Cited by 212Bone and Dental Protein Studiesdental development and anomaliesAlkaline Phosphatase Research Studies

Genetic basis for the evolution of vertebrate mineralized tissue

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Kawasaki, Kazuhiko, Suzuki, Tohru, Weiss, Kenneth M.·2004·Proceedings of the National Academy of Sciences

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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Crossref · 10.1073/pnas.0404279101

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  • The SCPP gene family arose via a series of gene duplications after the echinoderm-chordate divergence.

    “which supports the hypothesis that this family arose via a series of gene duplications after the echinoderm-chordate divergence (51).”

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Authors
Kawasaki, K., Suzuki, T., & Weiss, K. M.
Affiliations
Pennsylvania State University (US)
Venue
Proceedings of the National Academy of Sciences
Published
2004-07-22
Volume
101
Issue
31
Pages
11356-11361
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
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
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Rheumatology › Bone and Dental Protein Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › 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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