Thus, stathmin is expressed higher in DPSCs than in CDPSCs. The essential role of stathmin in regulating the cytoskeleton microtubules indicated that it may be required for the biological functions of DPSCs. Another group of differentially expressed proteins is correlated with cell cytoskeleton and motility and includes TPM2, MYL9, CAPZB, CAPG, KRT9 and KRT10. Tropomyosins are a family of actin-filament binding proteins expressed in most eukaryotic cells. In human, there are at least four TPM genes. TPM2 is found primarily in skeletal muscles and this protein helps regulate muscle contraction by interacting with other muscle proteins, particularly myosin and actin. In addition, TPM2 is essential for cytoskeleton establishment and the regulation of TGF-b induced stress fiber formation. MYL9 can be phosphorylated by myosin light chain kinase in the presence of calcium and calmodulin. This phosphorylation contributes to the increase in the actin-activated ATPase activities of myosins. MYL9 is involved in the regulation of both smooth muscle and nonmuscle cell contractile activity via its phosphorylation. Moreover, phosphorylation of MYL9 alters myocardium contraction by increasing the force and rate of force development. CAPZB is a heterodimer with an a subunit of 32-36 kDa and a b subunit of 28-32 kDa. The actin barbed end capping protein is highly conserved and found in nearly all eukaryotic cells. CAPZB regulates the assembly of actin filament structures which are required for numerous biological processes and precise coordination. CAPG is a member of the gelsolin-villin family, and it binds to actin in a calcium-dependent manner. CAPG is wildly distributed in tissues and cells. Previous studies have shown that its function is closely correlated with the motility and ruffling of various cell types including macrophages, neutrophils, fibroblasts, and endothelial cells,. Recently, CAPG was reported to be an essential protein for the embedding and dendrite elongation processes in osteocytes. KRT9, a type I intermediate filament protein, is abundant in human foot soles and palms. In mice, KRT9 is a major component of the perinuclear ring of manchette in spermatids and is required for normal sperm development. Mutation of KRT9 is responsible for human epidermolytic palmoplantar keratoderma and degenerative changes of keratin’s intermediate filament structure. KRT10, a type I keratin protein, is normally expressed in the suprabasal epidermal compartment. Deletion of KRT10 impairs permeability barrier function and stratum corneum hydration. KRT10 is required for epidermal integrity, as KRT10 mutation leads to epidermolytic hyperkeratosis. In this study, 3 identified proteins were mainly related to antioxidative function including TALDO1, GLRX3, and APEH. TALDO1 is an enzyme of the pentose phosphate pathway.