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J Biol Chem, Vol. 275, Issue 11, 7935-7941, March 17, 2000
From the GCDFP-15 (gross cystic
disease fluid protein,
15 kDa) is a secretory marker of apocrine differentiation
in breast carcinoma. In human breast cancer cell lines, gene expression
is regulated by hormones, including androgens and prolactin. The
protein is also known under different names in different body fluids
such as gp17 in seminal plasma. GCDFP-15/gp17 is a ligand of CD4 and is
a potent inhibitor of T-cell apoptosis induced by sequential CD4/T-cell
receptor triggering. We now report that GCDFP-15/gp17 is a protease
exhibiting structural properties relating it to the aspartyl proteinase
superfamily. Unexpectedly, GCDFP-15/gp17 appears to be related to the
retroviral members rather than to the known cellular members of this
class. Site-specific mutagenesis of Asp22 (predicted
to be catalytically important for the active site) and pepstatin A
inhibition confirmed that the protein is an aspartic-type protease. We
also show that, among the substrates tested, GCDFP-15/gp17 is specific
for fibronectin. The study of GCDFP-15/gp17-mediated proteolysis may
provide a handle to understand phenomena as diverse as mammary tumor
progression and fertilization.
A Novel Aspartyl Proteinase from Apocrine Epithelia and
Breast Tumors*
§,, and
International Institute of Genetics and
Biophysics and the ¶ Institute of Protein Biochemistry and
Enzymology, Consiglio Nazionale delle Ricerche, via G. Marconi 10, I-80125 Naples, Italy
*
This work was supported by grants from the Associazione
Italiana Ricerca sul Cancro and Consiglio Nazionale delle
Ricerche-Progetto Finalizzato Biotechnology and by Ministero
Università Ricerca Scientifica e Tecnologica Biotechnology
Program L.95/95.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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