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  • Title: Immunolocalization of keratin-associated beta-proteins (beta-keratins) in the regenerating lizard epidermis indicates a new process for the differentiation of the epidermis in lepidosaurians.
    Author: Alibardi L.
    Journal: J Morphol; 2012 Nov; 273(11):1272-9. PubMed ID: 22807268.
    Abstract:
    The process of keratinocyte differentiation was analyzed in the regenerating epidermis of the lizard Anolis carolinensis, where the genes coding for beta-proteins (beta-keratins) are known. The regenerating epidermis forms all epidermal layers found in normal scales (Oberhäutchen-, beta-, mesos-, and alpha-layer). Three specific proteins representing the larger families of beta-proteins, glycine-rich (HgG5, 28% glycine, 3.6% cysteine), glycine-cysteine medium-rich (HgGC10, 13% glycine, 14.5% cysteine), and glycine-cysteine rich (HgGC3, 30.4% glycine, 8.7% cysteine) have been immunolocalized at the ultrastructural level. HgG5 is only present in differentiating beta-cells, a weak or no labeling is observed in Oberhäutchen and is absent in alpha-cells. The protein is located in the pale corneous material forming the compact beta-layer but is absent in mature Oberhäutchen cells. HgGC10 is present among beta-packets in Oberhäutchen and beta-cells but disappears in more compact and electron-pale corneous material. The labeling disappears in mesos-cells and is present with variable intensity in alpha-cells, whereas lacunar and clear-cells are low labeled to unlabeled. HgGC3 is sparse or absent in beta-cells but is lightly present in the darker corneous material of differentiating and mature alpha-cells, lacunar-cells, and clear-cells. The study suggests that while glycine-rich proteins (electron-pale) are specifically used for building the resistant and hydrophobic beta-layer, cysteine-glycine rich proteins (electron-denser) are used to form the pliable corneous material present in the Oberhäutchen and alpha-cells. The differential accumulation of beta-proteins on the alpha-keratin cytoskeleton scaffold and not the alternance of beta- with alpha-keratins allow the differentiation of different epidermal layers.
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