The mammalian atrium is an endocrine organ that may be involved in the control of blood pressure and extracellular fluid volume. A series of peptides, which seem to be associated with atrium-specific secretory granules, have potent natriuretic, diuretic and smooth muscle relaxant activities. Sequence determination of several of these peptides, which range from 21 to 126 amino acids long, shows that they form a family, derived from a common precursor. Rat and human complementary DNAs that encode the precursor to the various peptides, collectively called atrial natriuretic factors (ANFs), have been cloned. Nucleotide sequencing showed that the ANFs are located at the C-terminus of a polypeptide of relative molecular mass 13,000. We describe here the isolation and characterization of the corresponding human gene. Two introns interrupt the gene; one is located in the region coding for the N-terminus of the precursor and the other separates the codon for the C-terminal tyrosine from the rest of the peptide.

We have isolated and characterized the gene for human apolipoprotein CIII, a major component of the triglyceride-rich lipoproteins. Determination of the complete DNA sequence of this gene revealed that the coding sequence is interrupted by three introns, which occur in the 5' noncoding region, in the region encoding the signal sequence and in the region coding for the mature plasma protein, respectively. We present an analysis of the structure of the apo CIII gene and compare it to the gene for apolipoprotein AI. In addition, we present the DNA sequence of the intergenic region lying between the apo AI and the apo CIII genes.

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