KERATOHYALIN GRANULES ARE HETEROGENEOUS IN RIDGED AND NON-RIDGED HUMAN SKIN - EVIDENCE FROM ANTI-FILAGGRIN IMMUNOGOLD LABELING OF NORMAL SKIN AND SKIN OF AUTOSOMAL DOMINANT ICHTHYOSIS-VULGARIS PATIENTS
KERATOHYALIN GRANULES ARE HETEROGENEOUS IN RIDGED AND NON-RIDGED HUMAN SKIN - EVIDENCE FROM ANTI-FILAGGRIN IMMUNOGOLD LABELING OF NORMAL SKIN AND SKIN OF AUTOSOMAL DOMINANT ICHTHYOSIS-VULGARIS PATIENTS
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DOI：
10.1007/bf00371777
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发表时间：
1991-01-01
影响因子：
3
通讯作者：
ANTONLAMPRECHT, I
中科院分区：
文献类型：
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作者：
GUNZEL, S;WEIDENTHALER, B;ANTONLAMPRECHT, I
最近的生化和形态学研究为人类皮肤中角质透明蛋白的异质成分提供了证据。主要成分是聚丝蛋白。在毛囊间表皮中，透明角质蛋白的异质性不直接可见，而在正常脊状皮肤中，通过电子显微镜可显示双组分透明角质蛋白。使用商业单克隆抗丝聚蛋白抗体，通过常规透射电子显微镜和免疫金包埋技术，对正常个体和常染色体显性寻常鱼鳞病 (ADI) 患者的脊状和非脊状皮肤进行皮肤活检，其特征是透明角质蛋白合成缺陷和丝聚蛋白缺乏。在正常的毛囊间表皮中，在角化透明蛋白颗粒和最下面的角化细胞中证实了丝聚蛋白标记，而在ADI患者中，存在易碎的角化透明蛋白颗粒，其没有显示丝聚蛋白的特异性标记。在正常的脊状皮肤中，只有主要（电子密度较高）成分与抗聚丝蛋白发生反应，而附着的（电子密度较低）成分则不发生反应。 ADI 患者的脊状皮肤含有不与抗聚丝蛋白发生反应的球状透明角质蛋白，因此与正常脊状皮肤中附着的角质透明蛋白成分相对应。我们的结果为最近对透明角质蛋白异质性的生化研究提供了可见的对应物，并有助于理解人类皮肤的终末分化和 ADI 中透明角质蛋白合成的缺陷。
Recent biochemical and morphological investigations have provided evidence for a heterogeneous composition of keratohyalin in human skin. A major component is filaggrin. In interfollicular epidermis the heterogeneity of keratohyalin is not directly visible, whereas in normal ridged skin bicomponent keratohyalin is revealed by electron microscopy. Skin biopsies of ridged and non-ridged skin of normal individuals and patients with autosomal dominant ichthyosis vulgaris (ADI) - characterized by defective keratohyalin synthesis and lack of filaggrin - were investigated by routine transmission electron microscopy and immunogold postembedding techniques using a commercial monoclonal anti-filaggrin antibody. In normal interfollicular epidermis filaggrin labelling was demonstrated on keratohyalin granules and in the lowermost cornified cells, whereas in ADI patients crumbly keratohyalin granules were present that did not show specific labelling for filaggrin. in normal ridged skin only the major (more electron-dense) component reacted with anti-filaggrin, whereas the attached (less electron-dense) component did not react. Ridged skin of ADI patients contained globular keratohyalin that did not react with anti-filaggrin, thus corresponding to the attached keratohyalin component in normal ridged skin. Our results provide a visible counterpart to the recent biochemical investigations of keratohyalin protein heterogeneity and contribute to the understanding of terminal differentiation in human skin and of the defective keratohyalin synthesis in ADI.