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Am J Physiol Cell Physiol 281: C603-C614, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 2, C603-C614, August 2001

A role for MAP kinase in regulating ectodomain shedding of APLP2 in corneal epithelial cells

Ke-Ping Xu1, Driss Zoukhri1, James D. Zieske1, Darlene A. Dartt1, Christian Sergheraert2, Estelle Loing2, and Fu-Shin X. Yu1

1 Schepens Eye Research Institute and Department of Ophthalmology, Harvard Medical School, Boston, Massachusetts 02114; and 2 UMR 8525, Lille II University, Institut de Biologie et Institut Pasteur de Lille, 59021 Lille, France

We previously reported an increased secretion of amyloid precursor-like protein 2 (APLP2) in the healing corneal epithelium. The present study sought to investigate signal transduction pathways involved in APLP2 shedding in vitro. APLP2 was constitutively shed and released into culture medium in SV40-immortalized human corneal epithelial cells as assessed by Western blotting, flow cytometry, and indirect immunofluorescence. Activation of protein kinase C (PKC) by phorbol 12-myristate 13-acetate (PMA) caused significant increases in APLP2 shedding. This was inhibited by staurosporine and a PKC-epsilon -specific, N-myristoylated peptide inhibitor. Epidermal growth factor (EGF) also induced APLP2 accumulation in culture medium. Basal APLP2 shedding as well as that induced by PMA and EGF was blocked by a mitogen-activated protein kinase (MAPK) kinase inhibitor, U-0126. Our results suggest that MAPK activity accounts for basal as well as PKC- and EGF-induced APLP2 shedding. In addition, PKC-epsilon may be involved in the induction of APLP2 shedding in corneal epithelial cells.

amyloid precursor-like protein 2; ectodomain shedding; epidermal growth factor; protein kinase C; mitogen-activated protein kinase


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