ArticleProceedings of the National Academy of Sciences of the United States of America2004
Genetic basis for the evolution of vertebrate mineralized tissue.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.
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81 citing papers in PubMed, 209 citations in OpenAlex.
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- Dynamics of Dental Enamel Surface Remineralization under the Action of Toothpastes with Substituted Hydroxyapatite and Birch Extract.Materials (Basel, Switzerland) · 2024Article
- Emergence of saliva protein genes in the secretory calcium-binding phosphoprotein (SCPP) locus and accelerated evolution in primates.bioRxiv : the preprint server for biology · 2024Article
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- A Comprehensive Genomic Analysis of Chinese Indigenous Ningxiang Pigs: Genomic Breed Compositions, Runs of Homozygosity, and Beyond.International journal of molecular sciences · 2023Article
- Overexpression of ameloblastin in secretory ameloblasts results in demarcated, hypomineralized opacities in enamel.Frontiers in physiology · 2023Article
- Renal osteodystrophy: A historical review of its origins and conceptual evolution.Bone reports · 2022Review
- Parallel Evolution of Ameloblastic scpp Genes in Bony and Cartilaginous Vertebrates.Molecular biology and evolution · 2022Article
- Redeployment of odontode gene regulatory network underlies dermal denticle formation and evolution in suckermouth armored catfish.Scientific reports · 2022Article
21 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Mineralized tissue is vital to many characteristic adaptive phenotypes in vertebrates. Three primary tissues, enamel (enameloid), dentin, and bone, are found in the body armor of ancient agnathans and mammalian teeth, suggesting that these two organs are homologous. Mammalian enamel forms on enamel-specific proteins such as amelogenin, whereas dentin and bone form on collagen and many acidic proteins, such as SPP1, coordinately regulate their mineralization. We previously reported that genes for three major enamel matrix proteins, five proteins necessary for dentin and bone formation, and milk caseins and salivary proteins arose from a single ancestor by tandem gene duplications and form the secretory calcium-binding phosphoprotein (SCPP) family. Gene structure and protein characteristics show that SCPP genes arose from the 5' region of ancestral sparcl1 (SPARC-like 1). Phylogenetic analysis on SPARC and SPARCL1 suggests that the SCPP genes arose after the divergence of cartilaginous fish and bony fish, implying that early vertebrate mineralization did not use SCPPs and that SPARC may be critical for initial mineralization. Consistent with this inference, we identified SPP1 in a teleost genome but failed to find any genes orthologous to mammalian enamel proteins. Based on these observations, we suggest a scenario for the evolution of vertebrate tissue mineralization, in which body armor initially formed on dermal collagen, which acted as a reinforcement of dermis. We also suggest that mammalian enamel is distinct from fish enameloid. Their similar nature as a hard structural overlay on exoskeleton and teeth is because of convergent evolution.
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