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Dentin matrix protein-1 isoforms promote differential cell attachment and migration
Zofia von Marschall1, Larry W Fisher
1Craniofacial and Skeletal Diseases Branch, NIDCR, National Institutes of Health, Bethesda, Maryland 20892-4320, USA.
The Journal of Biological Chemistry
|September 30, 2008
Summary
Dentin matrix protein-1 (DMP1), bone sialoprotein (BSP), and osteopontin (OPN) are SIBLING proteins crucial for cell interactions. This study reveals cells discriminate between these proteins and DMP1 isoforms, impacting attachment and migration.
Area of Science:
- Biochemistry
- Cell Biology
- Biomaterials Science
Background:
- Dentin matrix protein-1 (DMP1), bone sialoprotein (BSP), and osteopontin (OPN) are SIBLING proteins involved in skeletal and epithelial cell functions.
- Mutations in DMP1 are linked to human disease, yet it is the least studied of the three.
- All three SIBLINGs contain a conserved RGD motif essential for integrin binding.
Purpose of the Study:
- To compare the cell attachment and migration-enhancing properties of DMP1, BSP, and OPN.
- To investigate the role of integrin binding and specific protein domains in mediating these cellular responses.
- To explore cellular discrimination among SIBLINGs and DMP1 isoforms.
Main Methods:
- Cell attachment and haptotactic migration assays using human skeletal (MG63, dental pulp) and salivary gland (HSG) cells.
- Experiments involving mutation of the RGD motif and manipulation of protein sequences (exon swapping).
- Investigation of integrin subtypes (alphaVbeta5 and alphaVbeta3) and DMP1 isoforms (proteoglycan, BMP1-cleaved fragment).
Main Results:
- RGD motif mutation abolished cell attachment and migration for all SIBLINGs.
- HSG cells exhibited differential attachment and migration based on integrin expression (alphaVbeta5 vs. alphaVbeta3) and SIBLING type.
- DMP1 isoforms showed varying abilities in cell attachment and migration, with the proteoglycan isoform being significantly reduced.
Conclusions:
- Cellular responses to DMP1, BSP, and OPN are integrin-dependent and protein-specific.
- DMP1's functional domains and post-translational modifications significantly influence its cell-interactive properties.
- Cells demonstrate discrimination among SIBLING proteins and DMP1 isoforms, highlighting nuanced biological roles.
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