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PR-39, a syndecan-inducing antimicrobial peptide, binds and affects p130(Cas)
1Department of Dermatology and Division of Developmental and Newborn Medicine, Boston Children's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
The Journal of Biological Chemistry
|October 24, 1998
Summary
PR-39, an antimicrobial peptide, binds to SH3-containing proteins in mammalian cells. This interaction with signaling molecules like p130(Cas) helps explain PR-39
Area of Science:
- Biochemistry
- Cell Biology
- Immunology
Background:
- PR-39 is a proline-arginine-rich antimicrobial peptide crucial for innate immunity.
- Beyond antimicrobial activity, PR-39 influences mammalian cell gene expression and behavior.
Purpose of the Study:
- To elucidate the mechanism by which PR-39 affects mesenchymal cells.
- To identify specific binding targets of PR-39 using a biologically active fragment (PR-39(15)).
Main Methods:
- Investigated PR-39 binding to NIH 3T3 cells and lipid bilayers.
- Utilized PR-39(15) to identify cytoplasmic protein binding partners in human microvascular endothelial cells.
- Examined the interaction of PR-39(15) with SH3-containing proteins, including p130(Cas).
Main Results:
- PR-39 demonstrated saturable binding to NIH 3T3 cells, indicating specific target interaction.
- PR-39(15) interacted with lipid bilayers and entered endothelial cells, binding cytoplasmic proteins.
- PR-39(15) selectively bound SH3-containing proteins, including p130(Cas), and altered its cellular localization.
Conclusions:
- PR-39(15) binds to SH3-containing signal transduction molecules.
- This interaction with proteins like p130(Cas) provides a mechanistic basis for PR-39's effects on mammalian cell behavior.