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Peer-reviewedCC BY 4.0Frontiers in Bioengineering and Biotechnology

Copine proteins and derived bioactive peptides in tissue development and regeneration: from molecular mechanisms to biomaterial functionalization

  1. 1Laboratory of Tissue Engineering and Regenerative Medicine, Department of Anatomy, Division of Embryology, Faculty of Medicine, Medical University of Gdańsk, Gdańsk, Poland
  2. 2Department of Biochemistry, University of Physical Education and Sport, Gdańsk, Poland

Abstract

The Copine (CPNE) family comprises evolutionarily conserved, calcium-dependent phospholipid-binding proteins (CPNE1-CPNE9) that function as intracellular membrane adapters and signaling modulators. In response to intracellular Ca2+ fluctuations, CPNE proteins translocate to the plasma membrane and recruit specific effector proteins, thereby integrating calcium dynamics with membrane remodeling, vesicular transport, and cell differentiation. While individual members display tissue-specific expression patterns-such as CPNE6 in hippocampal synaptic plasticity and CPNE7 in mesenchymal cell differentiation during odontogenesis-recent translational focus has centered on CPNE-derived bioactive peptides. Short synthetic sequences derived from the CPNE7 C2B-vWA junction region, specifically Cpne7-DP and CDP4, replicate key pro-regenerative functions of full - length proteins without requiring cell - surface receptor binding. When functionalized into biomaterial matrices (such as collagen gels and chitosan hydrogels via modified sequences UG27 and UG28), these peptides stimulate dentin tubule regeneration, osteogenic lineage commitment, biomineralization, and chondrocyte extracellular matrix deposition and angiogenesis. This review synthesizes current knowledge on CPNE structural biology, intracellular membrane translocation mechanisms, physiological tissue development, and oncological diagnostic markers.

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BibTeX
@article{tyminska2026copine,
  title = {{Copine proteins and derived bioactive peptides in tissue development and regeneration: from molecular mechanisms to biomaterial functionalization}},
  author = {A. Tymińska and A. Kowalska and M. Rogińska and M. Pikuła},
  journal = {Frontiers in Bioengineering and Biotechnology},
  year = {2026},
  month = oct,
  doi = {10.3389/fbioe.2026.1889849},
  url = {https://doi.org/10.3389/fbioe.2026.1889849},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Copine proteins and derived bioactive peptides in tissue development and regeneration: from molecular mechanisms to biomaterial functionalization
AU  - A. Tymińska
AU  - A. Kowalska
AU  - M. Rogińska
AU  - M. Pikuła
PY  - 2026
DA  - 2026/10/21
JO  - Frontiers in Bioengineering and Biotechnology
DO  - 10.3389/fbioe.2026.1889849
UR  - https://doi.org/10.3389/fbioe.2026.1889849
AB  - The Copine (CPNE) family comprises evolutionarily conserved, calcium-dependent phospholipid-binding proteins (CPNE1-CPNE9) that function as intracellular membrane adapters and signaling modulators. In response to intracellular Ca2+ fluctuations, CPNE proteins translocate to the plasma membrane and recruit specific effector proteins, thereby integrating calcium dynamics with membrane remodeling, vesicular transport, and cell differentiation. While individual members display tissue-specific expression patterns-such as CPNE6 in hippocampal synaptic plasticity and CPNE7 in mesenchymal cell differentiation during odontogenesis-recent translational focus has centered on CPNE-derived bioactive peptides. Short synthetic sequences derived from the CPNE7 C2B-vWA junction region, specifically Cpne7-DP and CDP4, replicate key pro-regenerative functions of full - length proteins without requiring cell - surface receptor binding. When functionalized into biomaterial matrices (such as collagen gels and chitosan hydrogels via modified sequences UG27 and UG28), these peptides stimulate dentin tubule regeneration, osteogenic lineage commitment, biomineralization, and chondrocyte extracellular matrix deposition and angiogenesis. This review synthesizes current knowledge on CPNE structural biology, intracellular membrane translocation mechanisms, physiological tissue development, and oncological diagnostic markers.
SN  - 2296-4185
ER  -