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Arch Dermatol Res. 2000 Oct;292(10):496-9.

Membrane expression of annexin I is enhanced by calcium and TPA in cultured human keratinocytes.

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Department of Dermatology, Hokkaido University School of Medicine, Kita 15, Nishi 7, Kita-ku, Sapporo, 060-8638, Japan.


Annexin I plays an important role in the process of keratinization as a component of the cornified envelope. To elucidate the function of annexin I in keratinization, we investigated the effects of calcium, epinephrine, hydrocortisone, and 12-O-tetradecanoyl phorbol 13-acetate (TPA) on the expression and localization of annexin I in cultured human keratinocytes. Normal human keratinocytes were cultured in serum-free culture medium (0.15 mM calcium) until 70% confluence. After incubation with a higher concentration of calcium (1.8 mM), TPA (100 nM), epinephrine (50 microM), or hydrocortisone (10 microM) for 24 h, the expression of annexin I protein and mRNA was examined using immunofluorescence, Western blot, and Northern blot techniques. Immunofluorescence microscopy showed increased membrane staining of annexin I by calcium, which was inhibited by the addition of epinephrine or hydrocortisone. Western blotting confirmed elevated annexin I on the cell membrane. It was increased in the cell membrane fraction, but not in the cytosol fraction. Interestingly, the mRNA level of annexin I was slightly reduced after incubation with calcium, whereas TPA upregulated both membrane expression and the mRNA level. Secretion of annexin I was increased by TPA but inhibited by calcium. Because calcium and TPA are known to promote keratinization, our data suggest that annexin I expression on the cell membrane is involved in the process of keratinization.

[Indexed for MEDLINE]

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