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Galectin-lattice sustains function of cationic amino acid transporter and insulin secretion of pancreatic ß cells.
Maeda, Kento; Tasaki, Masayoshi; Ando, Yukio; Ohtsubo, Kazuaki.
Afiliación
  • Maeda K; Department of Analytical Biochemistry;, Graduate School of Health Sciences, Kumamoto University, 4-24-1 Kuhonji, Chuo-Ku, Kumamoto 862-0976, Japan.
  • Tasaki M; Department of Morphological and Physiological Sciences, Graduate School of Health Sciences, Kumamoto University, 4-24-1 Kuhonji, Chuo-Ku, Kumamoto 862-0976, Japan.
  • Ando Y; Department of Neurology, Graduate School of Medical Sciences, Kumamoto University, Kumamoto 860-0811, Japan.
  • Ohtsubo K; Depatment of Amyloidosis Research, Nagasaki International University, Nagasaki 859-3243, Japan.
J Biochem ; 167(6): 587-596, 2020 Jun 01.
Article en En | MEDLINE | ID: mdl-31960919
Maintenance of cell surface residency and function of glycoproteins by lectins are essential for regulating cellular functions. Galectins are ß-galactoside-binding lectins and form a galectin-lattice, which regulates stability, clustering, membrane sub-domain localization and endocytosis of plasmalemmal glycoproteins. We have previously reported that galectin-2 (Gal-2) forms a complex with cationic amino acid transporter 3 (CAT3) in pancreatic ß cells, although the biological significance of the molecular interaction between Gal-2 and CAT3 has not been elucidated. In this study, we demonstrated that the structure of N-glycan of CAT3 was either tetra- or tri-antennary branch structure carrying ß-galactosides, which works as galectin-ligands. Indeed, CAT3 bound to Gal-2 using ß-galactoside epitope. Moreover, the disruption of the glycan-mediated bindings between galectins and CAT3 significantly reduced cell surface expression levels of CAT3. The reduced cell surface residency of CAT3 attenuated the cellular arginine uptake activities and subsequently reduced nitric oxide production, and thus impaired the arginine-stimulated insulin secretion of pancreatic ß cells. These results indicate that galectin-lattice stabilizes CAT3 by preventing endocytosis to sustain the arginine-stimulated insulin secretion of pancreatic ß cells. This provides a novel cell biological insight into the endocrinological mechanism of nutrition metabolism and homeostasis.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Sistemas de Transporte de Aminoácidos Básicos / Galectina 2 / Células Secretoras de Insulina / Secreción de Insulina Límite: Animals Idioma: En Revista: J Biochem Año: 2020 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Transducción de Señal / Sistemas de Transporte de Aminoácidos Básicos / Galectina 2 / Células Secretoras de Insulina / Secreción de Insulina Límite: Animals Idioma: En Revista: J Biochem Año: 2020 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Reino Unido