Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in ichthyosis vulgaris.
Interaction of filaggrin with keratin filaments during advanced stages of normal human epidermal differentiation and in ichthyosis vulgaris.
复制标题
在正常人表皮分化的晚期阶段和寻常鱼鳞病中，聚丝蛋白与角蛋白丝的相互作用。
DOI：
10.1111/j.1432-0436.1991.tb00241.x
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发表时间：
1991
期刊：
影响因子：
--
通讯作者：
Dale,BA
中科院分区：
文献类型：
--
作者：
Manabe,M;Sanchez,M;Sun,TT;Dale,BA
Filaggrin is a histidine‐rich, basic protein whose name was first proposed based on its ability to aggregate intermediate filaments in vitro. Based on this in vitro observation, it has generally been assumed that filaggrin functions in vivo as a matrix protein which causes keratin filaments to become densely packed in the terminally differentiated cornified cells. Inconsistent with this view, however, is the well‐known observation that keratin aggregation appears to proceed normally in the affected epidermis of ichthyosis vulgaris patients despite a greatly reduced quantity of filaggrin. To address this issue, we used immuno‐electron microscopy to localize filaggrin and its cross‐reactive precursor, pro‐filaggrin, in human and mouse epidermis, as well as in ichthyosis vulgaris epidermis. We found that the localization of filaggrin in lower cornified cells correlates precisely with the formation of aggregated keratin filaments, and the disappearance of filaggrin in upper cornified cells correlates precisely with the loosening of keratin filaments. Furthermore, we showed that, even in ichthyosis vulgaris, small amounts of filaggrin/profilaggrin are present as electron‐dense deposits associated with keratin filaments in the granular cells, and that the localization of this small amount of antigen again correlates with the aggregation state of keratin filaments. These data strongly suggest that filaggrin is indeed involved in filament aggregation in vivo.
