Galectin-3 alters the lateral mobility and clustering of beta 1-integrin receptors

Glycoprotein receptors are influenced by myriad intermolecular interactions at the cell surface. Specific glycan structures may interact with endogenous lectins that enforce or disrupt receptor-receptor interactions. Glycoproteins bound by multivalent lectins may form extended oligomers or lattices, altering the lateral mobility of the receptor and influencing its function through endocytosis or changes in activation. In this study, we have examined the interaction of Galectin-3 (Gal-3), a human lectin, with adhesion receptors. We measured the effect of recombinant Gal-3 added exogenously on the lateral mobility of the alpha 5 beta 1 integrin on HeLa cells. Using single-particle tracking (SPT) we detected increased lateral mobility of the integrin in the presence of Gal-3, while its truncated C-terminal domain (Gal-3C) showed only minor reductions in lateral mobility. Treatment of cells with Gal-3 increased beta 1-integrin mediated migration with no apparent changes in viability. In contrast, Gal-3C decreased both cell migration and viability. Fluorescence microscopy allowed us to confirm that exogenous Gal-3 resulted in reorganization of the integrin into larger clusters. We used a proteomics analysis to confirm that cells expressed endogenous Gal-3, and found that addition of competitive oligosaccharide ligands for the lectin altered the lateral mobility of the integrin. Together, our results are consistent with a Gal-3-integrin lattice model of binding and confirm that the lateral mobility of integrins is natively regulated, in part, by galectins

Estimating a socially optimal water price for irrigation versus an environmentally optimal water price through the use of Geographical Information Systems and Social Accounting Matrices

Externalities, Input–Output models, GIS, Social Accounting Matrix (SAM), Water price,

Mice lacking galectin-3 (Lgals3) function have decreased home cage movement

Abstract Background Galectins are a large family of proteins evolved to recognize specific carbohydrate moieties. Given the importance of pattern recognition processes for multiple biological tasks, including CNS development and immune recognition, we examined the home cage behavioral phenotype of mice lacking galectin-3 (Lgals3) function. Using a sophisticated monitoring apparatus capable of examining feeding, drinking, and movement at millisecond temporal and 0.5 cm spatial resolutions, we observed daily behavioral patterns from 10 wildtype male C57BL/6J and 10 Lgals3 constitutive knockout (Lgals3 −/−; both cohorts aged 2–3 months) mice over 17 consecutive days. We performed a second behavioral assessment of this cohort at age 6–7 months. Results At both ages, Lgals3 −/− mice demonstrated less movement compared to wildtype controls. Both forward locomotion and movement-in-place behaviors were decreased in Lgals3 −/− mice, due to decreased bout numbers, initiation rates, and durations. We additionally noted perturbation of behavioral circadian rhythms in Lgals3 −/− mice, with mice at both ages demonstrating greater variability in day-to-day performance of feeding, drinking, and movement (as assessed by Lomb-Scargle analysis) compared to wildtype. Conclusion Carbohydrate recognition tasks performed by Lgals3 may be required for appropriate development of CNS structures involved in the generation and control of locomotor behavior