Galectin: Difference between revisions

Latest revision as of 11:34, 3 August 2021

Function

Galectin or galactoside-binding soluble lectin (GAL) are lectins which bind β-galactosidase (BGAL). GAL contains a carbohydrate recognition domain (CRD) residues 113-250^[1].

GAL-1 is thought to play a role as autocrine negative growth factor that regulates cell proliferation.
GAL-2 is expressed primarily in gastrointestinal tract.
GAL-3 has broad biological functionality.
GAL-4 has 2 CRDs.
GAL-5 is found in rat is a β-galactoside binding lectin^[2].
GAL-7 is associated with epithelial cells.
GAL-8 has a role in cellular defense against bacterial infection and vacuolar damage.
GAL-9 affects eosinophil survival.
GAL-10 or Charcot-Leyden crystal protein acts on biological membranes to regulate the multifunctional lysophospholipids.
GAL-13 is a placental protein which does not bind β-galactosides.

Relevance

GAL are known to inhibit chronic inflammation^[3]. GAL-3 has a role in experimental autoimmune encephalomyelitis and melanoma methastasis^[4].

Structural highlights

The CRD is a β-sandwich long enough to bind a tetrasaccharide. A ^[5]. Water molecules shown as red spheres.

3D structures of galectin

Galectin 3D structures

Structure of human galectin-1 complex with lactose, mercaptoethanol and sulfate (PDB entry 1w6o)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem. 1994 Aug 19;269(33):20807-10. PMID:8063692
↑ Barres C, Blanc L, Bette-Bobillo P, Andre S, Mamoun R, Gabius HJ, Vidal M. Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood. 2010 Jan 21;115(3):696-705. doi: 10.1182/blood-2009-07-231449. Epub 2009, Nov 10. PMID:19903899 doi:http://dx.doi.org/10.1182/blood-2009-07-231449
↑ Liu FT, Rabinovich GA. Galectins: regulators of acute and chronic inflammation. Ann N Y Acad Sci. 2010 Jan;1183:158-82. doi: 10.1111/j.1749-6632.2009.05131.x. PMID:20146714 doi:http://dx.doi.org/10.1111/j.1749-6632.2009.05131.x
↑ Radosavljevic G, Volarevic V, Jovanovic I, Milovanovic M, Pejnovic N, Arsenijevic N, Hsu DK, Lukic ML. The roles of Galectin-3 in autoimmunity and tumor progression. Immunol Res. 2012 Apr;52(1-2):100-10. doi: 10.1007/s12026-012-8286-6. PMID:22418727 doi:http://dx.doi.org/10.1007/s12026-012-8286-6
↑ Lopez-Lucendo MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol. 2004 Oct 29;343(4):957-70. PMID:15476813 doi:http://dx.doi.org/10.1016/j.jmb.2004.08.078

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Michal Harel, Alexander Berchansky, Joel L. Sussman

[1] Barondes SH, Cooper DN, Gitt MA, Leffler H. Galectins. Structure and function of a large family of animal lectins. J Biol Chem. 1994 Aug 19;269(33):20807-10. PMID:8063692

[2] Barres C, Blanc L, Bette-Bobillo P, Andre S, Mamoun R, Gabius HJ, Vidal M. Galectin-5 is bound onto the surface of rat reticulocyte exosomes and modulates vesicle uptake by macrophages. Blood. 2010 Jan 21;115(3):696-705. doi: 10.1182/blood-2009-07-231449. Epub 2009, Nov 10. PMID:19903899 doi:http://dx.doi.org/10.1182/blood-2009-07-231449

[3] Liu FT, Rabinovich GA. Galectins: regulators of acute and chronic inflammation. Ann N Y Acad Sci. 2010 Jan;1183:158-82. doi: 10.1111/j.1749-6632.2009.05131.x. PMID:20146714 doi:http://dx.doi.org/10.1111/j.1749-6632.2009.05131.x

[4] Radosavljevic G, Volarevic V, Jovanovic I, Milovanovic M, Pejnovic N, Arsenijevic N, Hsu DK, Lukic ML. The roles of Galectin-3 in autoimmunity and tumor progression. Immunol Res. 2012 Apr;52(1-2):100-10. doi: 10.1007/s12026-012-8286-6. PMID:22418727 doi:http://dx.doi.org/10.1007/s12026-012-8286-6

[5] Lopez-Lucendo MF, Solis D, Andre S, Hirabayashi J, Kasai K, Kaltner H, Gabius HJ, Romero A. Growth-regulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol. 2004 Oct 29;343(4):957-70. PMID:15476813 doi:http://dx.doi.org/10.1016/j.jmb.2004.08.078

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@@ Line 3: / Line 3: @@
 == Function ==
-'''Galectin''' (GAL) are lectins which bind β-galactosidase (BGAL).  GAL contains a carbohydrate recognition domain (CRD) residues 113-250<ref>PMID:8063692</ref>.  <br />
+'''Galectin''' or '''galactoside-binding soluble lectin''' (GAL) are lectins which bind β-galactosidase (BGAL).  GAL contains a carbohydrate recognition domain (CRD) residues 113-250<ref>PMID:8063692</ref>.  <br />
 * GAL-1 is thought to play a role as autocrine negative growth factor that regulates cell proliferation.<br />
 * GAL-2 is expressed primarily in gastrointestinal tract.<br />

Galectin: Difference between revisions

Latest revision as of 11:34, 3 August 2021

Contents

Function

Relevance

Structural highlights

3D structures of galectin

ReferencesReferences

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Galectin: Difference between revisions

Latest revision as of 11:34, 3 August 2021

Function

Relevance

Structural highlights

3D structures of galectin

ReferencesReferences

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