Scpppq1-KO Mouse

Scpppq1, or secretory calcium-binding phosphoprotein-proline-glutamine-rich 1, is a gene within the secretory calcium-binding phosphoprotein (Scpp) cluster. The SCPPPQ1 protein it encodes is a 75-residue, highly conserved, secreted protein rich in proline, leucine, glutamine and phenylalanine. It plays a crucial role in mediating the attachment of epithelial cells to mineralized tooth surfaces by participating in structuring the basal lamina at the cell-tooth interface [2]. It may also be involved in the evolution of milk casein genes as suggested by exon-intron structure and phylogenetic analysis [4].

Functional studies show that the SCPPPQ1/LAM332 protein complex enhances the adhesion and migration of oral epithelial cells, which has implications for dentogingival regeneration. The complex has a high-affinity adsorption for hydroxyapatite, the main component of mineralized tooth surfaces, and can double the adhesion strength of oral epithelial cells to HA compared to LAM332 alone. Gingival epithelial cells also show a significantly high migration rate over SCPPPQ1/LAM332-coated surfaces [1]. Additionally, SCPPPQ1 exhibits antimicrobial properties against Porphyromonas gingivalis, a major periodontopathogen. It can decrease bacterial number, form aggregates, and disrupt the bacterial membrane, with specific regions of the molecule sustaining these effects [3,5].

In conclusion, Scpppq1 is essential for the attachment of epithelial cells to tooth surfaces and shows potential in enhancing dentogingival regeneration. Its antimicrobial properties also suggest a role in maintaining oral health by protecting against periodontopathogens. The study of Scpppq1 provides insights into the mechanisms of epithelial attachment and antibacterial defense in the oral cavity, which could potentially lead to new strategies for treating periodontal diseases [1,2,3,5].

References:

1. Nouri, Shahrzad, Holcroft, James, Caruso, Laura-Lee, Master, Emma R, Ganss, Bernhard. 2022. An SCPPPQ1/LAM332 protein complex enhances the adhesion and migration of oral epithelial cells: Implications for dentogingival regeneration. In Acta biomaterialia, 147, 209-220. doi:10.1016/j.actbio.2022.05.035. https://pubmed.ncbi.nlm.nih.gov/35643199/

2. Moffatt, Pierre, Wazen, Rima M, Dos Santos Neves, Juliana, Nanci, Antonio. 2014. Characterisation of secretory calcium-binding phosphoprotein-proline-glutamine-rich 1: a novel basal lamina component expressed at cell-tooth interfaces. In Cell and tissue research, 358, 843-55. doi:10.1007/s00441-014-1989-3. https://pubmed.ncbi.nlm.nih.gov/25193156/

3. Fouillen, Aurélien, Mary, Charline, Ponce, Katia Julissa, Moffatt, Pierre, Nanci, Antonio. 2021. A proline rich protein from the gingival seal around teeth exhibits antimicrobial properties against Porphyromonas gingivalis. In Scientific reports, 11, 2353. doi:10.1038/s41598-021-81791-7. https://pubmed.ncbi.nlm.nih.gov/33504866/

4. Kawasaki, Kazuhiko, Lafont, Anne-Gaelle, Sire, Jean-Yves. 2011. The evolution of milk casein genes from tooth genes before the origin of mammals. In Molecular biology and evolution, 28, 2053-61. doi:10.1093/molbev/msr020. https://pubmed.ncbi.nlm.nih.gov/21245413/

5. Mary, Charline, Fouillen, Aurélien, Moffatt, Pierre, Grenier, Daniel, Nanci, Antonio. 2021. Effect of human secretory calcium-binding phosphoprotein proline-glutamine rich 1 protein on Porphyromonas gingivalis and identification of its active portions. In Scientific reports, 11, 23724. doi:10.1038/s41598-021-02661-w. https://pubmed.ncbi.nlm.nih.gov/34887426/