ArticleEuropean archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry2026
Comparative label-free quantitative proteomics of hypomineralised second primary molars (HSPM) and molar incisor hypomineralisation (MIH) reveals divergent enamel protein signatures underpinning distinct pathogenic mechanisms.
Article in European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
purposeThis study directly compared the enamel matrix proteomes of HSPM and MIH using label-free quantitative proteomics to identify differentially abundant proteins and understand condition-specific pathogenic mechanisms.
methodsEnamel samples from 10 HSPM and 10 MIH samples were subjected to label-free quantitative LC-MS/MS analysis (final comparative analysis: n = 6 per group). 120 proteins common to both groups were identified through secondary proteomic analysis; 90 met a ≥ 50% detection threshold and were retained for quantitative comparison. Sensitivity analysis evaluated detection frequencies and protein selectivity. Differential abundance was assessed using Welch's t-test with Benjamini-Hochberg false discovery rate (FDR) correction; significance was set at FDR < 0.05.
resultsDetection frequency analysis identified 78 proteins (86.7%) as common high confidence across both enamel types. Differential analysis identified 46 significantly abundant proteins (FDR < 0.05), of which 38 were enriched in HSPM enamel and 8 in MIH enamel. HSPM-enriched proteins were suggestive of immune infiltration and a protease-antiprotease imbalance during primary molar amelogenesis. In contrast, MIH enamel was selectively enriched for epidermal cornification and desmosomal junction proteins, which may reflect enamel organ epithelial disruption during permanent molar amelogenesis.
conclusionThis is the first comparative study of enamel proteomics in HSPM and MIH. Despite a largely shared protein pool, the two conditions have a near-identical qualitative protein inventory, with smaller quantitative differences that may reflect divergent biological processes, with an immune-inflammatory signature in HSPM and an epithelial disruption signature in MIH. These findings may inform the future development of candidate condition-specific markers and targeted preventive strategies.
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