S100A7 (psoriasin) interacts with epidermal fatty acid binding protein and localizes in focal adhesion-like structures in cultured keratinocytes

被引:50
作者
Ruse, M
Broome, AM
Eckert, RL
机构
[1] Case Western Reserve Univ, Sch Med, Dept Physiol Biophys, Cleveland, OH 44106 USA
[2] Case Western Reserve Univ, Sch Med, Dept Biochem, Cleveland, OH 44106 USA
[3] Case Western Reserve Univ, Sch Med, Dept Reprod Biol, Cleveland, OH 44106 USA
[4] Case Western Reserve Univ, Sch Med, Dept Oncol, Cleveland, OH 44106 USA
[5] Case Western Reserve Univ, Sch Med, Dept Dermatol, Cleveland, OH 44106 USA
关键词
epidermal fatty acid binding protein; keratinocyte differentiation; psoriasin; psoriasis; signal transduction;
D O I
10.1046/j.1523-1747.2003.12309.x
中图分类号
R75 [皮肤病学与性病学];
学科分类号
100206 ;
摘要
S100 proteins are calcium-responsive signaling proteins that are overexpressed in cancer and inflammatory diseases. They act by forming complexes with target proteins to modify target protein function. Identifying S100 intracellular distribution, site of action, and protein targets are important goals. S100A7 (psoriasin) is an important member of this family that is markedly overexpressed in psoriatic keratinocytes; however, its role in disease progression is poorly understood. In this study, we express S100A7 in normal keratinocytes as a means to study S100A7 function. We show that S100A7 is present in the cytosol and in BiP/GRP78-positive (endoplasmic reticulum) tubular structures. When cells are challenged with elevated intracellular calcium, cytoplasmic S100A7 redistributes to alpha-actinin- and paxillin-positive peripheral structures that contact the substrate surface. Epidermal fatty acid binding protein is also overexpressed in psoriasis, and is a putative target of S100A7 in keratinocytes. To study this interaction, we coexpressed S100A7 and epidermal fatty acid binding protein. These studies indicate that S100A7 and epidermal fatty acid binding protein colocalize in the cytoplasm in untreated cultures, and localize in peripheral structures in response to calcium challenge. In addition, S100A7 expression appears to stabilize epidermal fatty acid binding protein level, and vice versa. Moreover, the proteins can be coprecipitated in the presence of bifunctional cross-linker, suggesting that they are part of a common complex. The colocalization with alpha-actinin and paxillin suggests that S100A7 and epidermal fatty acid binding protein colocalize in focal adhesion-like structures following calcium treatment.
引用
收藏
页码:132 / 141
页数:10
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