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J Biol Chem, Vol. 274, Issue 20, 13800-13809, May 14, 1999
From the Departamento de Bioquímica y Biología
Molecular, Facultad de Medicina, Universidad de Oviedo,
33006-Oviedo, Spain
A cDNA encoding a new cysteine proteinase
belonging to the papain family and called cathepsin F has been cloned
from a human prostate cDNA library. This cDNA encodes a
polypeptide of 484 amino acids, with the same domain organization as
other cysteine proteinases, including a hydrophobic signal sequence, a
prodomain, and a catalytic region. However, this propeptide domain is
unusually long and distinguishes cathepsin F from other proteinases of
the papain family. Cathepsin F also shows all structural motifs
characteristic of these proteinases, including the essential cysteine
residue of the active site. Consistent with these structural features, cathepsin F produced in Escherichia coli as a fusion
protein with glutathione S-transferase degrades the
synthetic peptide benzyloxycarbonyl-Phe-Arg-7-amido-4-methylcoumarin, a
substrate commonly used for functional characterization of cysteine proteinases. Furthermore, this proteolytic activity is blocked by
trans-epoxysuccinyl-L-leucylamido-(4-guanidino)butane,
an inhibitor of cysteine proteinases. The gene encoding cathepsin
F maps to chromosome 11q13, close to that encoding cathepsin W. Cathepsin F is widely expressed in human tissues, suggesting a role in
normal protein catabolism. Northern blot analysis also revealed a
significant level of expression in some cancer cell lines opening
the possibility that this enzyme could be involved in degradative
processes occurring during tumor progression.
Molecular Cloning and Structural and Functional
Characterization of Human Cathepsin F, a New Cysteine Proteinase of
the Papain Family with a Long Propeptide Domain
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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