K. Sol-church et al., Characterization of mouse cathepsin R, a new member of a family of placentally expressed cysteine proteases, BBA-GENE ST, 1492(2-3), 2000, pp. 488-492
Citations number
24
Categorie Soggetti
Molecular Biology & Genetics
Journal title
BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
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 th
at cathepsin R is only expressed in placenta and thus is a new member of th
e emerging family of cathepsins whose expression is regulated during mouse
embryonic development. Modeling and structural analysis suggests that cathe
psin R will have a restricted substrate specificity when compared to that o
f cathepsin L. (C) 2000 Elsevier Science B.V. All rights reserved.