Molecular and Cellular Biology, February 2000, p. 1089-1094, Vol. 20, No. 3
Department of Oncology
Research1 and Department of Nonclinical
Drug Safety,3 Boehringer Ingelheim Pharma KG,
88397 Biberach, Germany, and Department of Molecular Biology,
Boehringer Ingelheim Austria, A-1121 Vienna,
Austria2
Received 25 October 1999/Accepted 27 October 1999
Human fibroblast activation protein (FAP), a member of the serine
prolyl oligopeptidase family, is a type II cell surface glycoprotein
selectively expressed by fibroblastic cells in areas of active tissue
remodeling, such as the embryonic mesenchyme, areas of wound healing,
the gravid uterus, and the reactive stroma of epithelial cancers.
Homologues of FAP have been identified in the mouse and Xenopus
laevis. FAP is a dual-specificity enzyme that acts as a
dipeptidyl peptidase and collagenase in vitro. To explore the role of
FAP in vivo, Fap
0270-7306/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Targeted Disruption of Mouse Fibroblast
Activation Protein

/
mice were generated by
homologous recombination. RNase protection analysis and reverse
transcription-PCR confirmed the absence of full-length Fap
transcripts in mouse embryonic tissues. No FAP protein was detected in
Fap
/
animals by immunohistochemistry, and
no FAP-specific dipeptidyl peptidase activity was found. We report that
Fap
/
mice are fertile, show no overt
developmental defects, and have no general change in cancer susceptibility.
*
Corresponding author. Mailing address: Department of
Oncology Research, Boehringer Ingelheim Pharma KG, 88397 Biberach an der Riss, Germany. Phone: 49 7351 54 5240. Fax: 49 7351 54 5148. E-mail: andreas.schnapp{at}bc.boehringer-ingelheim.com.
Present address: Research Institute for Molecular Pathology, A-1030
Vienna, Austria.
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