S100 calcium-binding protein P(S100P),a member of the S100 family of calcium-binding proteins with a typical EF-hand structure,was first purified from the placenta in 1992.Composed of 95 amino acid residues,S100P,like other S100 family members,contains two EF-hands with varying affinities for calcium ions.It has been demonstrated that S100P must form a homodimer to fulfill its role.S100P is expressed in both the cytoplasm and nucleus and is closely associated with various tumors,exhibiting aberrant expression that correlates with poor survival.S100P acts through different mechanisms both intracellularly and extracellularly.Intracellularly,it regulates multiple signaling pathways through the activation of ezrin,calcyclin binding protein/Siah-1-interacting protein(CacyBP-SIP),among others.Extracellularly,S100P binds to the cell surface protein RAGE,regulating tumor cell proliferation,metastasis,migration and invasion.Additionally,S100P plays a crucial role in cancer therapy,either promoting chemoresistance or enhancing chemosensitivity.As a significant component of the calcium signal transduction process,S100P interacts with divalent metal ions(such as Ca2+),leading to conformational changes that facilitate its binding to cell membrane receptors,eliciting corresponding biological effects.S100P is considered a promising target for tumor treatment,with potential to improve survival,prognosis,and treatment outcomes for cancer patients.This review summarizes the structure and function of S100P,explores its role in tumor proliferation,metastasis,migration,invasion,and drug resistance,and underscores its significance in tumor therapy and diagnosis.
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维普
