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Tomohisa Ogawa - One of the best experts on this subject based on the ideXlab platform.

  • diversified biomineralization roles of pteria penguin pearl shell Lectins as matrix proteins
    International Journal of Molecular Sciences, 2021
    Co-Authors: Tomohisa Ogawa, Saho Sato, Rie Sato, Takako Naganuma, Kyosuke Yoshimi, Makoto Osada, Kayeu Liu, Shizuka Sakaue, Koji Muramoto
    Abstract:

    Previously, we isolated jacalin-related Lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the Plant Lectin family, jacalin-related β-prism fold Lectins (JRLs). While PPL3s and PPL4 shared only 35%-50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these Lectins and compared their biomineral functions. It was found that these Lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • novel matrix proteins of pteria penguin pearl oyster shell nacre homologous to the jacalin related β prism fold Lectins
    PLOS ONE, 2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Saho Sato, Rie Sato, Kyosuke Yoshimi, Koji Muramoto, Makoto Osada, Tomohisa Ogawa
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of α and γ subunits, and PPL2B is a homo-dimer of β subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity and molecular evolution of this Lectin family involved in the mollusk shell formation.

Takako Naganuma - One of the best experts on this subject based on the ideXlab platform.

  • diversified biomineralization roles of pteria penguin pearl shell Lectins as matrix proteins
    International Journal of Molecular Sciences, 2021
    Co-Authors: Tomohisa Ogawa, Saho Sato, Rie Sato, Takako Naganuma, Kyosuke Yoshimi, Makoto Osada, Kayeu Liu, Shizuka Sakaue, Koji Muramoto
    Abstract:

    Previously, we isolated jacalin-related Lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the Plant Lectin family, jacalin-related β-prism fold Lectins (JRLs). While PPL3s and PPL4 shared only 35%-50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these Lectins and compared their biomineral functions. It was found that these Lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • novel matrix proteins of pteria penguin pearl oyster shell nacre homologous to the jacalin related β prism fold Lectins
    PLOS ONE, 2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Saho Sato, Rie Sato, Kyosuke Yoshimi, Koji Muramoto, Makoto Osada, Tomohisa Ogawa
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of α and γ subunits, and PPL2B is a homo-dimer of β subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • Novel Matrix Proteins of Pteria penguin Pearl Oyster Shell Nacre Homologous to the Jacalin-Related b-Prism Fold Lectins
    2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Rie Sato, Kaiyue Liu, Saho Sato
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of a and c subunits, and PPL2B is a homo-dimer of b subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity an

Koji Muramoto - One of the best experts on this subject based on the ideXlab platform.

  • diversified biomineralization roles of pteria penguin pearl shell Lectins as matrix proteins
    International Journal of Molecular Sciences, 2021
    Co-Authors: Tomohisa Ogawa, Saho Sato, Rie Sato, Takako Naganuma, Kyosuke Yoshimi, Makoto Osada, Kayeu Liu, Shizuka Sakaue, Koji Muramoto
    Abstract:

    Previously, we isolated jacalin-related Lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the Plant Lectin family, jacalin-related β-prism fold Lectins (JRLs). While PPL3s and PPL4 shared only 35%-50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these Lectins and compared their biomineral functions. It was found that these Lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • novel matrix proteins of pteria penguin pearl oyster shell nacre homologous to the jacalin related β prism fold Lectins
    PLOS ONE, 2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Saho Sato, Rie Sato, Kyosuke Yoshimi, Koji Muramoto, Makoto Osada, Tomohisa Ogawa
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of α and γ subunits, and PPL2B is a homo-dimer of β subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity and molecular evolution of this Lectin family involved in the mollusk shell formation.

Saho Sato - One of the best experts on this subject based on the ideXlab platform.

  • diversified biomineralization roles of pteria penguin pearl shell Lectins as matrix proteins
    International Journal of Molecular Sciences, 2021
    Co-Authors: Tomohisa Ogawa, Saho Sato, Rie Sato, Takako Naganuma, Kyosuke Yoshimi, Makoto Osada, Kayeu Liu, Shizuka Sakaue, Koji Muramoto
    Abstract:

    Previously, we isolated jacalin-related Lectins termed PPL2, PPL3 (PPL3A, 3B and 3C) and PPL4 from the mantle secretory fluid of Pteria penguin (Mabe) pearl shell. They showed the sequence homology with the Plant Lectin family, jacalin-related β-prism fold Lectins (JRLs). While PPL3s and PPL4 shared only 35%-50% homology to PPL2A, respectively, they exhibited unique carbohydrate binding properties based on the multiple glycan-binding profiling data sets from frontal affinity chromatography analysis. In this paper, we investigated biomineralization properties of these Lectins and compared their biomineral functions. It was found that these Lectins showed different effects on CaCO3 crystalization, respectively, although PPL3 and PPL2A showed similar carbohydrate binding specificities. PPL3 suppressed the crystal growth of CaCO3 calcite, while PPL2A increased the number of contact polycrystalline calcite composed of more than one crystal with various orientations. Furthermore, PPL4 alone showed no effect on CaCO3 crystalization; however, PPL4 regulated the size of crystals collaborated with N-acetyl-D-glucosamine and chitin oligomer, which are specific in recognizing carbohydrates for PPL4. These observations highlight the unique functions and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • novel matrix proteins of pteria penguin pearl oyster shell nacre homologous to the jacalin related β prism fold Lectins
    PLOS ONE, 2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Saho Sato, Rie Sato, Kyosuke Yoshimi, Koji Muramoto, Makoto Osada, Tomohisa Ogawa
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of α and γ subunits, and PPL2B is a homo-dimer of β subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity and molecular evolution of this Lectin family involved in the mollusk shell formation.

  • Novel Matrix Proteins of Pteria penguin Pearl Oyster Shell Nacre Homologous to the Jacalin-Related b-Prism Fold Lectins
    2014
    Co-Authors: Takako Naganuma, Wataru Hoshino, Yukihiro Shikanai, Rie Sato, Kaiyue Liu, Saho Sato
    Abstract:

    Nacreous layers of pearl oyster are one of the major functional biominerals. By participating in organic compound-crystal interactions, they assemble into consecutive mineral lamellae-like photonic crystals. Their biomineralization mechanisms are controlled by macromolecules; however, they are largely unknown. Here, we report two novel Lectins termed PPL2A and PPL2B, which were isolated from the mantle and the secreted fluid of Pteria penguin oyster. PPL2A is a hetero-dimer composed of a and c subunits, and PPL2B is a homo-dimer of b subunit, all of which surprisingly shared sequence homology with the jacalin-related Plant Lectin. On the basis of knockdown experiments at the larval stage, the identification of PPLs in the shell matrix, and in vitro CaCO3 crystallization analysis, we conclude that two novel jacalin-related Lectins participate in the biomineralization of P. penguin nacre as matrix proteins. Furthermore, it was found that trehalose, which is specific recognizing carbohydrates for PPL2A and is abundant in the secreted fluid of P. penguin mantle, functions as a regulatory factor for biomineralization via PPL2A. These observations highlight the unique functions, diversity an

Mark B Plenderleith - One of the best experts on this subject based on the ideXlab platform.

  • analysis of the unmyelinated primary sensory neurone projection through the dorsal columns of the rat spinal cord using transganglionic transport of the Plant Lectin bandeiraea simplicifolia i isoLectin b4
    Journal of the Neurological Sciences, 2004
    Co-Authors: Michelle B Gerke, Mark B Plenderleith
    Abstract:

    Abstract We have examined the projection of unmyelinated primary sensory neurones through the dorsal columns of the rat spinal cord using transganglionic transport of the Plant Lectin Bandeiraea simplicifolia I-isoLectin B 4 . A small volume of the Lectin was injected into the sciatic nerve of anaesthetised rats to label the central terminals of nociceptive primary sensory neurones. Following a survival period of 7 days, transverse and longitudinal sections of the superficial dorsal horn, dorsolateral funiculus and the dorsal columns from spinal segments L4 through to T13 were screened for Lectin transport using light and electron microscopy. Longitudinal sections of the thoraco-lumbar region of spinal cord were also examined for Lectin binding. Light and electron microscopy revealed transganglionically transported and bound Lectin in the superficial dorsal horn and dorsolateral funiculus of the L3 and L4 segments of spinal cord. However, no Lectin transport or binding was observed within the dorsal columns at any level of spinal cord examined. From these results, we suggest that the unmyelinated neurones within the dorsal columns do not express the binding site for BSI-B 4 and, as such, may be responsible for visceral rather than cutaneous sensation. In line with the theories regarding a postsynaptic dorsal column pathway, these results suggest that nociceptors that bind BSI-B 4 are not involved in a direct ascending projection through the dorsal columns.

  • analysis of the distribution of binding sites for the Plant Lectin bandeiraea simplicifolia i isoLectin b4 on primary sensory neurones in seven mammalian species
    Anatomical Record-advances in Integrative Anatomy and Evolutionary Biology, 2002
    Co-Authors: Michelle B Gerke, Mark B Plenderleith
    Abstract:

    The purpose of the present study was to investigate the binding patterns of the Plant Lectin Bandeiraea simplicifolia I-isoLectin B4 (BSI-B4) to sensory neurones in seven mammalian species. The dorsal root ganglia and spinal cords of three rats, mice, guinea pigs, rabbits, flying foxes, cats, and marmoset monkeys were screened for BSI-B4 using Lectin histochemistry. BSI-B4 binding was associated with the soma of predominantly small-diameter primary sensory neurones in the dorsal root ganglia and their axon terminals within laminae I and II of the superficial dorsal horn in all seven species. The similarities of Lectin binding patterns in each of these species suggest that the glycoconjugate to which BSI-B4 binds has a ubiquitous distribution in mammals, and supports the proposal that this Lectin may preferentially bind to a subpopulation of sensory neurones with a similar functional role in each of these species. Anat Rec 268:105–114, 2002. © 2002 Wiley-Liss, Inc.

  • Distribution of Binding Sites for the Plant Lectin Ulex europaeus Agglutinin I on Primary Sensory Neurones in Seven Different Mammalian Species
    The Histochemical Journal, 2002
    Co-Authors: Michelle B Gerke, Mark B Plenderleith
    Abstract:

    There is an increasing body of evidence to suggest that different functional classes of neurones express characteristic cell-surface carbohydrates. Previous studies have shown that the Plant Lectin Ulex europaeus agglutinin-I (UEA) binds to a population of small to medium diameter primary sensory neurones in rabbits and humans. This suggests that a fucose-containing glycoconjugate may be expressed by nociceptive primary sensory neurones. In order to determine the extent to which this glycoconjugate is expressed by other species, in the current study, we have examined the distribution of UEA-binding sites on primary sensory neurones in seven different mammals. Binding sites for UEA were associated with the plasma membrane and cytoplasmic granules of small to medium dorsal root ganglion cells and their axon terminals in laminae I–III of the grey matter of the spinal cord, in the rabbit, cat and marmoset monkey. However, no binding was observed in either the dorsal root ganglia or spinal cord in the mouse, rat, guinea pig or flying fox. These results indicate an inter-species variation in the expression of cell-surface glycoconjugates on mammalian primary sensory neurones.

  • binding sites for the Plant Lectin bandeiraea simplicifolia i isoLectin b4 are expressed by nociceptive primary sensory neurones
    Brain Research, 2001
    Co-Authors: Michelle B Gerke, Mark B Plenderleith
    Abstract:

    Circumstantial evidence suggests that binding sites for the Plant Lectin Bandeiraea simplicifolia I-isoLectin B4 are expressed by nociceptive primary sensory neurones. In order to test this hypothesis directly, we have used a combination of intracellular staining of functionally characterised primary sensory neurones and Lectin binding. Consistent with the hypothesis, none of the low threshold primary sensory neurones we sampled expressed Lectin binding sites, whilst a subpopulation of the nociceptive neurones did.