Syndecan-1 of 310 aas and 2 TMSs, N- and C-terminal.  The binding of cytokines and growth factors to heparan sulfate (HS) chains on proteoglycans generates gradients that control development and regulate wound healing. Syndecan-1 (sdc1) is an integral membrane HS proteoglycan. Its structure allows it to bind with cytosolic, transmembrane, and extracellular matrix (ECM) proteins. It plays important roles in mediating key events during wound healing because it regulates a number of important processes, including cell adhesion, cell migration, endocytosis, exosome formation, and fibrosis (Stepp et al. 2015). Syndecan-1 mediates sorting of soluble lipoprotein lipase into sphingomyelin-rich membranes in the golgi apparatus (Sundberg et al. 2019). The structural characteristics, shedding process, and nuclear translocation of SDC-1 have been reviewed (Guo et al. 2021).