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Science 6 December 1985: Vol. 230. no. 4730, pp. 1168 - 1171 DOI: 10.1126/science.2933808
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Articles
Science, Vol 230, Issue 4730, 1168-1171
Copyright © 1985 by American Association for the Advancement of Science
Biosynthesis and secretion of proatrial natriuretic factor by cultured rat cardiocytes
KD Bloch,
JA Scott,
JB Zisfein,
JT Fallon,
MN Margolies,
CE Seidman,
GR Matsueda,
CJ Homcy,
RM Graham,
and
JG Seidman
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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Circ. Res.
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- Corin, a transmembrane cardiac serine protease, acts as a pro-atrial natriuretic peptide-converting enzyme.
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PNAS
97, 8525-8529
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