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Localization and characterization of specific cornification proteins in avian epidermis.

机译:禽表皮中特定角质蛋白的定位和表征。

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Little is known about proteins involved in the formation of the stratum corneum in the avian apteric epidermis. The present immunocytochemical, autoradiographic and electrophoretic study shows that antibodies against characteristic proteins of mammalian cornification (alpha-keratins, loricrin, sciellin, filaggrin, transglutaminase) recognize avian epidermal proteins. This suggests the presence of avian protein with epitopes common to related mammalian proteins. These proteins may also be involved in the formation of the cornified core and cell envelope of mature avian corneocytes. The immunoblotting study suggests that protein bands, cross-reactive for antibodies against loricrin (45, 52-57 kDa), sciellin (54, 84 kDa), filaggrin (32, 38, 45-48 kDa), and transglutaminase (40, 50, 58 kDa), are present in the avian epidermis. Immunocytochemistry shows that immunoreactivity for the above proteins is localized in the transitional and lowermost corneous layer of apteric epidermis. Their epitopes are rapidly masked/altered in cornifying cells and are no longer detectable in mature corneocytes. In scaled epidermis a thick layer made of beta-keratins of 14-18, 20-22, and 33 kDa is formed. Only in feathered epidermis (not in scale epidermis), an antifeather chicken beta-keratin antibody recognized a protein band at 8-12 kDa. This small beta-keratin is probably suitable for the formation of long, axial filaments in elongated barb, barbule and calamus cells. Conversely, the larger beta-keratins in scales are irregularly deposited forming flat plates. Tritiated histidine coupled to autoradiography show an absence of both keratohyalin and histidine-rich proteins in adult feathered and scaled epidermis. Most of the labeling appears in proteins within the range of beta- and alpha-keratins. These data on apteric epidermis support the hypothesis of an evolution of the apteric and interfollicular epidermis from the expansion of hinge regions of protoavian archosaurians.
机译:关于在鸟的精子表皮中形成角质层的蛋白质知之甚少。目前的免疫细胞化学,放射自显影和电泳研究表明,针对哺乳动物角质化特征蛋白(α-角蛋白,loricrin,sciellin,丝聚蛋白,转谷氨酰胺酶)的抗体可识别禽类表皮蛋白。这表明存在禽蛋白以及相关哺乳动物蛋白共有的表位。这些蛋白质也可能参与成熟禽角质细胞的角质化核心和细胞包膜的形成。免疫印迹研究表明,蛋白带与针对Loricrin(45,52-57 kDa),sciellin(54,84 kDa),丝聚蛋白(32、38、45-48 kDa)和转谷氨酰胺酶(40,50)的抗体具有交叉反应性(58 kDa),存在于禽表皮中。免疫细胞化学表明,上述蛋白质的免疫反应性定位在过渡和最下面的角质层表皮中。它们的表位在角质形成细胞中迅速被掩盖/改变,而在成熟的角质细胞中不再可检测到。在鳞片状表皮中,形成了由14-18、20-22和33 kDa的β-角蛋白制成的厚层。只有在羽毛状的表皮中(而不是鳞状表皮中),抗羽毛鸡的β-角蛋白抗体才能识别8-12 kDa的蛋白带。这种小的β-角蛋白可能适合在细长的倒钩,鳞茎和and蒲细胞中形成长的轴向细丝。相反,规模较大的β-角蛋白会不规则沉积,形成平板。 ti化的组氨酸与放射自显影结合显示在成年羽毛和成鳞的表皮中不存在角蛋白透明质酸和富含组氨酸的蛋白质。大多数标记出现在β-角蛋白和α-角蛋白范围内的蛋白质中。这些关于无翅表皮的数据支持假说,即原甲考古学家的铰链区扩展了无翅表皮和小孔间表皮的演变。

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