Histochemical detection of sugar residues in lizard teeth (Liolaemus gravenhorsti): a lectin-binding study
Abstract
The structural diversity of the many oligosaccharide chains of surface glycoconjugates renders them likely candidates for modulators of cell-interactions, cellular movements, differentiation, and cellular recognition. A selection of different lectins was used to investigate the appearance of cellular distribution and changes in sugar residues during tooth development in the polyphyodont lizard, Liolaemus gravenhorsti. Lectins from three groups were used: (1) N-acetylgalactosamine specificity: BS-1, PNA, RCA-(120); (2) N-acetylglucosamine specificity: EGA; and (3) fucose specificity: UEA 1 and LTA.. Digital images were processed using Scion Image. Grayscale graphics in each image were obtained. The lectins used showed a strong, wide distribution of the L-fucose and N-acetylgalactosamine at the cell surface and in the cytoplasm of multinucleate odontoclast cell, while mononuclear odontoclast cells showed no binding, suggesting some roles that the residues sugar might play in the resorption of dentine or with multinucleation of odontoclast after the attachment to the dentine surface in this polyphyodont species. Further studies must be planned to determine the specific identities of these glycoconjugates,and to elucidate the roles played by these sugar residues in the complex processes related to odontogenesis in polyphyodont species.
Más información
Título según WOS: | Histochemical detection of sugar residues in lizard teeth (Liolaemus gravenhorsti): a lectin-binding study |
Título según SCOPUS: | Histochemical detection of sugar residues in lizard teeth (Liolaemus gravenhorsti): A lectin-binding study |
Título según SCIELO: | Histochemical detection of sugar residues in lizard teeth (Liolaemus gravenhorsti): a lectin-binding study |
Título de la Revista: | BIOLOGICAL RESEARCH |
Volumen: | 33 |
Número: | 3-4 |
Editorial: | SOC BIOLGIA CHILE |
Fecha de publicación: | 2000 |
Página de inicio: | 215 |
Página final: | 226 |
Idioma: | English |
DOI: |
10.4067/S0716-97602000000300008 |
Notas: | ISI, SCIELO, SCOPUS |