Journal
ACTA ZOOLOGICA
Volume 95, Issue 4, Pages 465-471Publisher
WILEY
DOI: 10.1111/azo.12042
Keywords
lizard; dewlap; skin; ultrastructure; beta-protein immunocytochemistry
Categories
Funding
- Italian Ministry of Education and Scientific Research [2008 AXS E-002]
Ask authors/readers for more resources
The dewlap in the lizard Anolis carolinensis is made of scales separated by large interscale regions capable of broad stretching during fan extension. This indicates that the skin contains proteins that allow extension of interscale regions. The immunocytochemical analysis of the epidermis indicates that HgG5, a glycine-rich hydrophobic beta-protein poor in cysteine is localized only in the stiff beta-layer of the outer scale surface, but is completely absent in mesos and alpha-layers and in hinge regions. HgGC10, a cysteine-medium-rich beta-protein is present in beta-layers but especially in alpha-layers of interscale epidermis that presents folds and lacks a beta-layer. HgGC3 is weakly localized in the alpha-layer, but is mainly found in hinge regions. HgGC8 and HgG13 are low to absent in the alpha-and beta-layer. The immunolocalization of cysteine-rich beta-proteins such as HgGC10/3 in alpha-layers and interscale epidermis suggests that these small proteins are involved in the formation of a corneous material compatible with dewlap extension. The basement membrane underneath scales is joined to bundles of collagen fibrils in the dermis through anchoring fibrils that likely determine flattening of the epidermis during the extension of the throat fan.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available