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Genetic basis for the evolution of vertebrate mineralized tissue
Open accessAbstract
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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“which supports the hypothesis that this family arose via a series of gene duplications after the echinoderm-chordate divergence (51).”
From The Genome of the Sea Urchin Strongylocentrotus purpuratus (2006) · cites this paper as [51]
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Metadata
- Authors
- Kawasaki, K., Suzuki, T., & Weiss, K. M.
- Affiliations
- Pennsylvania State University (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2004-07-22
- Volume
- 101
- Issue
- 31
- Pages
- 11356-11361
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC509207
- OpenAlex
- W2081946704
- Cited by
- 212
- References
- 65
- Citations by year
- 2026: 4 · 2025: 5 · 2024: 9 · 2023: 6 · 2022: 7 · 2021: 9 · 2020: 9 · 2019: 7 · 2018: 8 · 2017: 6 · 2016: 8 · 2015: 16 · 2014: 7 · 2013: 24 · 2012: 12
- FWCI
- 6.98
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Bone and Dental Protein Studies
- Health Sciences › Dentistry › General Dentistry › dental development and anomalies
- Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Alkaline Phosphatase Research Studies
- Keywords
- enamel, dentin, bone, enamel matrix proteins, amelogenin, SPARC, SPARCL1, osteopontin, tandem gene duplication, jawless fishes, teleosts, milk casein, salivary proteins, collagen, convergent evolution, homology
- MeSH terms
- Animals, Bone and Bones, Calcification, Physiologic, Caseins, Collagen, Dental Enamel, Mammals, Molecular Sequence Data, Phylogeny, Vertebrates, Osteonectin, Evolution, Molecular, Takifugu
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