title: Expression of the fibroblast activation protein during mouse embryo development.
abstract: Human Fibroblast Activation Protein (FAP), a member of the serine prolyl oligopeptidase family, is a type II cell surface glycoprotein that acts as a dual-specificity dipeptidyl-peptidase (DPP) and collagenase in vitro. Its restricted expression pattern in embryonic mesenchyme, in wound healing and in reactive stromal fibroblasts of epithelial cancers, has suggested a role for the FAP protease in extracellular matrix degradation or growth factor activation in sites of tissue remodeling. The FAP homologue in Xenopus laevis has been reported to be induced in the thyroid hormone-induced tail resorption program during tadpole metamorphosis supporting a role for FAP in tissue remodeling processes during embryonic development. However, Fap-deficient mice show no overt developmental defects and are viable. To study the expression of FAP during mouse embryogenesis, a second Fap-deficient mouse strain expressing beta-Galactosidase under the control of the Fap promoter was generated by homologous recombination (Fap-/- lacZ mice). FAP deficiency was confirmed by the absence of FAP-specific dipeptidyl-peptidase activity in detergent-soluble extracts isolated from 17.5 d.p.c. Fap-/- lacZ embryos. We report that Fap-/- lacZ mice express beta-Galactosidase at regions of active tissue remodeling during embryogenesis including somites and perichondrial mesenchyme from cartilage primordia.
authors.affiliation: Oncology Research Group, Boehringer Ingelheim Pharma KG, Biberach, Germany.
authors.forename: J
authors.initials: J
authors.lastname: Niedermeyer
authors.forename: P
authors.initials: P
authors.lastname: Garin-Chesa
authors.forename: M
authors.initials: M
authors.lastname: Kriz
authors.forename: F
authors.initials: F
authors.lastname: Hilberg
authors.forename: E
authors.initials: E
authors.lastname: Mueller
authors.forename: U
authors.initials: U
authors.lastname: Bamberger
authors.forename: W J
authors.initials: WJ
authors.lastname: Rettig
authors.forename: A
authors.initials: A
authors.lastname: Schnapp
mesh_terms: D000818:Animals; D000951:Antigens, Neoplasm; D014408:Biomarkers, Tumor; D002356:Cartilage / Q000196:embryology / Q000378:metabolism / Q000502:physiology; D010450:Endopeptidases; D005109:Extracellular Matrix / Q000378:metabolism / Q000502:physiology*; D018093:Gelatinases; D018507:Gene Expression Regulation, Developmental; D017930:Genes, Reporter; D005838:Genotype; D006133:Growth Substances / Q000235:genetics / Q000378:metabolism*; D008565:Membrane Proteins; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D016133:Polymerase Chain Reaction; D011401:Promoter Regions, Genetic; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D019170:Somites / Q000378:metabolism / Q000502:physiology; D001616:beta-Galactosidase / Q000235:genetics / Q000378:metabolism; D000099167:Fibroblast Activation Protein Alpha
chemical_list: D000951:Antigens, Neoplasm; D014408:Biomarkers, Tumor; D010450:Endopeptidases; D018093:Gelatinases; D006133:Growth Substances; D008565:Membrane Proteins; D011993:Recombinant Fusion Proteins; D012697:Serine Endopeptidases; D001616:beta-Galactosidase; D000099167:Fibroblast Activation Protein Alpha