Key result
In vitro translation identifies a 58-kDa protein as the unglycosylated primary ANP receptor product.
The identification of a 58-kDa unglycosylated precursor supports the model that the mature ANP receptor is composed of two 70-kDa subunits rather than a single 140-kDa precursor.
Supports two-subunit ANP receptor model in bovine tissue; leaves open extension to human physiology and therapy.
The primary translation product of mRNA encoding atrial natriuretic peptide (ANP) receptor has been shown to have an Mr of 58,000. Poly(A)+ RNA was isolated from the bovine kidney and lung and translated in a rabbit reticulocyte lysate system containing [35S]methionine. Immunoprecipitation of the labeled translation products, followed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography, identified a 58-kDa protein as the primary translation product which is the unglycosylated precursor to be processed to the glycosylated mature 70-kDa form found in the plasma membranes. The result lends strong support to our previous proposal that mature ANP receptor is composed of two disulfide-linked 70-kDa subunits, eliminating the possibility that the two 70-kDa subunits arise from a larger 140-kDa precursor by proteolytic cleavage.
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Uchida et al. (1987) studied this question. In vitro translation of ANP receptor mRNA was evaluated on Identification of the primary translation product of ANP receptor mRNA. In vitro translation of bovine kidney and lung mRNA identified a 58-kDa protein as the unglycosylated primary translation product of the atrial natriuretic peptide receptor.
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