Key result
The discovery and structural elucidation of atrial natriuretic factor as a 28-residue peptide hormone substantiated the endocrine function of the heart atria.
The structural elucidation of atrial natriuretic factor provided foundational evidence that the heart functions as an endocrine organ.
May guide volume regulation research; leaves open clinical translation in heart failure.
The benchmark experiments of Adolfo de Bold and Harald Sonnenberg revealed that heart atria contained a substance or substances (atrial natriuretic factor) which when injected into rats caused a profound diuresis, natriuresis, and fall in blood pressure. Acid extraction and purification of atrial natriuretic factor resulted initially in the purification of a low molecular weight peptide containing a disulfide bond. This peptide was named cardionatrin I. Amino acid sequencing of less than 1 nmol of cardionatrin I revealed it to be a 28-residue peptide with the following structure: (sequence; see text) The position of the disulfide bond was verified by a radioactive method. From the sequence of complementary DNA for atrial natriuretic factor, the 28-residue peptide was shown to be the C-terminal portion of a larger protein called pro-atrial natriuretic factor. The discovery and characterization of atrial natriuretic factor substantiated the idea that the heart atria serve in an endocrine capacity.
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T. Geoffrey Flynn (1987) reported a review. Atrial natriuretic factor was evaluated. The discovery and structural elucidation of atrial natriuretic factor as a 28-residue peptide hormone substantiated the endocrine function of the heart atria.
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