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MAP kinase pathways involving hsp27 regulate fibroblast-mediated wound contraction
Sahoko Hirano1, Riley S Rees, Robert R Gilmont
1Department of Surgery, University of Michigan Medical Center, Ann Arbor, Michigan 48109, USA.
The Journal of Surgical Research
|February 14, 2002
Summary
Heat shock protein 27 (hsp27) phosphorylation is linked to wound contraction. Inhibiting specific kinases (MAPK, ERK, p38) reduced hsp27 phosphorylation and delayed wound healing in models.
Area of Science:
- Cellular Biology
- Wound Healing Research
- Protein Kinase Signaling
Background:
- Heat shock protein 27 (hsp27) phosphorylation influences actin dynamics.
- Mitogen-activated protein (MAP) kinases regulate hsp27 phosphorylation via MAP kinase-activated protein kinase 2/3.
Purpose of the Study:
- To investigate the role of hsp27 phosphorylation in modulating wound contraction.
- To determine the involvement of p38 and ERK kinase pathways in hsp27-mediated wound contraction.
Main Methods:
- Utilized fibroblast-populated collagen lattice (FPCL) and rat skin defect models.
- Administered specific inhibitors for p38 MAP kinase (SB203580) and ERK kinase (PD98059).
- Assessed hsp27 phosphorylation status using isoelectric focusing and Western blot analysis.
Main Results:
- hsp27 phosphorylation positively correlated with both in vitro (FPCL) and in vivo wound contraction.
- Kinase inhibitors reduced FPCL contraction and hsp27 phosphorylation.
- Inhibition of p38 and ERK pathways significantly delayed wound contraction in vivo, accompanied by reduced hsp27 phosphorylation.
Conclusions:
- ERK and p38 kinase cascades are critical for wound contraction.
- hsp27 acts as a key mediator in the effects of these kinase pathways on wound contraction.