{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nDentin sialophosphoprotein (DSPP) is a pivotal extracellular matrix protein that is abundantly expressed by odontoblasts and transiently by presecretory ameloblasts during tooth development. Once secreted, DSPP is proteolytically cleaved into distinct fragments—dentin sialoprotein (DSP) and dentin phosphoprotein (DPP)—each of which contributes critically to dentin biomineralization. DPP’s highly charged, phosphorylated character enables it to bind calcium ions and nucleate hydroxyapatite crystal formation, while DSP is thought to regulate cell–matrix interactions that support formation of the dentin–enamel junction and proper enamel maturation. Collectively, these coordinated events ensure that the dentin matrix is appropriately organized and mineralized, laying the foundation for normal tooth structure and function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMutations in the DSPP gene give rise to a spectrum of hereditary dentin disorders—most notably, dentinogenesis imperfecta (DGI) and dentin dysplasia (DD). These mutations, which include missense, nonsense, splice-site, and frameshift changes, often disrupt normal protein processing by altering critical leader sequences or the repetitive Ca²⁺‐binding domain of DSPP. Such alterations can lead to retention of the mutant protein in the endoplasmic reticulum or the production of aberrant hydrophobic peptides that interfere with secretion, thereby exhibiting dominant negative effects on the overall dentin matrix. The subsequent impairment of DSPP function interferes with calcium binding and crystal growth, ultimately compromising dentin mineralization and leading to the clinical manifestations of discolored, brittle teeth with abnormal pulp morphology."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its central role in dentin mineralization, DSPP and its proteolytic fragments are emerging as active participants in diverse cell signaling pathways that extend their influence beyond the confines of the mineralized matrix. DSPP-derived peptides can function as ligands by interacting with integrin receptors to activate intracellular cascades that regulate cellular proliferation, differentiation, and migration. Moreover, DSPP has been implicated in the modulation of matrix metalloproteinase activity, contributing to extracellular matrix turnover and tissue remodeling in both mineralizing (e.g., periodontal ligament and pulp) and non‐mineralizing tissues (e.g., salivary glands). Recent evidence has also documented DSPP upregulation in certain cancers, suggesting that its aberrant expression may be associated with tumor progression and metastasis. These findings underscore the multifaceted biological roles of DSPP in orchestrating extracellular matrix organization and cellular responses during development, repair, and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "17", "end_ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "P Papagerakis, A Berdal, M Mesbah, et al. 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