INVESTIGADORES
CROCI RUSSO Diego Omar
artículos
Título:
REGULATED EXPRESSION OF GALECTIN-3, A MULTIFUNCTIONAL
Autor/es:
VICTORIA SUNDBLAD; DIEGO O. CROCI; GABRIEL RABINOVICH
Revista:
HISTOLOGY AND HISTOPATHOLOGY
Editorial:
F HERNANDEZ
Referencias:
Lugar: MADRID; Año: 2010
ISSN:
0213-3911
Resumen:
Abstract Galectin-3 belongs to a family of highly conserved animal lectins characterized by their ability to recognize multiple N-acetyllactosamine sequences, which can be displayed on both N- and O-glycans on cell surface glycoconjugates. Although first identified in macrophages, galectin-3 (also called ‘Mac-2, åBP, CBP35 or L-29’) has been found to be widely distributed in several tissues and developmental stages where, depending on its extracellular or intracellular localization, it can display a broad diversity of biological functions including immunomodulation, host-pathogen interactions, embryogenesis, angiogenesis, cell migration, wound healing and apoptosis. In spite of the existence of several reviews describing the multifunctional properties of galectin-3, an integrated view of the regulated expression of this glycan-binding protein in different normal tissues is lacking. Here we attempt to summarize and coordinate available information on galectin-3 distribution in normal haematopoietic and nonhaematopoietic tissues, mainly in adulthood with only a brief reference to its expression during embryonic stages. In addition, given the multiplicity of biological roles attributed to this protein, a brief description of galectin-3 functions is also included. Understanding how galectin-3 is regulated in normal tissues will contribute to a logic design of approaches aimed at modulating galectin-3 expression and subcellular localization for experimental and therapeutic purposes.a family of highly conserved animal lectins characterized by their ability to recognize multiple N-acetyllactosamine sequences, which can be displayed on both N- and O-glycans on cell surface glycoconjugates. Although first identified in macrophages, galectin-3 (also called ‘Mac-2, åBP, CBP35 or L-29’) has been found to be widely distributed in several tissues and developmental stages where, depending on its extracellular or intracellular localization, it can display a broad diversity of biological functions including immunomodulation, host-pathogen interactions, embryogenesis, angiogenesis, cell migration, wound healing and apoptosis. In spite of the existence of several reviews describing the multifunctional properties of galectin-3, an integrated view of the regulated expression of this glycan-binding protein in different normal tissues is lacking. Here we attempt to summarize and coordinate available information on galectin-3 distribution in normal haematopoietic and nonhaematopoietic tissues, mainly in adulthood with only a brief reference to its expression during embryonic stages. In addition, given the multiplicity of biological roles attributed to this protein, a brief description of galectin-3 functions is also included. Understanding how galectin-3 is regulated in normal tissues will contribute to a logic design of approaches aimed at modulating galectin-3 expression and subcellular localization for experimental and therapeutic purposes.åBP, CBP35 or L-29’) has been found to be widely distributed in several tissues and developmental stages where, depending on its extracellular or intracellular localization, it can display a broad diversity of biological functions including immunomodulation, host-pathogen interactions, embryogenesis, angiogenesis, cell migration, wound healing and apoptosis. In spite of the existence of several reviews describing the multifunctional properties of galectin-3, an integrated view of the regulated expression of this glycan-binding protein in different normal tissues is lacking. Here we attempt to summarize and coordinate available information on galectin-3 distribution in normal haematopoietic and nonhaematopoietic tissues, mainly in adulthood with only a brief reference to its expression during embryonic stages. In addition, given the multiplicity of biological roles attributed to this protein, a brief description of galectin-3 functions is also included. Understanding how galectin-3 is regulated in normal tissues will contribute to a logic design of approaches aimed at modulating galectin-3 expression and subcellular localization for experimental and therapeutic purposes.is also included. Understanding how galectin-3 is regulated in normal tissues will contribute to a logic design of approaches aimed at modulating galectin-3 expression and subcellular localization for experimental and therapeutic purposes.