Chicken corneocyte cross-linked proteome

Robert H. Rice, Brett R. Winters, Blythe P. Durbin-Johnson, David M Rocke

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Shotgun proteomic analysis was performed of epidermal scale, feather, beak and claw from the domestic chicken. To this end, the samples were separated first into solubilized and particulate fractions, the latter enriched in isopeptide cross-linking, by exhaustive extraction in sodium dodecyl sulfate under reducing conditions. Among the 205 proteins identified were 17 keratins (types α and β), 51 involved in protein synthesis, 8 junctional, 8 histone, 5 heat shock, and 5 14-3-3 proteins. Considerable overlap among the beak, claw, feather, and scale samples was observed in protein profiles, but those from beak and claw were the most similar. Scale and feather profiles were the most distinctive, each exhibiting specific proteins. Less than 20% of the proteins were found only in the detergent-solubilized fraction, while 34-57% were found only in the particulate fraction, depending on the source, and the rest in both fractions. The results provide the first comprehensive analysis of the content of these cornified structures, reveal the efficient use of available proteins in conferring mechanical and chemical stability to them, and emphasize the importance of isopeptide cross-linking in avian epithelial cornification.

Original languageEnglish (US)
Pages (from-to)771-776
Number of pages6
JournalJournal of Proteome Research
Volume12
Issue number2
DOIs
StatePublished - Feb 1 2013

Fingerprint

Proteome
Chickens
Beak
Hoof and Claw
Feathers
Proteins
Keratin-17
14-3-3 Proteins
Mechanical stability
Chemical stability
Firearms
Sodium Dodecyl Sulfate
Detergents
Proteomics
Histones
Shock
Hot Temperature

Keywords

  • beak
  • claw
  • detergent extraction
  • epidermal scale
  • feather
  • isopeptide bonding
  • keratin
  • transglutaminase

ASJC Scopus subject areas

  • Biochemistry
  • Chemistry(all)

Cite this

Rice, R. H., Winters, B. R., Durbin-Johnson, B. P., & Rocke, D. M. (2013). Chicken corneocyte cross-linked proteome. Journal of Proteome Research, 12(2), 771-776. https://doi.org/10.1021/pr301036k

Chicken corneocyte cross-linked proteome. / Rice, Robert H.; Winters, Brett R.; Durbin-Johnson, Blythe P.; Rocke, David M.

In: Journal of Proteome Research, Vol. 12, No. 2, 01.02.2013, p. 771-776.

Research output: Contribution to journalArticle

Rice, RH, Winters, BR, Durbin-Johnson, BP & Rocke, DM 2013, 'Chicken corneocyte cross-linked proteome', Journal of Proteome Research, vol. 12, no. 2, pp. 771-776. https://doi.org/10.1021/pr301036k
Rice, Robert H. ; Winters, Brett R. ; Durbin-Johnson, Blythe P. ; Rocke, David M. / Chicken corneocyte cross-linked proteome. In: Journal of Proteome Research. 2013 ; Vol. 12, No. 2. pp. 771-776.
@article{03d3d1893f7040f7b968e8be6dd4a31d,
title = "Chicken corneocyte cross-linked proteome",
abstract = "Shotgun proteomic analysis was performed of epidermal scale, feather, beak and claw from the domestic chicken. To this end, the samples were separated first into solubilized and particulate fractions, the latter enriched in isopeptide cross-linking, by exhaustive extraction in sodium dodecyl sulfate under reducing conditions. Among the 205 proteins identified were 17 keratins (types α and β), 51 involved in protein synthesis, 8 junctional, 8 histone, 5 heat shock, and 5 14-3-3 proteins. Considerable overlap among the beak, claw, feather, and scale samples was observed in protein profiles, but those from beak and claw were the most similar. Scale and feather profiles were the most distinctive, each exhibiting specific proteins. Less than 20{\%} of the proteins were found only in the detergent-solubilized fraction, while 34-57{\%} were found only in the particulate fraction, depending on the source, and the rest in both fractions. The results provide the first comprehensive analysis of the content of these cornified structures, reveal the efficient use of available proteins in conferring mechanical and chemical stability to them, and emphasize the importance of isopeptide cross-linking in avian epithelial cornification.",
keywords = "beak, claw, detergent extraction, epidermal scale, feather, isopeptide bonding, keratin, transglutaminase",
author = "Rice, {Robert H.} and Winters, {Brett R.} and Durbin-Johnson, {Blythe P.} and Rocke, {David M}",
year = "2013",
month = "2",
day = "1",
doi = "10.1021/pr301036k",
language = "English (US)",
volume = "12",
pages = "771--776",
journal = "Journal of Proteome Research",
issn = "1535-3893",
publisher = "American Chemical Society",
number = "2",

}

TY - JOUR

T1 - Chicken corneocyte cross-linked proteome

AU - Rice, Robert H.

AU - Winters, Brett R.

AU - Durbin-Johnson, Blythe P.

AU - Rocke, David M

PY - 2013/2/1

Y1 - 2013/2/1

N2 - Shotgun proteomic analysis was performed of epidermal scale, feather, beak and claw from the domestic chicken. To this end, the samples were separated first into solubilized and particulate fractions, the latter enriched in isopeptide cross-linking, by exhaustive extraction in sodium dodecyl sulfate under reducing conditions. Among the 205 proteins identified were 17 keratins (types α and β), 51 involved in protein synthesis, 8 junctional, 8 histone, 5 heat shock, and 5 14-3-3 proteins. Considerable overlap among the beak, claw, feather, and scale samples was observed in protein profiles, but those from beak and claw were the most similar. Scale and feather profiles were the most distinctive, each exhibiting specific proteins. Less than 20% of the proteins were found only in the detergent-solubilized fraction, while 34-57% were found only in the particulate fraction, depending on the source, and the rest in both fractions. The results provide the first comprehensive analysis of the content of these cornified structures, reveal the efficient use of available proteins in conferring mechanical and chemical stability to them, and emphasize the importance of isopeptide cross-linking in avian epithelial cornification.

AB - Shotgun proteomic analysis was performed of epidermal scale, feather, beak and claw from the domestic chicken. To this end, the samples were separated first into solubilized and particulate fractions, the latter enriched in isopeptide cross-linking, by exhaustive extraction in sodium dodecyl sulfate under reducing conditions. Among the 205 proteins identified were 17 keratins (types α and β), 51 involved in protein synthesis, 8 junctional, 8 histone, 5 heat shock, and 5 14-3-3 proteins. Considerable overlap among the beak, claw, feather, and scale samples was observed in protein profiles, but those from beak and claw were the most similar. Scale and feather profiles were the most distinctive, each exhibiting specific proteins. Less than 20% of the proteins were found only in the detergent-solubilized fraction, while 34-57% were found only in the particulate fraction, depending on the source, and the rest in both fractions. The results provide the first comprehensive analysis of the content of these cornified structures, reveal the efficient use of available proteins in conferring mechanical and chemical stability to them, and emphasize the importance of isopeptide cross-linking in avian epithelial cornification.

KW - beak

KW - claw

KW - detergent extraction

KW - epidermal scale

KW - feather

KW - isopeptide bonding

KW - keratin

KW - transglutaminase

UR - http://www.scopus.com/inward/record.url?scp=84873326908&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84873326908&partnerID=8YFLogxK

U2 - 10.1021/pr301036k

DO - 10.1021/pr301036k

M3 - Article

C2 - 23256538

AN - SCOPUS:84873326908

VL - 12

SP - 771

EP - 776

JO - Journal of Proteome Research

JF - Journal of Proteome Research

SN - 1535-3893

IS - 2

ER -