Lizard epidermis is made of beta- and alpha-layers. Using western-blot tested antibodies the ultrastructural immunolocalization of specific keratin-associated beta-proteins in the epidermis of different lizard species reveals that glycine-rich beta-proteins (HgG5) localize in the beta-layer while glycine-cysteine-medium-rich beta-proteins (HgGC10) are present in oberhautchen and alpha-layers. This suggests a new explanation for the formation of different epidermal layers during the shedding cycle in lepidosaurian epidermis instead of an alternance between beta-keratins and alpha-keratins. It is proposed that different sets of genes coding for specific beta-proteins are activated in keratinocytes during the renewal phase of the shedding cycle. Initially glycine-cysteine-medium rich beta-proteins with hydrophilic and elastic properties accumulate over alpha-keratins in the oberhautchen but are replaced in the next cell layer with glycine-rich hydrophobic beta-proteins forming a resistant, stiff and hydrophobic beta-layer. The synthesis of glycine-rich proteins terminates in mesos and alpha-cells where these proteins are replaced with glycine-cysteine-rich beta-proteins. The pattern of beta-protein deposition onto a scaffold of intermediate filament keratins is typical for keratin associated proteins and the association between alpha-keratins and specific keratin associated beta-proteins during the renewal phase of the shedding cycle gives rise to epidermal layers possessing different structural, mechanical and texture properties.

Alibardi L (2014). Comparative immunolocalization of Keratin-associated beta-proteins (Beta-keratins) supports a new explanation for the cyclical process of keratinocyte differentiation in lizard epidermis. ACTA ZOOLOGICA, 95(1), 32-43 [10.1111/azo.12003].

Comparative immunolocalization of Keratin-associated beta-proteins (Beta-keratins) supports a new explanation for the cyclical process of keratinocyte differentiation in lizard epidermis

ALIBARDI, LORENZO
2014

Abstract

Lizard epidermis is made of beta- and alpha-layers. Using western-blot tested antibodies the ultrastructural immunolocalization of specific keratin-associated beta-proteins in the epidermis of different lizard species reveals that glycine-rich beta-proteins (HgG5) localize in the beta-layer while glycine-cysteine-medium-rich beta-proteins (HgGC10) are present in oberhautchen and alpha-layers. This suggests a new explanation for the formation of different epidermal layers during the shedding cycle in lepidosaurian epidermis instead of an alternance between beta-keratins and alpha-keratins. It is proposed that different sets of genes coding for specific beta-proteins are activated in keratinocytes during the renewal phase of the shedding cycle. Initially glycine-cysteine-medium rich beta-proteins with hydrophilic and elastic properties accumulate over alpha-keratins in the oberhautchen but are replaced in the next cell layer with glycine-rich hydrophobic beta-proteins forming a resistant, stiff and hydrophobic beta-layer. The synthesis of glycine-rich proteins terminates in mesos and alpha-cells where these proteins are replaced with glycine-cysteine-rich beta-proteins. The pattern of beta-protein deposition onto a scaffold of intermediate filament keratins is typical for keratin associated proteins and the association between alpha-keratins and specific keratin associated beta-proteins during the renewal phase of the shedding cycle gives rise to epidermal layers possessing different structural, mechanical and texture properties.
2014
Alibardi L (2014). Comparative immunolocalization of Keratin-associated beta-proteins (Beta-keratins) supports a new explanation for the cyclical process of keratinocyte differentiation in lizard epidermis. ACTA ZOOLOGICA, 95(1), 32-43 [10.1111/azo.12003].
Alibardi L
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/214675
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