Galectin-1

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Galectin-1 is the best-studied of the prototypic galectins. The crystal structure of galectin-1 is known, and was the first crystal structure identified for a prototypic galectin.
In addition, galectin-1...

  • was the first prototypic galectin for which a function was identified.
  • was the first prototypic galectin that was genetically ablated in mice; galectin-1 knockout mice have distinct phenotypes, including aberrant T lymphocyte development and increased susceptibility to autoimmune disease.
  • is the only prototypic galectin that has been administered in animal models of disease to assess therapeutic potential.
  • has novel dynamics and functions regarding it oxidized versus reduced status, as well as its dimerization status[1][2].
  • binds novel N- and O-glycan determinants that are involved in cell signaling[2][3][4][5][6].
  • demonstrates novel distributions in muscle cells versus non-muscle cells[7].
  • ligands are modulated by their differential sialylation that is also associated with glycoprotein positioning in membranes[8].
  • is involved in lymphocyte trafficking and leukocyte recruitment[5][9].


Contents

CFG Participating Investigators contributing to the understanding of this paradigm

CFG Participating Investigators (PIs) contributing to the understanding of galectin-1 include:

  • Linda Baum
  • C. Fred Brewer
  • Richard Cummings
  • Anne Dell
  • Ten Feizi
  • M.G. Finn
  • Thomas Gerken
  • Benhur Lee
  • J. Michael Pierce
  • Mauro Perretti
  • Gabriel Rabinovich
  • James Rini
  • Sachiko Sato
  • Gerald Schwarting
  • Pamela Stanley
  • Victor Thijssen
  • Gerardo Vasta
  • John Wang

Progress toward understanding this GBP paradigm

Carbohydrate ligands


Cellular expression


Structure


Biological roles of GBP-ligand interaction


CFG resources used in investigations

Glycan profiling


Glycogene microarray


Knockout mouse lines

CFG-generated galectin-1 knockout mice have been used to study the biological functions of this paradigm GBP. The phenotype of galectin-1 knockout mice was analyzed by the CFG.

Glycan array

Investigators have used carbohydrate compounds and glycan microarrays to study ligand binding specificity of galectin-1.


CFG database search results for Galectin-1
Resources Data Molecule Pages
All All All
Reagents Glycan profiling Glycan structures
Mouse lines Glycogene microarray GBP molecules
Resource requests Mouse phenotyping Glycosyltransferases
Other resources Glycan array


Related GBPs

Galectins-2, -5, -7, -10, -11, -13, and -14


References

  1. Stowell SR, et al. Ligand reduces galectin-1 sensitivity to oxidative inactivation by enhancing dimer formation. J Biol Chem 284, 4989-4999 (2009).
  2. 2.0 2.1 Leppanen A, Stowell S, Blixt O, Cummings RD. Dimeric galectin-1 binds with high affinity to alpha2,3-sialylated and non-sialylated terminal N-acetyllactosamine units on surface-bound extended glycans. J Biol Chem 280, 5549-5562 (2005).
  3. Earl LA, Bi S, Baum LG. N- and O-glycans modulate galectin-1 binding, CD45 signaling, and T cell death. J Biol Chem 285, 2232-2244 (2010).
  4. Song X, et al. Novel fluorescent glycan microarray strategy reveals ligands for galectins. Chem Biol 16, 36-47 (2009).
  5. 5.0 5.1 Cooper D, Norling LV, Perretti M. Novel insights into the inhibitory effects of Galectin-1 on neutrophil recruitment under flow. J Leukoc Biol 83, 1459-1466 (2008).
  6. Stillman BN, et al. Galectin-3 and galectin-1 bind distinct cell surface glycoprotein receptors to induce T cell death. J Immunol 176, 778-789 (2006).
  7. Dias-Baruffi M, et al. Differential expression of immunomodulatory galectin-1 in peripheral leukocytes and adult tissues and its cytosolic organization in striated muscle. Glycobiology In Press. (2010).
  8. Cha SK, et al. Removal of sialic acid involving Klotho causes cell-surface retention of TRPV5 channel via binding to galectin-1. Proc Natl Acad Sci U S A 105, 9805-9810 (2008).
  9. Norling LV, Sampaio AL, Cooper D, Perretti M. Inhibitory control of endothelial galectin-1 on in vitro and in vivo lymphocyte trafficking. Faseb J 22, 682-690 (2008).
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