This preclinical study demonstrates that a small molecular weight form of BNP is cosecreted with ANP from porcine atrial cardiocytes, providing early basic science insights into natriuretic peptide physiology.
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Neonatal porcine secretion data should not guide human natriuretic peptide interpretation; leaves open cosecretion mechanisms across species and disease states.
Using primary cultures of atrial cardiocytes from neonatal pig, the secretion brain natriuretic peptide (BNP) and atrial natriuretic peptide (ANP)-like immunoreactivities (LI) was studied in vitro. Porcine cardiocytes time-dependently secreted both BNP-LI and ANP-LI into medium under a serum-free condition, although the amount of BNP-LI secreted was about one-third that of ANP-LI. Phorbol ester and Ca2+ ionophore had less stimulatory effects on secretion of BNP-LI than that of ANP-LI. Reverse-phase HPLC of the conditioned medium revealed a single major BNP-LI component corresponding to synthetic porcine BNP(1-26). These data suggest that a small molecular weight form BNP, possibly BNP(1-26), is cosecreted with ANP from porcine cardiocytes.
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Iida et al. (1990) studied this question.
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