CAS Registry Number: 9015-71-8
CAS Name: Corticotropin-releasing factor
Additional Names: CRH; corticoliberin(e); corticotropin-releasing hormone
Literature References: Hypothalamic substance that stimulates secretion of ACTH, q.v. and b-endorphin from the pituitary. First direct evidence for its presence in hypothalami: R. Guillemin, B. Rosenberg, Endocrinology 57, 599 (1955); M. Saffran, A. V. Schally, Can. J. Biochem. Physiol. 33, 408 (1955). Purification and characterization of a 41-residue ovine hypothalamic CRF that is highly potent in stimulating secretion of corticotropin and b-endorphin-like immunoactivities: W. Vale et al., Science 213, 1394 (1981). Primary structure: J. Spiess et al., Proc. Natl. Acad. Sci. USA 78, 6517 (1981). When centrally administered, CRF activates the sympathetic nervous system and may therefore function as a key hormone in stress mobilization of the organism, cf. W. Vale et al., loc. cit.; M. Brown et al., Life Sci. 30, 207 (1982). CRF also stimulates a-MSH secretion and cyclic AMP accumulation in rat pars intermedia cells: H. Meunier et al., ibid. 31, 2129 (1982). A functional relationship between CRF and dynorphin-related opioid peptides has also been suggested: K. A. Roth et al., Science 219, 189 (1983). Reviews: A. V. Schally et al., Recent Prog. Horm. Res. 24, 497-588 (1968); R. Burgus, R. Guillemin, Annu. Rev. Biochem. 39, 499-526 (1970); M. Saffran in Hypothalamic Peptide Hormones and Pituitary Regulation, J. C. Porter, Ed. (Plenum Press, New York, 1977) pp 225-235; W.Vale et al. in The Role of Peptides in Neuronal Function, J. L. Barker, J. G. Smith, Eds. (Dekker, New York, 1980) pp 432-454; several authors in Polypeptide Hormones, R. F. Beers, E. G. Bassett, Eds. (Raven Press, New York, 1980) pp 165-271; B. Lutz-Bucher et al., J. Physiol. 77, 939-950 (1981); N. Yasuda et al., Endocr. Rev. 3, 123-140 (1982); E. Stark, G. B. Makara in Hormonally Active Brain Peptides: Structure and Function, K. W. McKerns, V. Pantic, Eds. (Plenum Press, New York, 1982) pp 157-179.
Properties: Activity is destroyed by trypsin; unaffected by thioglycolate, pepsin, chymotrypsin.