Zinc Binding Protein

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Tsutomu Chiba - One of the best experts on this subject based on the ideXlab platform.

  • identification of xanthine dehydrogenase xanthine oxidase as a rat paneth cell Zinc Binding Protein
    Biochimica et Biophysica Acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

  • Identification of xanthine dehydrogenase/xanthine oxidase as a rat Paneth cell Zinc-Binding Protein.
    Biochimica et biophysica acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

Johannes M. Herrmann - One of the best experts on this subject based on the ideXlab platform.

  • the Zinc Binding Protein hot13 promotes oxidation of the mitochondrial import receptor mia40
    EMBO Reports, 2008
    Co-Authors: Nikola Mesecke, Karl Bihlmaier, Barbara Grumbt, Sebastian Longen, Nadia Terziyska, Kai Hell, Johannes M. Herrmann
    Abstract:

    A disulphide relay system mediates the import of cysteine-containing Proteins into the intermembrane space of mitochondria. This system consists of two essential Proteins, Mia40 and Erv1, which bind to newly imported Proteins by disulphide transfer. A third component, Hot13, was proposed to be important in the biogenesis of cysteine-rich Proteins of the intermembrane space, but the molecular function of Hot13 remained unclear. Here, we show that Hot13, a conserved Zinc-Binding Protein, interacts functionally and physically with the import receptor Mia40. It improves the Erv1-dependent oxidation of Mia40 both in vivo and in vitro. As a consequence, in mutants lacking Hot13, the import of substrates of Mia40 is impaired, particularly in the presence of Zinc ions. In mitochondria as well as in vitro, Hot13 can be functionally replaced by Zinc-Binding chelators. We propose that Hot13 maintains Mia40 in a Zinc-free state, thereby facilitating its efficient oxidation by Erv1.

  • The Zinc‐Binding Protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40
    EMBO reports, 2008
    Co-Authors: Nikola Mesecke, Karl Bihlmaier, Barbara Grumbt, Sebastian Longen, Nadia Terziyska, Kai Hell, Johannes M. Herrmann
    Abstract:

    A disulphide relay system mediates the import of cysteine-containing Proteins into the intermembrane space of mitochondria. This system consists of two essential Proteins, Mia40 and Erv1, which bind to newly imported Proteins by disulphide transfer. A third component, Hot13, was proposed to be important in the biogenesis of cysteine-rich Proteins of the intermembrane space, but the molecular function of Hot13 remained unclear. Here, we show that Hot13, a conserved Zinc-Binding Protein, interacts functionally and physically with the import receptor Mia40. It improves the Erv1-dependent oxidation of Mia40 both in vivo and in vitro. As a consequence, in mutants lacking Hot13, the import of substrates of Mia40 is impaired, particularly in the presence of Zinc ions. In mitochondria as well as in vitro, Hot13 can be functionally replaced by Zinc-Binding chelators. We propose that Hot13 maintains Mia40 in a Zinc-free state, thereby facilitating its efficient oxidation by Erv1.

Nikola Mesecke - One of the best experts on this subject based on the ideXlab platform.

  • the Zinc Binding Protein hot13 promotes oxidation of the mitochondrial import receptor mia40
    EMBO Reports, 2008
    Co-Authors: Nikola Mesecke, Karl Bihlmaier, Barbara Grumbt, Sebastian Longen, Nadia Terziyska, Kai Hell, Johannes M. Herrmann
    Abstract:

    A disulphide relay system mediates the import of cysteine-containing Proteins into the intermembrane space of mitochondria. This system consists of two essential Proteins, Mia40 and Erv1, which bind to newly imported Proteins by disulphide transfer. A third component, Hot13, was proposed to be important in the biogenesis of cysteine-rich Proteins of the intermembrane space, but the molecular function of Hot13 remained unclear. Here, we show that Hot13, a conserved Zinc-Binding Protein, interacts functionally and physically with the import receptor Mia40. It improves the Erv1-dependent oxidation of Mia40 both in vivo and in vitro. As a consequence, in mutants lacking Hot13, the import of substrates of Mia40 is impaired, particularly in the presence of Zinc ions. In mitochondria as well as in vitro, Hot13 can be functionally replaced by Zinc-Binding chelators. We propose that Hot13 maintains Mia40 in a Zinc-free state, thereby facilitating its efficient oxidation by Erv1.

  • The Zinc‐Binding Protein Hot13 promotes oxidation of the mitochondrial import receptor Mia40
    EMBO reports, 2008
    Co-Authors: Nikola Mesecke, Karl Bihlmaier, Barbara Grumbt, Sebastian Longen, Nadia Terziyska, Kai Hell, Johannes M. Herrmann
    Abstract:

    A disulphide relay system mediates the import of cysteine-containing Proteins into the intermembrane space of mitochondria. This system consists of two essential Proteins, Mia40 and Erv1, which bind to newly imported Proteins by disulphide transfer. A third component, Hot13, was proposed to be important in the biogenesis of cysteine-rich Proteins of the intermembrane space, but the molecular function of Hot13 remained unclear. Here, we show that Hot13, a conserved Zinc-Binding Protein, interacts functionally and physically with the import receptor Mia40. It improves the Erv1-dependent oxidation of Mia40 both in vivo and in vitro. As a consequence, in mutants lacking Hot13, the import of substrates of Mia40 is impaired, particularly in the presence of Zinc ions. In mitochondria as well as in vitro, Hot13 can be functionally replaced by Zinc-Binding chelators. We propose that Hot13 maintains Mia40 in a Zinc-free state, thereby facilitating its efficient oxidation by Erv1.

Yukari Morita - One of the best experts on this subject based on the ideXlab platform.

  • identification of xanthine dehydrogenase xanthine oxidase as a rat paneth cell Zinc Binding Protein
    Biochimica et Biophysica Acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

  • Identification of xanthine dehydrogenase/xanthine oxidase as a rat Paneth cell Zinc-Binding Protein.
    Biochimica et biophysica acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

Hiroshi Hiai - One of the best experts on this subject based on the ideXlab platform.

  • Identification of xanthine dehydrogenase/xanthine oxidase as a rat Paneth cell Zinc-Binding Protein.
    Biochimica et biophysica acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

  • identification of xanthine dehydrogenase xanthine oxidase as a rat paneth cell Zinc Binding Protein
    Biochimica et Biophysica Acta, 2001
    Co-Authors: Yukari Morita, Mitsutaka Sawada, Naoki Miyake, Hiroshi Hiai, Hiroshi Seno, Shigeo Takaishi, Hiroaki Fukuzawa, Tsutomu Chiba
    Abstract:

    Paneth cells are Zinc-containing cells localized in small intestinal crypts, but their function has not been fully elucidated. Previously, we showed that an intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, induced selective killing of Paneth cells, and purified a Zinc-Binding Protein in Paneth cells. In the present study, we further characterized one of these Proteins, named Zinc-Binding Protein of Paneth cells (ZBPP)-1. Partial amino acid sequences of ZBPP-1 showed identity with rat xanthine dehydrogenase (XD)/xanthine oxidase (XO). Anti-rat XD antibody (Ab) recognized ZBPP-1, and conversely anti ZBPP-1 Ab recognized 85 kDa fragment of rat XD in Western blotting. Messenger RNA and Protein levels of XD were consistent with our previous data on the fluctuation of Paneth cell population after dithizone injection. Thus, ZBPP-1 is an 85 kDa fragment of XD/XO in Paneth cells. XD/XO in Paneth cells may play important roles in intestinal function.

  • Monoclonal antibodies to a Zinc-Binding Protein of rat Paneth cells.
    Journal of Histochemistry and Cytochemistry, 1994
    Co-Authors: Mitsutaka Sawada, Y Horiguchi, P Abujiang, Naoki Miyake, Yukihiko Kitamura, Midorikawa O, Hiroshi Hiai
    Abstract:

    Paneth cells are morphologically well characterized but their function has been not elucidated. Previously, we identified and purified a 90 KD Zinc-Binding Protein (ZBPP-1) in rat intestine that was localized to Paneth cell granules, consistent with their high Zinc content. To further elucidate the structure and function of ZBPP-1, we immunized Balb/c mice with purified ZBPP-1 and identified four independent monoclonal antibodies (MAb) producing MAb ZIP-1 (IgM), ZIP-2 (IgG1), ZIP-3 (IgM), and ZIP-4 (IgM). Immunohistochemistry (IHC) and immunoelectron microscopy (IEM) with these MAb showed positive staining of Paneth cell cytoplasmic granules. MAb ZBPP-1 also stained a population of mononuclear cells in the lamina propria of digestive tract mucosa and a few cells in spleen, presumably a subset of macrophages. These MAb will provide a useful tool to study the function of Paneth cells in human health and disease, since they cross-reacted with human intestinal Paneth cells and mucosal mononuclear cells.

  • A Paneth cell specific Zinc-Binding Protein in the rat. Purification and immunohistochemical localization.
    Laboratory investigation; a journal of technical methods and pathology, 1993
    Co-Authors: Mitsutaka Sawada, M Nishikawa, T Adachi, O Midorikawa, Hiroshi Hiai
    Abstract:

    Background Paneth cells are Zinc-containing cells widely distributed in Lieberkuhn's crypts of small intestine in many species, but their function has remained obscure. Our previous study showed that a single intravenous injection of diphenylthiocarbazone (dithizone), a Zinc chelator, forms Zinc-dithizonate complexes in the cytoplasm of Paneth cells to ensure rapid and selective killing of the cells. Experimental design To verify the Proteins that selectively deleted from intestinal mucosa after dithizone treatment, intestinal Proteins from the rats with or without dithizone injection were compared in sodium dodecyl sulfate-polyacrylamide gel electrophoresis. One such Protein, a 90 kilodalton (kd) Protein, was purified to homogeneity from normal rat intestine. A polyclonal antiserum was prepared by immunizing a rabbit with purified 90 kd Protein to use in immunohistochemical study. Results Among several Proteins deleted after dithizone injection, a 90 kd Protein with an isoelectric point of 5.9 +/- 0.2, was purified to homogeneity from normal intestine by a combination of Zinc affinity column and electroelution. Immunohistochemistry with rabbit anti-90 kd antiserum showed that the cytoplasmic granules in Paneth cells were stained. After dithizone administration, the 90 kd Protein containing cells rapidly disappeared, but resumed as Paneth cells regenerated. Also positively stained with this antibody were a few mononuclear cells broadly distributed in the lamina propria of the digestive tract, but they were not affected by dithizone treatment. Conclusions A 90 kd Zinc-Binding Protein was identified and purified from rat Paneth cells that was deleted in dithizone-treated rat intestine. We propose to designate it as a Zinc-Binding Protein of Paneth cell.

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