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Serum protease cleaves proANF into a 14-kilodalton peptide and ANF

Journal Article · · Am. J. Physiol.; (United States)
OSTI ID:6411170
Proatrial natriuretic factor (proANF), the 126-amino acid precursor of ANF, is the major storage form in mammalian atria. In contrast, two ANF peptides containing the 28- and 24-carboxyterminal residues of proANF have been isolated from rat plasma. Whether the cleavage of proANF in vivo to these ANF peptides occurs during or after its release into the circulation has not been determined. The latter possibility was suggested by a previous study where, by using a cultured rat cardiocyte preparation, the authors demonstrated that proANF is secreted intact into the culture medium. They now report that serum, but not plasma, contains a protease that specifically cleaves the 17-kdalton proANF to a 14-kdalton amino-terminal peptide and the carboxyterminal 3-kdalton circulating forms of ANF. The role of this proANF-cleaving enzyme in the generation of the biologically active ANF peptides remains to be defined. Its isolation and characterization should provide insights into its site of production and whether in vivo it is involved in the processing of circulating proANF. Radiolabeled proANF is used in these studies.
Research Organization:
Harvard Medical School, Boston, MA
OSTI ID:
6411170
Journal Information:
Am. J. Physiol.; (United States), Journal Name: Am. J. Physiol.; (United States) Vol. 252:1; ISSN AJPHA
Country of Publication:
United States
Language:
English