: Kyoka Hoshi, Hiromi Ito, Yoshinobu Kariya, Kiyomitsu Nara, Kana Matsumoto, Masamichi Nagae, Yoshiki Yamaguchi, Madoka Nakajima, Masakazu Miyajima, Hajime Arai
    Abstract:

    We developed a high-throughput Enzyme-linked immunosorbent assay (ELISA) for measuring α2,6-sialylated transferrin (Tf), based on inhibition of anti-Tf Antibody binding to α2,6-sialylated Tf by a lectin, Sambucus sieboldiana Agglutinin (SSA). The inhibition was not observed with other glycoforms, such as periodate-treated, sialidase-treated and sialidase/galactosidase-treated Tf, suggesting that the assay was glycoform specific. This finding was applied to an automated latex-agglutination immunoassay, using SSA lectin as an inhibitor (SSA-ALI). The concentration of α2,6-sialylated Tf measured by SSA-ALI in human cerebrospinal fluid was correlated with that of ELISA (r2 = 0.8554), previously developed for measuring α2,6-sialylated Tf.

Shinya Toyokuni - One of the best experts on this subject based on the ideXlab platform.

  • intermittent microwave irradiation facilitates Antigen Antibody Reaction in western blot analysis
    Methods of Molecular Biology, 2009
    Co-Authors: Yuting Liu, Shinya Toyokuni
    Abstract:

    We established a shortened protocol for western blot analysis using intermittent microwave irradiation. With this method, the procedure is completed within 1 h after applying the primary Antibody, and thus greatly saves time. This procedure appears to be applicable to any Antibody based on our experience of several years.

  • intermittent microwave irradiation facilitates Antigen Antibody Reaction in western blot analysis
    Pathology International, 2003
    Co-Authors: Shinya Toyokuni, Waka Kawaguchi, Shinya Akatsuka, Makoto Hiroyasu, Hiroshi Hiai
    Abstract:

    In the March 2002 issue of Pathology International , Li et al . presented the first report describing the use of intermittent microwave irradiation in Western blot analysis. 1 We have independently developed a more rapid Western blot protocol that we would like to introduce here. Specific Reaction between Antigen and Antibody can be visualized by various methods such as Western blot analysis and immunohistochemistry. Microwave radiation, an energy wave with a frequency of approximately 1–300 GHz, has been used not only for radar, cooking procedures and radio communication but also for pathological methods in Antigen retrieval from formaldehyde-fixed paraffin-embedded specimens. 2,3 Recently, intermittent microwave irradiation was also applied to the fluorescent in situ hybridization technique. 4