{"title":"对臼齿-切牙低矿化中蛋白质组学改变的综述:来自牙釉质和唾液成分的见解。","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":"{\"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. 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引用次数: 0
摘要
目的:通过了解与该缺陷相关的蛋白质组学变化,可以进一步研究磨牙-切牙低矿化(MIH)的病因和治疗。本综述旨在系统地检查与MIH相关的唾液和牙釉质蛋白质组学的现有文献,表征与缺陷相关的特定蛋白质,并评估当前蛋白质组学研究中使用的方法。方法:按照PRISMA-ScR指南进行综述。系统检索PUBMED、SCOPUS、EMBASE、Web of Science和Cochrane数据库,检索2025年2月前发表的临床试验和观察性研究。纳入标准包括人类样本的研究,检查与MIH相关的蛋白质组学与对照组。两位审稿人独立筛选文章的资格。结果:6项研究符合纳入标准。关键发现揭示了mih影响的牙釉质和唾液中蛋白质组成的显著改变,包括蛋白质,如几丁质酶1、人血清白蛋白、胶原α 1 (I)、胶原α 2 (I)、α 1-抗胰蛋白酶和牙本质唾液磷蛋白(DSPP)。特别是,MIH样品显示出与炎症和应激反应相关的蛋白质过度表达,包括白蛋白、纤维蛋白原和补体C3。蛋白质组学分析强调了唾液和牙釉质蛋白作为MIH生物标志物的潜力,尽管研究方法的变化在建立标准化生物标志物方面提出了挑战。结论:这篇综述强调了蛋白质组学分析在理解MIH分子机制中的重要性。识别特定的蛋白质可以提高对患病儿童的诊断和治疗策略。然而,大量的研究空白仍然存在,特别是在探索各种蛋白质组学来源和唾液蛋白的动态性质。
A scoping review of proteomic alterations in molar-incisor hypomineralisation: insights from enamel and salivary composition.
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.