Abstract
The human hair proteome was investigated using two-dimensional LC-MS/MS. Among the 343 identified proteins, 70 were detected in high relative abundance, including keratin intermediate filament proteins, largely extractable with denaturants. Over 300 proteins were found to constitute the insoluble complex formed by transglutaminase cross-linking. The intracellular distribution of identified proteins is wide from cytoplasm to nucleus, mitochondria, ribosome, and plasma membrane. These results help rationalize ultrastructural features visible in the mature hair. Keratins and several substrates for transglutaminase were found to be posttranslationally modified by methylation and dimethylation. Evidence for ubiquitination of hair proteins was also obtained.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 789-800 |
| Number of pages | 12 |
| Journal | Molecular and Cellular Proteomics |
| Volume | 5 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 2006 |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Proteome analysis of human hair shaft : From protein identification to posttranslational modification. / Lee, Young Jin; Rice, Robert H.; Lee, Young Moo.
In: Molecular and Cellular Proteomics, Vol. 5, No. 5, 05.2006, p. 789-800.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Proteome analysis of human hair shaft
T2 - From protein identification to posttranslational modification
AU - Lee, Young Jin
AU - Rice, Robert H.
AU - Lee, Young Moo
PY - 2006/5
Y1 - 2006/5
N2 - The human hair proteome was investigated using two-dimensional LC-MS/MS. Among the 343 identified proteins, 70 were detected in high relative abundance, including keratin intermediate filament proteins, largely extractable with denaturants. Over 300 proteins were found to constitute the insoluble complex formed by transglutaminase cross-linking. The intracellular distribution of identified proteins is wide from cytoplasm to nucleus, mitochondria, ribosome, and plasma membrane. These results help rationalize ultrastructural features visible in the mature hair. Keratins and several substrates for transglutaminase were found to be posttranslationally modified by methylation and dimethylation. Evidence for ubiquitination of hair proteins was also obtained.
AB - The human hair proteome was investigated using two-dimensional LC-MS/MS. Among the 343 identified proteins, 70 were detected in high relative abundance, including keratin intermediate filament proteins, largely extractable with denaturants. Over 300 proteins were found to constitute the insoluble complex formed by transglutaminase cross-linking. The intracellular distribution of identified proteins is wide from cytoplasm to nucleus, mitochondria, ribosome, and plasma membrane. These results help rationalize ultrastructural features visible in the mature hair. Keratins and several substrates for transglutaminase were found to be posttranslationally modified by methylation and dimethylation. Evidence for ubiquitination of hair proteins was also obtained.
UR - http://www.scopus.com/inward/record.url?scp=33646927209&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=33646927209&partnerID=8YFLogxK
U2 - 10.1074/mcp.M500278-MCP200
DO - 10.1074/mcp.M500278-MCP200
M3 - Article
C2 - 16446289
AN - SCOPUS:33646927209
VL - 5
SP - 789
EP - 800
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
SN - 1535-9476
IS - 5
ER -