Movatterモバイル変換

[0]ホーム
URL:

Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
Thehttps:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

NIH NLM Logo
Log inShow account info
Access keysNCBI HomepageMyNCBI HomepageMain ContentMain Navigation
pubmed logo
Advanced Clipboard
User Guide

Full text links

Springer full text link Springer
Full text links

Actions

Share

.2015 Nov;252(6):1529-36.
doi: 10.1007/s00709-015-0782-9. Epub 2015 Mar 5.

Immunolocalization of sulfhydryl oxidase in reptilian epidermis indicates that the enzyme participates mainly to the hardening process of the beta-corneous layer

Affiliations

Immunolocalization of sulfhydryl oxidase in reptilian epidermis indicates that the enzyme participates mainly to the hardening process of the beta-corneous layer

Lorenzo Alibardi. Protoplasma.2015 Nov.

Abstract

Reptilian skin is tough and scaled representing an evolutionary adaptation to the terrestrial environment. The presence of sulfhydryl oxidase during the process of hardening of the corneous layer in reptilian epidermis has been analyzed by immunocytochemistry and immunoblotting. Sulfhydryl oxidase-like immunoreactivity of proteins in the 50-65 kDa range of molecular weight is mainly observed in the transitional and pre-corneous layers of crocodilians, chelonian, and in the forming beta-layer of lepidosaurians. The ultrastructural localization of the enzyme by immunogold in lizard epidermis during renewal and resting stages shows that the labeling is mainly distributed in the cytoplasm and along the accumulating beta-packets of differentiating beta-cells while it appears very low to undetectable in differentiating alpha-cells of the lacunar, clear, mesos, and alpha-layers. The labeling however becomes absent or undetectable also in the fully mature beta-layer. The study shows that an oxidative enzyme is likely responsible of the cross-linking of the numerous cysteines present in the main proteins accumulated in corneocytes of reptilian epidermis, known as corneous beta-proteins (beta-keratins). This process of disulphide bond formation is probably largely responsible for the formation of hard beta-corneous layers in reptilian scales, a difference with alpha-corneous layers where substrate proteins of transglutaminase appear predominant.

Keywords: Differentiation; Epidermis; Immunocytochemistry; Reptiles; Sulfhydryl oxidase.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

References

    1. J Exp Zool B Mol Dev Evol. 2004 Nov 15;302(6):526-49 - PubMed
    1. Mol Biol Evol. 2014 Dec;31(12):3194-205 - PubMed
    1. J Struct Biol. 2014 Dec;188(3):213-24 - PubMed
    1. Z Zellforsch Mikrosk Anat. 1970;110(2):153-65 - PubMed
    1. J Invest Dermatol. 2014 Nov;134(11):2685-2692 - PubMed

Publication types

MeSH terms

Substances

Related information

LinkOut - more resources

Full text links
Springer full text link Springer
Cite
Send To

NCBI Literature Resources

MeSHPMCBookshelfDisclaimer

The PubMed wordmark and PubMed logo are registered trademarks of the U.S. Department of Health and Human Services (HHS). Unauthorized use of these marks is strictly prohibited.

[8]ページ先頭
©2009-2025 Movatter.jp