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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

Online
ISSN
1437-4315
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Volume 392, Issue 3 (Mar 2011)

Issues

Expression and role of the cell surface protease seprase/fibroblast activation protein-α (FAP-α) in astroglial tumors

Rolf Mentlein / Kirsten Hattermann / Charles Hemion / Achim A. Jungbluth
  • Ludwig Institute for Cancer Research, New York Branch at Memorial Sloan-Kettering Cancer Center, New York, NY 10065, USA
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Janka Held-Feindt
  • Department of Neurosurgery, University of Schleswig-Holstein Medical Center, D-24105 Kiel, Germany
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2011-06-18 | DOI: https://doi.org/10.1515/bc.2010.119

Abstract

Seprase or fibroblast activation protein-α (FAP-α) is a cell-surface serine protease that was previously described nearly exclusively on reactive and tumor stromal fibroblasts and thought to be involved in tissue remodeling. We investigated the expression and significance of FAP-α in astrocytomas/glioblastomas. As shown by quantitative reverse transcription polymerase chain reaction (RT-PCR) and immunohisto-chemistry, FAP-α was elevated in whole glioblastoma tissues and in particular in most glioma cells in situ and in vitro. In glioma stem-like cells (gliospheres), FAP-α was detected at low levels; however, FAP-α was considerably induced upon differentiation with 10% fetal calf serum. To explore its functional role, FAP-α was silenced by siRNA transfection. In Boyden chamber assays, FAP-α silenced cells migrated similar as control cells through non-coated or Matrigel (basal lamina)-coated porous membranes, but significantly slower through membranes coated with gelatin or brevican, a major component of brain extracellular matrix. Furthermore, FAP-α-silenced glioma cells migrated through murine brain slices much slower under the conditions tested than differentially fluorescent-labeled control cells. Thus, FAP-α is highly expressed on the surface of glioma cells and contributes to diffuse glioma invasion through extracellular matrix components.

Keywords: astrocytoma; cell surface protease; extracellular matrix; glioblastoma; proteases; tumor invasion

About the article

Corresponding author


Received: 2010-05-03

Accepted: 2010-06-24

Published Online: 2011-06-18

Published in Print: 2011-03-01


Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/bc.2010.119.

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