This basic science study demonstrates that rat cardiocytes secrete proANF, which is then converted by a serum protease into a smaller active peptide.
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Cultured rat cardiocyte data on proANF secretion and cleavage warrant no clinical change; leaves open the responsible protease and human relevance.
Rat atrial natriuretic factor (ANF) is translated as a 152-amino acid precursor preproANF. PreproANF is converted to the 126-amino acid proANF, the storage form of ANF in the atria. ANF isolated from the blood is approximately 25 amino acids long. It is demonstrated here that rat cardiocytes in culture store and secrete proANF. Incubation of proANF with serum produced a smaller ANF peptide. PreproANF seems to be processed to proANF in the atria, and proANF appears to be released into the blood, where it is converted by a protease to a smaller peptide.
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Bloch et al. (1985) studied this question.
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