Open AccessThe cellular retinoic acid binding protein I is dispensable.
Author(s) -
Philippe Gorry,
Thomas Lufkin,
A. Dierich,
Cécile RochetteEgly,
Didier Décimo,
Pascal Dollé,
Manuel Mark,
Béatrice Durand,
Pierre Chambon
Publication year - 1994
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.91.19.9032
Subject(s) - retinoic acid , mutant , microbiology and biotechnology , retinoic acid inducible orphan g protein coupled receptor , mutation , signal transduction , tretinoin , embryonic stem cell , retinoic acid receptor , retinoic acid receptor beta , biology , gene , chemistry , biochemistry
The cellular retinoic acid binding proteins I and II (CRABPI and CRABPII) bind retinoic acid with high affinity, exhibit distinct patterns of expression during embryonic development, and are thought to play important roles in the RA signaling pathway. We have generated a targeted mutation of the CRABPI gene using the "hit-and-run" strategy and shown that it prevents the production of a functional CRABPI protein. Homozygous mutant mice were normal, indicating that CRABPI does not play a crucial role in the RA signaling pathway.
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