RGD Reference Report - Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1. - Rat Genome Database

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Characterization of the interaction between galectin-1 and lymphocyte glycoproteins CD45 and Thy-1.

Authors: Symons, A  Cooper, DN  Barclay, AN 
Citation: Symons A, etal., Glycobiology. 2000 Jun;10(6):559-63.
RGD ID: 1643027
Pubmed: PMID:10814697   (View Abstract at PubMed)

Galectin-1 is a sugar binding protein specific for beta-galactosides and not requiring metal ions for binding activity. It exists as a soluble protein which forms a noncovalent homodimer and is expressed with a broad tissue distribution. Recently, galectin-1 has been shown to play a possible role in the immune system mediating apoptosis of activated T cells with indirect evidence suggesting that galectin-1 interacts with the heavily glycosylated, transmembrane, protein phosphotyrosine phosphatase CD45. The interaction of galectin-1 with purified lymphocyte cell surface proteins was studied using surface plasmon resonance in a BIAcoretrade mark. Galectin-1 was shown to bind CD45 and Thy-1 in a carbohydrate-dependent manner. Several galectin-1 molecules could bind each CD45 molecule. The dissociation constant of dimeric galectin-1 binding to CD45 was measured at approximately 5 microM, indicating the concentration at which cross-linking of cell surface glycoproteins by galectin-1 would occur. A possible role for galectin-1 in the organization of cell surface glycoproteins is discussed.



Gene Ontology Annotations    Click to see Annotation Detail View

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
PtprcRatcell surface  IDA  RGD 

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Lgals1  (galectin 1)
Ptprc  (protein tyrosine phosphatase, receptor type, C)
Thy1  (Thy-1 cell surface antigen)


Additional Information