This lectin regulates cell-cell and cell-extracellular matrix interactions, cell signaling, inflammatory responses and biological events, such as cellular activation, migration, differentiation, apoptosis and tumor metastasis. Moreover, galectin-3 acts as a powerful pro-inflammatory molecule to myeloid cells by inducing chemotaxis of monocytes and phagocytosis by macrophages. It also controls T cell activation, proliferation and death, modulates carbohydrate-dependent thymocyte interactions in thymic microenvironments, and inhibits conventional/B2 and peritoneal/B1 lymphocytes differentiation into plasma cells. Galectin-3 null mice are viable under normal conditions and long lasting inflammatory responses, like Chagas’ Disease and Schistosomiasis. Galectin-3 is highly expressed by human monocyte differentiating into macrophages and is lowly expressed by human monocytes that differentiate into dendritic cells. In the MLNs homeostasis, the role of galectin-3 it is not clear. MLNs continuously draining the major part of tissues involved by schistosomiasis. In the course of the chronic phase, there is progressive hyperplasia and the lymphoid organization is maintained. Our results are not sufficient to prove whether galectin-3 controls these microenvironments, although it has been described that AZ 960 JAK inhibitor resident macrophages are responsible for phagocytosis of apoptotic cells and constitutively these cells control the distinct steps of trafficking and differentiation of these B cells. It is known that strict mechanisms regulate B cell decision between follicular and extrafollicular areas, where B lymphocytes rapidly differentiate into antibody-secreting cells. Although some light has been shed on this subject, it remains unclear how galectin-3 regulates B cell differentiation into plasma cells. In this context, it was shown that galectin-3 inhibits Blimp-1 expression in different experimental models, interfering with terminal differentiation of B lymphocytes in antibody-secreting plasma cells. These cells were described as typical tissue macrophages predominantly detected in subcapsular sinus, follicles and throughout paracortical and medullary regions. By definition, tingible body macrophages are large phagocytic cells containing many apoptotic cells in distinct states of degradation. In humans, mutations in the TWIST1 gene are associated with Saethre-Chotzen Syndrome, which is an autosomal dominant disorder characterized by craniosynostosis, brachydactyly, soft tissue syndactyly and facial dysmorphism. The skeletal phenotype of Twist1-heterozygous mouse consistently resembles that of human SCS with premature fusion of the cranial suture. As mouse embryonic development progresses, the Twist1 expression declines in the developing bones of the skull. In addition, Twist1 overexpression was found to inhibit osteoblast differentiation in vitro and in vivo. Together, these observations suggest that Twist1 negatively regulates osteoblast differentiation and bone formation. Various molecular mechanisms may be responsible for the inhibitory role of Twist1 in osteoblast differentiation. Twist1 may modulate FGF signaling, especially Fgfr2 expression in cranial suture development or it may directly bind to and inhibit the transactivation function of Runx2, a master regulator of osteogenesis. In addition, Twist1 might indirectly regulate the Runx2 expression through modulating FGFR2 expression as shown in the ex vivo cultured primary osteoblasts isolated from human SCS patients. Finally, it is possible that Twist1 inhibits osteoblast apoptosis via the suppression of TNF-a expression. Twist2 has been shown to have an inhibitory function similar to that of Twist1 in bone formation. While recessive TWIST2 mutations in humans and its inactivation in mice result in a focal facial dermal dysplasia syndrome, there is no Twist2- deficient skeletal phenotype. The phenotypic difference between the Twist1- and Twist2-deficient subjects is indeed intriguing when viewed in the context of their significantly overlapping expression patterns in vivo and their similar functions in bone formation. Thus, it is largely unknown how Twist1 and Twist2 synergistically regulate bone formation and what molecular mechanism is involved. Accumulating evidence supports the notion that Twist1 might control cranial suture development through modulating FGF signaling. It was found that the mutations in FGF receptors FGFR1, FGFR2, and FGFR3 in humans are associated with craniosynostosis, a characteristic phenotype of the Saethre- Chotzen Syndrome caused by dominant loss-of-function TWIST1 mutations. In addition, the primary cranial osteoblasts isolated from SCS patients with Twist1 mutations show reduced FGFR2 transcript levels, which can be restored by overexpression of TWIST1.