{"title":"A scoping review of proteomic alterations in molar-incisor hypomineralisation: insights from enamel and salivary composition.","authors":"G Sivaramakrishnan, K Sridharan","doi":"10.1007/s40368-025-01050-5","DOIUrl":null,"url":null,"abstract":"<p><strong>Objectives: </strong>The aetiology and treatment of molar-incisor hypomineralisation (MIH) may be further investigated by understanding the proteomic changes associated with the defect. The present scoping review aimed to systematically examine existing literature on salivary and enamel proteomics related to MIH, characterising specific proteins associated with the defect and evaluating methodologies employed in current proteomic studies.</p><p><strong>Methods: </strong>The review was conducted following the PRISMA-ScR guidelines. A systematic search of PUBMED, SCOPUS, EMBASE, Web of Science, and Cochrane databases was performed for clinical trials and observational studies published until February 2025. Inclusion criteria encompassed studies on human samples examining proteomics related to MIH with a control group. Two reviewers independently screened articles for eligibility.</p><p><strong>Results: </strong>Six studies met the inclusion criteria. Key findings revealed significant alterations in protein composition in MIH-affected enamel and saliva, including proteins, such as chitinase 1, human serum albumin, collagen alpha 1 (I), collagen alpha 2 (I), alpha-1-antitrypsin, and dentin sialophosphoprotein (DSPP). In particular, MIH samples exhibited overexpression of proteins linked to inflammation and stress responses, including albumin, fibrinogen, and complement C3. Proteomic analyses highlighted the potential of salivary and enamel proteins as biomarkers for MIH, although variations in research methodologies presented challenges in establishing standardised biomarkers.</p><p><strong>Conclusions: </strong>This review underscores the importance of proteomic analysis in understanding the molecular mechanisms underlying MIH. Identifying specific proteins may enhance diagnostic and therapeutic strategies for affected children. However, substantial research gaps remain, particularly in the exploration of various proteomic sources and the dynamic nature of salivary proteins.</p>","PeriodicalId":520615,"journal":{"name":"European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry","volume":" ","pages":""},"PeriodicalIF":2.0000,"publicationDate":"2025-05-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/s40368-025-01050-5","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
Abstract
Objectives: The aetiology and treatment of molar-incisor hypomineralisation (MIH) may be further investigated by understanding the proteomic changes associated with the defect. The present scoping review aimed to systematically examine existing literature on salivary and enamel proteomics related to MIH, characterising specific proteins associated with the defect and evaluating methodologies employed in current proteomic studies.
Methods: The review was conducted following the PRISMA-ScR guidelines. A systematic search of PUBMED, SCOPUS, EMBASE, Web of Science, and Cochrane databases was performed for clinical trials and observational studies published until February 2025. Inclusion criteria encompassed studies on human samples examining proteomics related to MIH with a control group. Two reviewers independently screened articles for eligibility.
Results: Six studies met the inclusion criteria. Key findings revealed significant alterations in protein composition in MIH-affected enamel and saliva, including proteins, such as chitinase 1, human serum albumin, collagen alpha 1 (I), collagen alpha 2 (I), alpha-1-antitrypsin, and dentin sialophosphoprotein (DSPP). In particular, MIH samples exhibited overexpression of proteins linked to inflammation and stress responses, including albumin, fibrinogen, and complement C3. Proteomic analyses highlighted the potential of salivary and enamel proteins as biomarkers for MIH, although variations in research methodologies presented challenges in establishing standardised biomarkers.
Conclusions: This review underscores the importance of proteomic analysis in understanding the molecular mechanisms underlying MIH. Identifying specific proteins may enhance diagnostic and therapeutic strategies for affected children. However, substantial research gaps remain, particularly in the exploration of various proteomic sources and the dynamic nature of salivary proteins.
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