Corticotropin-releasing factor (CRF) is a 41 residue polypeptide hormone that is recognized as an early chemical signal in the response to stress. The hormone exhibits its actions through plasma membrane receptors which have been characterized from several sources. The molecular interaction between these receptors and CRF is under investigation by several laboratories. It is expected that further molecular information on the receptor will enhance the CRF biology and thereby stress research.
One year ago, scientists of the Department of Molecular Neuroendocrinology of the Max Planck Institute for Experimental Medicine in Goettingen/ Germany published the first report on the predicted amino acid sequences of two frog (Xenopus laevis) CRF receptors (Frank M. Dautzenberg, Konstanze Dietrich, Monika R. Palchaudhuri and Joachim Spiess. Identification of Two Corticotropin-Releasing Factor Receptors from Xenopus Laevis with High Ligand Selectivity: Unusual Pharmacology of the Type 1 Receptor. Journal of Neurochemistry pp.1640-1649, 1997). Principal investigator of the project was Dr. Frank Dautzenberg. The group found that frog - like all other species investigated - synthesizes two receptor types (types 1 and 2). Frog CRF receptor 1 (CRF-R1) exhibits a surprisingly high ligand selectivity. Human/rat CRF or urocortin are bound with significantly higher affinity than ovine CRF or sauvagine, a frog-specific CRF analog. These results contrast with the observation confirmed by many groups that mammalian CRF-R1 does not discriminate between the naturally occurring CRF analogs mentioned above.
On the basis of this difference, it was possible to identify the ligand-specific domain of frog
Contact: Frank Dautzenberg