Amino acid sequence analysis of human S100A7 (psoriasin) by tandem mass spectrometry

Biochem Biophys Res Commun. 1995 Dec 5;217(1):257-63. doi: 10.1006/bbrc.1995.2772.

Abstract

The Ca(2+)-binding proteins regulate a number of cellular and extracellular activities and deregulations of S100 gene expression are associated with several human diseases. For example, S100A7 is upregulated in psoriatic skin, implicating a link with psoriasis, a chronic inflammatory dermatosis. We purified human S100A7 and determined its protein sequence by tandem mass spectrometry and Edman microsequence analysis. Interestingly, a sequence comparison of S100A7 with all known human S100 proteins showed that S100A7 is the most divergent of all S100 proteins.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Calcium-Binding Proteins / chemistry
  • Calcium-Binding Proteins / genetics*
  • Cytosol / chemistry
  • Humans
  • Mass Spectrometry
  • Membranes / chemistry
  • Molecular Sequence Data
  • Molecular Structure
  • Psoriasis / genetics
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • Sequence Homology, Amino Acid

Substances

  • Calcium-Binding Proteins
  • S100 Calcium Binding Protein A7
  • S100 Proteins
  • S100A7 protein, human

Associated data

  • GENBANK/P31151