Distribution of specific keratin-associated beta-proteins (beta-keratins) in the epidermis of the lizard Anolis carolinensis helps to clarify the process of cornification in lepidosaurians.
The epidermis of different scales in the lizard Anolis carolinensis expresses specific keratin-associated beta-proteins (beta-keratins). In order to localize the sites of accumulation of different beta-proteins, we have utilized antibodies directed against representative members of the main families of beta-proteins, the glycine-rich (HgG5), glycine-cysteine rich (HgGC3), glycine-cysteine medium-rich (HgGC10), and cysteine-rich (HgC1) beta-proteins. Immunoblotting and immunocytochemical controls confirm the specificity of the antibodies made against these proteins. Light and ultrastructural immunocytochemistry shows that the glycine-rich protein HgG5 is present in beta-layers of different body scales but is scarce in the oberhautchen and claws, and is absent in alpha-layers and adhesive setae. The cysteine-glycine-rich protein HgGC3 is low to absent in the oberhautchen, beta-layer, and mesos-layer but increases in alpha-layers. This beta-protein is low in claws where it is likely associated with the hard alpha-keratins previously studied in this lizard. The glycine-cysteine medium-rich HgGC10 protein is low in the beta-layer, higher in alpha-layers, and in the oberhautchen. This protein forms a major component of setal proteins including those of the adhesive spatula that allow this lizard to stick on vertical surfaces. HgC1 is poorly localized in most epidermis analyzed including adhesive setae and claws and appears as a minor component of the alpha-layers. In conclusion, the present study suggests that beta- and alpha-layers of lizard epidermis represent regions with different accumulation of glycine-rich proteins (mainly for mechanical resistance and hydrophobicity in the beta-layer) or cysteine-glycine-rich proteins (for both resistance and elasticity in both alpha- and beta-layers).
Comparative Histolab and Department of Biology, University of Bologna, Bologna, Italy. lorenzo.alibardi@unibo.it
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D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D004817:Epidermis / Q000378:metabolism / Q000502:physiology* / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D006724:Hoof and Claw / Q000378:metabolism*; D007150:Immunohistochemistry; D008116:Lizards / Q000378:metabolism / Q000502:physiology*; D009024:Morphogenesis / Q000502:physiology*; D014048:Tolonium Chloride; D053800:beta-Keratins / Q000235:genetics / Q000378:metabolism*
D053800:beta-Keratins; D014048:Tolonium Chloride