Proteome analysis of human hair shaft: From protein identification to posttranslational modification

Young Jin Lee, Robert H. Rice, Young Moo Lee

Research output: Contribution to journalArticle

77 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)789-800
Number of pages12
JournalMolecular and Cellular Proteomics
Volume5
Issue number5
DOIs
StatePublished - May 2006

Fingerprint

Proteome
Post Translational Protein Processing
Hair
Transglutaminases
Keratins
Proteins
Intermediate Filament Proteins
Mitochondria
Methylation
Ubiquitination
Cell membranes
Ribosomes
Cytoplasm
Cell Membrane
Substrates

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 journalArticle

Lee, Young Jin ; Rice, Robert H. ; Lee, Young Moo. / Proteome analysis of human hair shaft : From protein identification to posttranslational modification. In: Molecular and Cellular Proteomics. 2006 ; Vol. 5, No. 5. pp. 789-800.
@article{e44332da60c947dda70fea8a5cc215ab,
title = "Proteome analysis of human hair shaft: From protein identification to posttranslational modification",
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.",
author = "Lee, {Young Jin} and Rice, {Robert H.} and Lee, {Young Moo}",
year = "2006",
month = "5",
doi = "10.1074/mcp.M500278-MCP200",
language = "English (US)",
volume = "5",
pages = "789--800",
journal = "Molecular and Cellular Proteomics",
issn = "1535-9476",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "5",

}

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 -