Characterization of the cysteine-rich calcium-binding S100A3 protein from human hair cuticles

Biochem Biophys Res Commun. 2002 Dec 20;299(5):857-62. doi: 10.1016/s0006-291x(02)02744-4.

Abstract

S100A3, a unique protein among all members of the calcium-binding S100 family, is specifically expressed at the inner endocuticle of human hair fibers. Upon hair damage, S100A3 is released from hair fibers and possibly destabilizes the hair tissue architecture. This study describes the purification and characterization of native S100A3 isolated from human hair fibers. We extracted native S100A3 from cuticles and purified the protein by anion-exchange chromatography. The results of 2D gel electrophoresis showed that cuticle S100A3 has a slightly lower isoelectric point compared to the recombinant protein. Tandem mass spectrometry of the peptides resulting from endoproteinase digest of cuticle S100A3 revealed that the N-terminal methionine is replaced with an acetyl group. This is the first report on biochemical characteristics of S100A3 in hair cuticle.

MeSH terms

  • Calcium-Binding Proteins / chemistry*
  • Calcium-Binding Proteins / isolation & purification
  • Chromatography, Ion Exchange
  • Cysteine / analysis
  • Electrophoresis, Gel, Two-Dimensional
  • Hair Follicle / chemistry*
  • Humans
  • Male
  • S100 Proteins*
  • Spectrometry, Mass, Electrospray Ionization

Substances

  • Calcium-Binding Proteins
  • S100 Proteins
  • S100A3 protein, human
  • Cysteine