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首页> 外文期刊>Protoplasma: An International Journal of Cell Biology >Immunolocalization of alpha-keratins and associated beta-proteins in lizard epidermis shows that acidic keratins mix with basic keratin-associated beta-proteins
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Immunolocalization of alpha-keratins and associated beta-proteins in lizard epidermis shows that acidic keratins mix with basic keratin-associated beta-proteins

机译：蜥蜴表皮中的α-角蛋白和相关β蛋白的免疫定位表明，酸性角蛋白与碱性角蛋白相关的β蛋白混合在一起

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摘要

The differentiation of the corneous layers of lizard epidermis has been analyzed by ultrastructural immunocytochemistry using specific antibodies against alpha-keratins and keratin associated beta-proteins (KAbetaPs, formerly indicated as beta-keratins). Both beta-cells and alpha-cells of the corneous layer derive from the same germinal layer. An acidic type I alpha-keratin is present in basal and suprabasal layers, early differentiating clear, oberhautchen, and beta-cells. Type I keratin apparently disappears in differentiated beta- and alphalayers of the mature corneous layers. Conversely, a basic type II alpha-keratin rich in glycine is absent or very scarce in basal and suprabasal layers and this keratin likely does not pair with type I keratin to form intermediate filaments but is weakly detected in the pre-corneous and corneous alpha-layer. Single and double labeling experiments show that in differentiating beta-cells, basic KAbetaPs are added and replace type-I keratin to form the hard beta-layer. Epidermal alpha-keratins contain scarce cysteine (0.2-1.4 %) that instead represents 4- 19 % of amino acids present in KAbetaPs. Possible chemical bonds formed between alpha-keratins and KAbetaPs may derive from electrostatic interactions in addition to crosslinking through disulphide bonds. Both the high content in glycine of keratins and KAbetaPs may also contribute to increase the hydrophobicy of the beta- and alpha-layers and the resistance of the corneous layer. The increase of gly-rich KAbetaPs amount and the bonds to the framework of alphakeratins give rise to the inflexible beta-layer while the cys-rich KAbetaPs produce a pliable alpha-layer.
机译：蜥蜴表皮角质层的分化已通过超结构免疫细胞化学分析，使用针对α-角蛋白和角蛋白相关β蛋白（KAbetaP，以前表示为β-角蛋白）的特异性抗体。角质层的β细胞和α细胞均来自同一生发层。酸性I型α-角蛋白存在于基底层和基底层中，可早期区分透明细胞，上清细胞和β细胞。 I型角蛋白显然在成熟角质层的分化的β-和α层中消失。相反，基底层和基底上层缺乏或富含甘氨酸的基本II型α-角蛋白，这种角蛋白可能不会与I型角蛋白配对形成中间的细丝，但在角质层和角质层的α-角蛋白中检测不到。层。单标记和双标记实验表明，在区分β细胞的过程中，添加了基本的KAbetaP，并取代了I型角蛋白以形成硬β层。表皮α-角蛋白含有稀缺的半胱氨酸（0.2-1.4％），而它代表了KAbetaPs中存在的氨基酸的4-19％。除通过二硫键交联外，α-角蛋白与KAbetaP之间可能形成的化学键还可能源自静电相互作用。甘氨酸的角蛋白和KAbetaPs中的高含量都可能有助于增加β-和α-层的疏水性和角质层的抵抗力。富含甘氨酸的KAbetaPs数量的增加以及与α-角蛋白骨架的键合形成了非柔性的β-层，而富含cys的KAbetaPs产生了柔韧的α-层。

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