Immunolocalization and characterization of cornification proteins in snake epidermis
Article first published online: 5 JAN 2005
Copyright © 2005 Wiley-Liss, Inc.
The Anatomical Record Part A: Discoveries in Molecular, Cellular, and Evolutionary Biology
Volume 282A, Issue 2, pages 138–146, February 2005
How to Cite
Alibardi, L. and Toni, M. (2005), Immunolocalization and characterization of cornification proteins in snake epidermis. Anat. Rec., 282A: 138–146. doi: 10.1002/ar.a.20153
- Issue published online: 24 JAN 2005
- Article first published online: 5 JAN 2005
- Manuscript Accepted: 8 OCT 2004
- Manuscript Received: 13 JUL 2004
- University of Bologna Grant (Segnali Molecolari dello Sviluppo and 60% Grant)
- cornification proteins;
Little is known about specific proteins involved in keratinization of the epidermis of snakes, which is composed of alternating β- and α-keratin layers. Using immunological techniques (immunocytochemistry and immunoblotting), the present study reports the presence in snake epidermis of proteins with epitopes that cross-react with certain mammalian cornification proteins (loricrin, filaggrin, sciellin, transglutaminase) and chick β-keratin. α-keratins were found in all epidermal layers except in the hard β- and α-layers. β-keratins were exclusively present in the oberhautchen and β-layer. After extraction and electrophoresis, α-keratins of 40–67 kDa in molecular weights were found. Loricrin-like proteins recorded molecular weights of 33, 50, and 58 kDa; sciellin, 55 and 62 kDa; filaggrin-like, 52 and 65 kDa; and transglutaminase, 45, 50, and 56 kDa. These results suggest that α-layers of snake epidermis utilize proteins with common epitopes to those present during cornification of mammalian epidermis. The β-keratin antibody on extracts from whole snake epidermis showed a strong cross-reactive band at 13–16 kDa. No cross-reactivity was seen using an antibody against feather β-keratin, indicating absence of a common epitope between snake and feather keratins. © 2005 Wiley-Liss, Inc.