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Updated: Jun 14, 2026

Methods to Study Mrp4-containing Macromolecular Complexes in the Regulation of Fibroblast Migration
Published on: May 19, 2016
Fructose-1,6-bisphosphate aldolase A is involved in HaCaT cell migration by inducing lamellipodia formation
Takumi Tochio1, Hiroshi Tanaka, Satoru Nakata
1Graduate School of Biological Science, Hiroshima University, Higashihiroshima, Japan.
Background:
No 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.
Objective:
To investigate the possible role of ALDOA in keratinocyte migration.
Methods:
The 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.
Results:
Strong 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.
Conclusion:
We concluded that ALDOA is involved in keratinocyte migration following the induction of lamellipodia formation, and ALDOA-related migration is enhanced by EGF.
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