Title: Metastasis-associated C4.4A, a GPI-anchored protein cleaved by ADAM10 and ADAM17
Authors: Esselens, Carl ×
Malapeira, Jordi
Colome, Nuria
Moss, Marcia
Canals, Francesc
Arribas, Joaquin #
Issue Date: Aug-2008
Publisher: W. de Gruyter
Series Title: Biological Chemistry vol:389 issue:8 pages:1075-1084
Conference: 5th General Meeting of the International-Proteolysis-Society location:Patras, GREECE date:20-24 Oct 2007
Abstract: Metalloproteases play a complex role in tumor progression. While the activity of some ADAM, ADAMTS and matrix metalloproteases (MMPs) seems to be protumorigenic, the activity of others seems to prevent tumor progression. The identification of the array of substrates of a given metalloprotease (degradome) seems an adequate approach to predict the effect of the inhibition of a metalloprotease in tumors. Here, we present the proteomic identification of a novel substrate for ADAM10 and -17. We used SILAC (Stable Isotope Labeling by Amino acids in Cell culture), a proteomic technique based on the differential metabolic labeling of cells in different conditions. This was applied to MCF7 cells derived from an invasive mammary tumor, and the same cells expressing shRNAs that knock down ADAM10 or -17. Following this approach, we have identified C4.4A as a substrate to both metalloproteases. Since C4.4A is likely involved in tumor invasion, these results indicate that the cleavage of C4.4A by ADAM 10 and ADAM17 contributes to tumor progression.
ISSN: 1431-6730
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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