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Papers In Press, published online ahead of print August 14, 2002
Dermatology, Ehime University School of Medicine, Onsengun, Ehime 791-0295
Corresponding Author: sayama{at}m.ehime-u.ac.jp
The survival and growth of epithelial cells depend on adhesion to the extracellular matrix. Since epidermal keratinocytes differentiate as they leave the basement membrane, an adhesion signal may regulate the initiation of differentiation. Phosphatidyl inositol (PI) 3 kinase is a fundamental signaling molecule that regulates the adhesion signal. Transfection of a dominant-negative form of PI3 kinase into keratinocytes using an adenovirus vector resulted in significant morphological changes comparable to differentiation and the induction of differentiation markers, keratin (K) 1, and K10. In turn, transfection with the constitutively active form of PI3 kinase almost completely abolished the induction of K1 and K10 by differentiation in suspension cultures using poly-HEMA-coated dishes. PI3 kinase activity was lost in suspension culture, except by cells bearing the constitutively active form of PI3 kinase. These data demonstrate that blockade of PI3 kinase results in differentiation, and that activation of PI3 kinase prevents differentiation. Furthermore, expression of the dominant-negative form of PI3 kinase significantly inhibited keratinocyte adhesion to the extracellular matrix and reduced the surface expression of
J. Biol. Chem, 10.1074/jbc.M112423200
Submitted on December 28, 2001
Revised on August 14, 2002
Accepted on August 14, 2002
Phosphatidyl inositol 3 kinase is a key regulator of early phase differentiation in keratinocytes
6 and 
1 integrins in suspension culture. Moreover, expression of the active form of PI3 kinase restored the mRNA levels of adhesion molecules that were reduced in suspension culture, including 3, 6, and 1 integrins, BP180, and BP230. In conclusion, loss of PI3 kinase activity results in keratinocytes leaving the basement membrane and the initiation of a “default” differentiation mechanism.
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