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

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

doi:10.1074/mcp.M500278-MCP200

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

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

Environmental Toxicology

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82 Scopus citations

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	https://doi.org/10.1074/mcp.M500278-MCP200
State	Published - May 2006

ASJC Scopus subject areas

Biochemistry

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Lee, Y. J., Rice, R. H., & Lee, Y. M. (2006). Proteome analysis of human hair shaft: From protein identification to posttranslational modification. Molecular and Cellular Proteomics, 5(5), 789-800. https://doi.org/10.1074/mcp.M500278-MCP200

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