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

Citation
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
ISSN journal
01674781 → ACNP
Volume
1492
Issue
2-3
Year of publication
2000
Pages
488 - 492
Database
ISI
SICI code
0167-4781(20000724)1492:2-3<488:COMCRA>2.0.ZU;2-E
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 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.