Abstract:
:Scales of snakes contain hard proteins (beta-keratins), now referred to as keratin-associated beta-proteins. In the present study we report the isolation, sequencing, and expression of a new group of these proteins from snake epidermis, designated cysteine-glycine-proline-rich proteins. One deduced protein from expressed mRNAs contains 128 amino acids (12.5 kDa) with a theoretical pI at 7.95, containing 10.2% cysteine and 15.6% glycine. The sequences of two more snake cysteine-proline-rich proteins have been identified from genomic DNA. In situ hybridization shows that the messengers for these proteins are present in the suprabasal and early differentiating beta-cells of the renewing scale epidermis. The present study shows that snake scales, as previously seen in scales of lizards, contain cysteine-rich beta-proteins in addition to glycine-rich beta-proteins. These keratin-associated beta-proteins mix with intermediate filament keratins (alpha-keratins) to produce the resistant corneous layer of snake scales. The specific proportion of these two subfamilies of proteins in different scales can determine various degrees of hardness in scales.
journal_name
J Anatjournal_title
Journal of anatomyauthors
Dalla Valle L,Nardi A,Alibardi Ldoi
10.1111/j.1469-7580.2009.01192.xsubject
Has Abstractpub_date
2010-03-01 00:00:00pages
356-67issue
3eissn
0021-8782issn
1469-7580pii
JOA1192journal_volume
216pub_type
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journal_title:Journal of anatomy
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journal_title:Journal of anatomy
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journal_title:Journal of anatomy
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journal_title:Journal of anatomy
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