When galectins recognize glycans: From biochemistry to physiology and back again
In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes o...
Guardado en:
| Autores principales: | , , , , , , |
|---|---|
| Formato: | JOUR |
| Materias: | |
| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_00062960_v50_n37_p7842_DiLella |
| Aporte de: |
| id |
todo:paper_00062960_v50_n37_p7842_DiLella |
|---|---|
| record_format |
dspace |
| spelling |
todo:paper_00062960_v50_n37_p7842_DiLella2023-10-03T14:04:32Z When galectins recognize glycans: From biochemistry to physiology and back again Di Lella, S. Sundblad, V. Cerliani, J.P. Guardia, C.M. Estrin, D.A. Vasta, G.R. Rabinovich, G.A. Biological functions Biological process Broad spectrum Carbohydrate specificity Cell biology Cell surfaces Cellular communication Functional aspects Galectins Glycans Limited information Monitoring change Multifunctional properties Wide spectrum Biochemistry Carbohydrates Cell membranes Cytology Pathology Proteins Physiology arachidonic acid arginase beta galactosidase binding protein carbohydrate ecalectin Fc receptor galectin galectin 1 galectin 10 galectin 2 galectin 3 galectin 4 galectin 8 gamma interferon glycan interleukin 10 interleukin 27 major histocompatibility antigen class 2 mitogen activated protein kinase nitric oxide protein kinase C unclassified drug adaptive immunity antiinflammatory activity apoptosis article B lymphocyte biochemistry carboxy terminal sequence cell activation cell maturation cell viability cytokine production dendritic cell dimerization DNA fragmentation enzyme activity enzyme analysis enzyme structure homeostasis immunology innate immunity ligand binding molecular biology molecular dynamics mutant nonhuman nuclear magnetic resonance oligomerization phagocytosis physiology priority journal protein expression protein function protein protein interaction regulatory mechanism signal transduction T lymphocyte tandem repeat Th1 cell Th17 cell Animals Biochemical Phenomena Crystallography, X-Ray Galectins Humans Polysaccharides Protein Binding In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings. © 2011 American Chemical Society. Fil:Sundblad, V. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Guardia, C.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Estrin, D.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_00062960_v50_n37_p7842_DiLella |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
Biological functions Biological process Broad spectrum Carbohydrate specificity Cell biology Cell surfaces Cellular communication Functional aspects Galectins Glycans Limited information Monitoring change Multifunctional properties Wide spectrum Biochemistry Carbohydrates Cell membranes Cytology Pathology Proteins Physiology arachidonic acid arginase beta galactosidase binding protein carbohydrate ecalectin Fc receptor galectin galectin 1 galectin 10 galectin 2 galectin 3 galectin 4 galectin 8 gamma interferon glycan interleukin 10 interleukin 27 major histocompatibility antigen class 2 mitogen activated protein kinase nitric oxide protein kinase C unclassified drug adaptive immunity antiinflammatory activity apoptosis article B lymphocyte biochemistry carboxy terminal sequence cell activation cell maturation cell viability cytokine production dendritic cell dimerization DNA fragmentation enzyme activity enzyme analysis enzyme structure homeostasis immunology innate immunity ligand binding molecular biology molecular dynamics mutant nonhuman nuclear magnetic resonance oligomerization phagocytosis physiology priority journal protein expression protein function protein protein interaction regulatory mechanism signal transduction T lymphocyte tandem repeat Th1 cell Th17 cell Animals Biochemical Phenomena Crystallography, X-Ray Galectins Humans Polysaccharides Protein Binding |
| spellingShingle |
Biological functions Biological process Broad spectrum Carbohydrate specificity Cell biology Cell surfaces Cellular communication Functional aspects Galectins Glycans Limited information Monitoring change Multifunctional properties Wide spectrum Biochemistry Carbohydrates Cell membranes Cytology Pathology Proteins Physiology arachidonic acid arginase beta galactosidase binding protein carbohydrate ecalectin Fc receptor galectin galectin 1 galectin 10 galectin 2 galectin 3 galectin 4 galectin 8 gamma interferon glycan interleukin 10 interleukin 27 major histocompatibility antigen class 2 mitogen activated protein kinase nitric oxide protein kinase C unclassified drug adaptive immunity antiinflammatory activity apoptosis article B lymphocyte biochemistry carboxy terminal sequence cell activation cell maturation cell viability cytokine production dendritic cell dimerization DNA fragmentation enzyme activity enzyme analysis enzyme structure homeostasis immunology innate immunity ligand binding molecular biology molecular dynamics mutant nonhuman nuclear magnetic resonance oligomerization phagocytosis physiology priority journal protein expression protein function protein protein interaction regulatory mechanism signal transduction T lymphocyte tandem repeat Th1 cell Th17 cell Animals Biochemical Phenomena Crystallography, X-Ray Galectins Humans Polysaccharides Protein Binding Di Lella, S. Sundblad, V. Cerliani, J.P. Guardia, C.M. Estrin, D.A. Vasta, G.R. Rabinovich, G.A. When galectins recognize glycans: From biochemistry to physiology and back again |
| topic_facet |
Biological functions Biological process Broad spectrum Carbohydrate specificity Cell biology Cell surfaces Cellular communication Functional aspects Galectins Glycans Limited information Monitoring change Multifunctional properties Wide spectrum Biochemistry Carbohydrates Cell membranes Cytology Pathology Proteins Physiology arachidonic acid arginase beta galactosidase binding protein carbohydrate ecalectin Fc receptor galectin galectin 1 galectin 10 galectin 2 galectin 3 galectin 4 galectin 8 gamma interferon glycan interleukin 10 interleukin 27 major histocompatibility antigen class 2 mitogen activated protein kinase nitric oxide protein kinase C unclassified drug adaptive immunity antiinflammatory activity apoptosis article B lymphocyte biochemistry carboxy terminal sequence cell activation cell maturation cell viability cytokine production dendritic cell dimerization DNA fragmentation enzyme activity enzyme analysis enzyme structure homeostasis immunology innate immunity ligand binding molecular biology molecular dynamics mutant nonhuman nuclear magnetic resonance oligomerization phagocytosis physiology priority journal protein expression protein function protein protein interaction regulatory mechanism signal transduction T lymphocyte tandem repeat Th1 cell Th17 cell Animals Biochemical Phenomena Crystallography, X-Ray Galectins Humans Polysaccharides Protein Binding |
| description |
In the past decade, increasing efforts have been devoted to the study of galectins, a family of evolutionarily conserved glycan-binding proteins with multifunctional properties. Galectins function, either intracellularly or extracellularly, as key biological mediators capable of monitoring changes occurring on the cell surface during fundamental biological processes such as cellular communication, inflammation, development, and differentiation. Their highly conserved structures, exquisite carbohydrate specificity, and ability to modulate a broad spectrum of biological processes have captivated a wide range of scientists from a wide spectrum of disciplines, including biochemistry, biophysics, cell biology, and physiology. However, in spite of enormous efforts to dissect the functions and properties of these glycan-binding proteins, limited information about how structural and biochemical aspects of these proteins can influence biological functions is available. In this review, we aim to integrate structural, biochemical, and functional aspects of this bewildering and ancient family of glycan-binding proteins and discuss their implications in physiologic and pathologic settings. © 2011 American Chemical Society. |
| format |
JOUR |
| author |
Di Lella, S. Sundblad, V. Cerliani, J.P. Guardia, C.M. Estrin, D.A. Vasta, G.R. Rabinovich, G.A. |
| author_facet |
Di Lella, S. Sundblad, V. Cerliani, J.P. Guardia, C.M. Estrin, D.A. Vasta, G.R. Rabinovich, G.A. |
| author_sort |
Di Lella, S. |
| title |
When galectins recognize glycans: From biochemistry to physiology and back again |
| title_short |
When galectins recognize glycans: From biochemistry to physiology and back again |
| title_full |
When galectins recognize glycans: From biochemistry to physiology and back again |
| title_fullStr |
When galectins recognize glycans: From biochemistry to physiology and back again |
| title_full_unstemmed |
When galectins recognize glycans: From biochemistry to physiology and back again |
| title_sort |
when galectins recognize glycans: from biochemistry to physiology and back again |
| url |
http://hdl.handle.net/20.500.12110/paper_00062960_v50_n37_p7842_DiLella |
| work_keys_str_mv |
AT dilellas whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT sundbladv whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT cerlianijp whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT guardiacm whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT estrinda whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT vastagr whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain AT rabinovichga whengalectinsrecognizeglycansfrombiochemistrytophysiologyandbackagain |
| _version_ |
1807320244360839168 |