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. Author manuscript; available in PMC: 2013 Jan 9.
Published in final edited form as: J Immunol. 2009 Jun 1;182(11):7001–7008. doi: 10.4049/jimmunol.0804329

Figure 1.

Figure 1

Galectin-1 binding to T cells results in fodrin degradation. A) Fodrin cleavage products of 150 kD and 120 kD are abundant in galectin-1 (G) Jurkat treated cells, compared to control (C) cells. B) Fodrin associates with CD45 before and after cleavage. CD45 was immunoprecipitated from control (C) and galectin-1 (G) treated Jurkat cells, and fodrin detected by immunoblotting. Full length fodrin associates with CD45 in control cells, while the 150 and 120 kD cleavage products associate with CD45 in galectin-1 treated cells. C) Fodrin cleavage does not occur in cells that lack CD45. Jurkat and J45.01 cells were treated with buffer control or galectin-1. Fodrin cleavage products are abundant in galectin-1 Jurkat cells, but not in J45.01 cells. D) Fodrin degradation was reduced in galectin-1 treated Jurkat cells in the presence of calpain inhibitor IV that inhibits m-calpain, while calpain inhibitor VI that inhibits μ-calpain had no effect on fodrin cleavage. Data are representative of three or more independent experiments for each panel.