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Micromorphology, microstructure and micro-Raman spectroscopy of a case of amelogenesis imperfecta
Published in J. Belinha, R.M. Natal Jorge, J.C. Reis Campos, Mário A.P. Vaz, João Manuel, R.S. Tavares, Biodental Engineering V, 2019
Sebastiana Arroyo Bote, Alfonso Villa-Vigil, M.C. Manzanares Céspedes, Esteban Brau-Aguadé
Amelogenesis Imperfecta (AI) is characterized by presenting enamel defects, without defects in others tissues (Witkop, 1988). Hereditary defects in the enamel development or environmental exposure to chemicals and drugs can damage the ameloblasts (Ferreira et al., 2005). AI is characterized by its heterogeneous phenotypical clinical patterns of variable severity, as well as for its complex genetype (Wright, 2006; Gibson, 2008; Wang et al., 2013) and/or environmental aetiology (Hedge, 2012; Malik et al., 2012). Based on its heredity and clinical evidences, four types and numerous subtypes of AI were described in 1988 by Witkop (hypoplastic, hypomaturation, hypocalcified AI and a combination of them), and today this is the most widely used classification in the clinical practice. The development of enamel starts with the secretion of the enamel protein matrix by the ameloblasts, followed by its calcification and maturation (Sapp et al., 2005; Malik et al., 2012). Less than 1% of the mature enamel is constituted by organic components, while the mineral components constitute more than a 95%. The enamel mineral crystals are deposited in compact hexagonal rod-shaped structure, making this tissue the hardest in the human body (Nanci, 2012). Numerous genes have been reported as responsible of the regulation of this complex process (Sapp et al., 2005; Bailleul-Forestier et al., 2008; Lee et al., 2008; Misiadis & Luder, 2011; Luder et al., 2013; Simmer et al., 2013; Wang et al., 2014; Zhang et al., 2015; Prasad et al., 2016). Mutations of AMELX (amelogenin), ENAM (enamelin) (Misiadis & Luder, 2011), COL17A1 (Prasad et al., 2016) and FAM20A (Wang et al., 2014) have been proven as causes of hypoplastic AI, either with smooth or rough enamel; while the AI with hypomature phenotype has been attributed to genetic defects in AMELX, MMP20, KLK4 and WDR72. Hypocalcified AI have been reported to be caused by FAM83H or C4orf26 (Kim et al., 2008; Parry et al., 2012; Luder et al., 2013) in humans. Additionally, some studies indicate that a mutation in one gene could be related to more than one type of AI; thus CNNM4 mutation is related to hypoplastic/hypomineralized types (Lee et al., 2008), DLX3 mutation is related with and hypomature/hypoplastic types (Wang et al., 2014) and C4orf26 hypomineralized-hypoplastic types (Prasad et al., 2016).
The Genes Involved in Dentinogenesis
Published in Organogenesis, 2022
Shuang Chen, Han Xie, Shouliang Zhao, Shuai Wang, Xiaoling Wei, Shangfeng Liu
Dentin sialoprotein (DSP) and dentin phosphoprotein (DPP) are encoded by dentin sialophosphoprotein (Dspp) and its deficiency may lead to dentin hypoplasia or dysplasia and opalescent, shell, and abnormal deciduous teeth with short roots. Therefore, Dspp is an important marker of odontoblasts6 and is the first direct target of distal-less homeobox 3 (Dlx3), which was identified in odontoblasts.7
Transcriptomic analysis reveals the regulatory mechanism underlying the indirubin-mediated amelioration of dextran sulfate sodium-induced colitis in mice
Published in Pharmaceutical Biology, 2023
Zhe Liu, Jin-ru Zhang, Yong-xiang Huang, Xue-ying Li, Hai-peng Zhu, Rui-yi Yang, Song Chen
Compared with those in the DSS model group, 434 DEGs were identified in the IDR treatment groups, among which 123 and 313 genes were upregulated and downregulated, respectively. Seven of the top 10 upregulated genes were predicted and novel genes with unknown functions (Figure 4(A)). The remaining three genes encoded kallikrein 1-related peptidase b4 (Kik1b4), sodium-dependent phosphate transport protein 2B (Slc34a2), and leukocyte antigen-6 (Ly6g6c). In contrast, the top 10 downregulated genes were signal recognition particle 54b (Srp54b), Ig family (immunoglobulin kappa variable genes Igkv1-88, Igkv4-53, Igkv13-85, and Igkv3-1, and immunoglobulin kappa heavy variable 1-50), Cd300lg, inter-α-trypsin inhibitor heavy chain 4 (Itih4), kirre-like nephrin family adhesion molecule 3 (Kirrel3os), and Nlrp3. The heatmap shows the separation of the clustered DEGs of the IDR treatment groups from those of the DSS model group and the sample homogeneity in each group (Figure 4(B)). PPI analysis with DEG-corresponding proteins revealed hubs, including NLRP3 (including IL-1β, myeloperoxidase, and chemokines). Additionally, the HB family (Hbb-bt, Hbb-bs, Hba-a2, and Hba-a1 encoding proteins) formed a distinct cluster (Figure 4(C)). In contrast, most genes commonly used to evaluate AhR pathway activation, including IDO-1 and IL-22, were unaffected. Functional KEGG pathways were then predicted. Among the top enriched KEGG pathways, African trypanosomiasis and the malaria pathway were downregulated (Figure 4(D)). The members of these two KEGG pathways overlapped and mainly comprised the Hb family, Il10, and Il1β (Table S5). The DEG-relevant transcription factors are shown in Figure 4(E). Homeobox family (including distal-less homeobox 3 [DLX3], homeobox C6 [Hoxc6], Msh homeobox 1 [MSX1], mesenchyme homeobox 2 [MEOX2], and paired related homeobox 1 [PRRX1]) and zf-C2H2 are the dominant transcription factors. GO pathway predictions are shown in Supplementary Figure 3. AS analysis revealed that SE was still the most common and its proportion decreased, whereas the proportions of A5SS, A3SS, and RI in the DSS model group increased compared with those in the control groups (Figure 4(F)). The neurotrophin signaling pathway was the most-enriched KEGG pathway based on the AS events. Necroptosis, NOD receptor signaling, and tumor necrosis factor signaling pathways were also among the top 20 enriched pathways; however, they were not significant based on the FDR < 0.05 threshold (Figure 4(G)). Considering the critical roles of these pathways in inflammation, AS may also contribute to the therapeutic effects of IDR in DSS-induced colitis.