4.1 Article

Cornification in reptilian epidermis occurs through the deposition of keratin-associated beta-proteins (beta-keratins) onto a scaffold of intermediate filament keratins

期刊

JOURNAL OF MORPHOLOGY
卷 274, 期 2, 页码 175-193

出版社

WILEY
DOI: 10.1002/jmor.20086

关键词

reptiles; scales; alpha-keratins; beta-proteins; ultrastructure; immunocytochemistry

资金

  1. Comparative Histolab
  2. Italian Ministry of Education and Scientific Research [2008 AXS E-002]

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The isolation of genes for alpha-keratins and keratin-associated beta-proteins (formerly beta-keratins) has allowed the production of epitope-specific antibodies for localizing these proteins during the process of cornification epidermis of reptilian sauropsids. The antibodies are directed toward proteins in the alpha-keratin range (4070 kDa) or beta-protein range (1030 kDa) of most reptilian sauropsids. The ultrastructural immunogold study shows the localization of acidic alpha-proteins in suprabasal and precorneous epidermal layers in lizard, snake, tuatara, crocodile, and turtle while keratin-associated beta-proteins are localized in precorneous and corneous layers. This late activation of the synthesis of keratin-associated beta-proteins is typical for keratin-associated and corneous proteins in mammalian epidermis (involucrin, filaggrin, loricrin) or hair (tyrosine-rich or sulfur-rich proteins). In turtles and crocodilians epidermis, keratin-associated beta-proteins are synthesized in upper spinosus and precorneous layers and accumulate in the corneous layer. The complex stratification of lepidosaurian epidermis derives from the deposition of specific glycine-rich versus cysteine-glycine-rich keratin-associated beta-proteins in cells sequentially produced from the basal layer and not from the alternation of beta- with alpha-keratins. The process gives rise to Oberhautchen, beta-, mesos-, and alpha-layers during the shedding cycle of lizards and snakes. Differently from fish, amphibian, and mammalian keratin-associated proteins (KAPs) of the epidermis, the keratin-associated beta-proteins of sauropsids are capable to form filaments of 34 nm which give rise to an X-ray beta-pattern as a consequence of the presence of a beta-pleated central region of high homology, which seems to be absent in KAPs of the other vertebrates. J. Morphol., 2013. (c) 2012 Wiley Periodicals, Inc.

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