Galectin-3 Plays an Important Role in BMP7-Induced Cementoblastic Differentiation of Human Periodontal Ligament Cells by Interacting with Extracellular Components

Figure 9

Schematics of galectin-3 function during BMP7-mediated cementoblastic differentiation. Cytosolic galectin-3 is secreted by a nonclassical mechanism via exosomes, because galectins lack a signal peptide (dotted line) [61]. Once in the extracellular space, galectin-3 can interact with innumerous glycosylated molecules, such as cell adhesion molecules, integrins, and ECM molecules such as laminins. Additional galectin-3 partner is glycosylated BMP7, and galectin-3 may gather BMP7 in extracellular space. According to long-term stimulation by BMP7, galectin-3 expression is highly increased, and the differentiation efficiency is amplified due to cell-ECM interaction and BMP7 concentration. GB1107, a galectin-3 inhibitor, reduces the efficiency of cementoblastic differentiation by inhibiting the interaction of laminin and BMP7 with galectins.