Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues

Elena G. Novikova, Sandra E. Reznik, Oleg Varlamov, Lloyd D. Fricker

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Carboxypeptidase Z (CPZ) is a newly reported member of the metallocarboxypeptidase gene family, but unlike other members of this family, CPZ contains an N-terminal domain that has amino acid sequence similarity to Wnt-binding proteins. In order to gain insights as to the potential function of CPZ, the intracellular localization of this protein was determined in cell culture and in human tissues. When expressed in the ART-20 mouse pituitary cell line, CPZ protein is routed to the regulated secretory pathway and secreted upon stimulation. A fraction of the secreted CPZ remains associated with the extracellular matrix. Endogenous CPZ in the PC12 rat pheochromocytoma cell line is also associated with the extracellular matrix. In human placenta, CPZ is present within invasive trophoblasts and in the surrounding extracellular space, indicating an association with extracellular matrix. CPZ is also present in amnion cells, but is not readily apparent in the extracellular matrix of this cell type. A human adenocarcinoma of the colon shows expression of CPZ in the extracellular matrix adjacent to malignant cells. Taken together, CPZ appears to be a component of the extracellular matrix in some cell types, where it may function in the binding of Wnt.

Original languageEnglish (US)
Pages (from-to)4865-4870
Number of pages6
JournalJournal of Biological Chemistry
Volume275
Issue number7
DOIs
StatePublished - Feb 18 2000

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Carboxypeptidase Z is present in the regulated secretory pathway and extracellular matrix in cultured cells and in human tissues'. Together they form a unique fingerprint.

  • Cite this