Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases

Biochim Biophys Acta. 2000 Jul 24;1492(2-3):488-92. doi: 10.1016/s0167-4781(00)00114-7.

Abstract

A new mouse cysteine protease, termed cathepsin R, has been identified. The complete nucleotide sequence of this gene was derived from a set of cDNAs generated from 15.5-day mouse placenta. Sequence analysis revealed an open reading frame encoding a 334 amino acid long polypeptide closely related to placentally expressed cathepsins P, Q, and M. RT-PCR analysis indicated that cathepsin R is only expressed in placenta and thus is a new member of the emerging family of cathepsins whose expression is regulated during mouse embryonic development. Modeling and structural analysis suggests that cathepsin R will have a restricted substrate specificity when compared to that of cathepsin L.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / genetics
  • DNA, Complementary / analysis
  • Mice
  • Models, Molecular
  • Molecular Sequence Data
  • Placenta / enzymology*
  • Polymerase Chain Reaction
  • Protein Conformation
  • Sequence Homology, Amino Acid
  • Serine Endopeptidases / chemistry
  • Serine Endopeptidases / genetics*
  • Substrate Specificity

Substances

  • DNA, Complementary
  • ribosomal neutral proteinase
  • Serine Endopeptidases
  • Cysteine Endopeptidases