| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 3213765 | Journal of Dermatological Science | 2010 | 7 Pages |
BackgroundNo previous report has investigated the involvement of glycolytic enzymes in keratinocyte migration. Fructose-1,6-bisphosphate aldolase A (ALDOA) is a glycolytic enzyme bound to the cytoskeleton by certain growth factors, which are known to enhance keratinocyte migration. We postulated that ALDOA is involved in keratinocyte migration.ObjectiveTo investigate the possible role of ALDOA in keratinocyte migration.MethodsThe localization of endogenous ALDOA and the actin cytoskeleton was observed by laser scanning confocal microscopy in HaCaT cells. The effects of ALDOA on lamellipodia formation and migration were evaluated using ALDOA siRNA-transfected cells. In addition, the involvement of epidermal growth factor (EGF) in ALDOA-induced events was investigated.ResultsStrong ALDOA expression was observed along the ruffling membrane and lamellipodia, and it was colocalized with the actin cytoskeleton in lamellipodia. In a scratch wound assay, the wound recovery area was significantly decreased on transfection with ALDOA siRNA. The rate of lamellipodia-forming cells also decreased. On stimulation with EGF, the wound recovery area and ALDOA and its mRNA levels increased. On the other hand, ALDOA siRNA transfection suppressed EGF-enhanced migration.ConclusionWe concluded that ALDOA is involved in keratinocyte migration following the induction of lamellipodia formation, and ALDOA-related migration is enhanced by EGF.
