Liang Tian, Zhang Hong, Hu Yuanyuan, Solanki Mansi, Zhang Chuhua, Sasaki Takako, Smith Charles E, Hu Jan C-C, Simmer James P
Department of Orthodontics and Pediatric Dentistry, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109, USA.
Department of Biologic and Materials Sciences, University of Michigan School of Dentistry, 1011 North University, Ann Arbor, MI 48109, USA.
Int J Mol Sci. 2025 Apr 26;26(9):4134. doi: 10.3390/ijms26094134.
The human laminin family is composed of five α, four β, and three γ chains. Laminins are heterotrimers of α, β, and γ chains. Laminins play critical roles during organogenesis, mostly as basement membrane components. The expression of all and the localization of most laminin chains were characterized in mouse developing teeth. Primary laminin isoforms in basement membranes along the inner enamel epithelium before the secretory stage and outside of the outer enamel epithelium were laminins 111 (α1β1γ1) and 511. The mouse laminin α3 chain has two variants, α3A and α3B. Although a basement membrane structure is absent, laminin 3A32 was localized along the secretory surface of the secretory stage ameloblast Tomes' processes. Laminin 3A32 was localized along the atypical basement membrane of maturation stage ameloblasts and the specialized basement membrane of junctional epithelium facing the enamel surface. The endothelial basement membrane in the dental papilla and outside of the enamel organ contained laminins 411 and 511. Laminin 332 was detected in the extracellular matrix but not the basement membrane of the apical loop. Laminin 111 was localized in the extracellular matrix of the apical dental papilla without forming a visible basement membrane. These findings suggest the multifaceted functions of laminins in tooth development and set the foundation for functional investigations.
人类层粘连蛋白家族由五条α链、四条β链和三条γ链组成。层粘连蛋白是α、β和γ链的异源三聚体。层粘连蛋白在器官发生过程中发挥关键作用，主要作为基底膜成分。在小鼠发育中的牙齿中，对所有层粘连蛋白链的表达和大多数链的定位进行了表征。分泌期前沿着内釉上皮和外釉上皮外侧的基底膜中的主要层粘连蛋白异构体是层粘连蛋白111（α1β1γ1）和511。小鼠层粘连蛋白α3链有两种变体，α3A和α3B。尽管不存在基底膜结构，但层粘连蛋白3A32定位于分泌期成釉细胞托姆斯突的分泌表面。层粘连蛋白3A32定位于成熟阶段成釉细胞的非典型基底膜以及面向釉质表面的结合上皮的特殊基底膜。牙乳头和釉器外侧的内皮基底膜含有层粘连蛋白411和511。在细胞外基质中检测到层粘连蛋白332，但在顶端环的基底膜中未检测到。层粘连蛋白111定位于顶端牙乳头的细胞外基质中，未形成可见的基底膜。这些发现提示了层粘连蛋白在牙齿发育中的多方面功能，并为功能研究奠定了基础。
