Sequence analysis and expression of human neuropsin cDNA and gene

Gene. 1998 Jun 15;213(1-2):9-16. doi: 10.1016/s0378-1119(98)00232-7.


Neuropsin is a serine protease which is thought to function in a variety of tissues including the brain and skin. This protease has been shown to have important roles in neural plasticity in mice. Here we have cloned a cDNA and analyzed the gene for human neuropsin by polymerase chain reaction-based strategies. The cDNA had 72% identity to mouse neuropsin. The deduced amino acid sequence showed 72% identity to mouse neuropsin. Key amino acid residues for the enzyme activity and all cysteine residues were conserved between human and mouse neuropsin. The gene for human neuropsin had six exons and five introns, and the gene organization is similar to trypsin-type serine proteases. The mRNA was expressed in primary cultures of keratinocytes.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • Enzyme Induction
  • Exons
  • Genes*
  • Hippocampus / enzymology
  • Humans
  • Introns
  • Kallikreins*
  • Mice
  • Molecular Sequence Data
  • Nerve Tissue Proteins / biosynthesis
  • Nerve Tissue Proteins / genetics*
  • Polymerase Chain Reaction
  • Sequence Alignment
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / biosynthesis
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics*
  • Species Specificity


  • DNA, Complementary
  • Nerve Tissue Proteins
  • KLK8 protein, human
  • Kallikreins
  • Serine Endopeptidases

Associated data

  • GENBANK/AB009849
  • GENBANK/AB012761