Gene structure of human cardiac hormone precursor, pronatriodilatin View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1984-12

AUTHORS

Mona Nemer, Michel Chamberland, Diane Sirois, Stephania Argentin, Jacques Drouin, Richard A. F. Dixon, Robert A. Zivin, Jon H. Condra

ABSTRACT

Atrial cardiocytes contain granules typical of protein-secreting cells1, and atrial extracts are known to contain a powerful natriuretic and diuretic activity2 and to possess smooth muscle relaxant activity3. A variety of active atrial peptides have been isolated, including a family of related peptides showing natriuretic, diuretic and smooth muscle relaxant activities in rat4–9 and human atria10; these peptides were named atrial natriuretic factor (ANF). Another unrelated peptide from pig atria11, cardiodilatin, is thought to possess only smooth muscle relaxant activity. Its partial amino acid sequence shows no homology with ANF sequences. The sequence analysis of a large form (106 amino acids) of ANF12 and of ANF complementary DNA clones13–16 indicates that cardiodilatin and ANF peptides are synthesized from a common precursor. This precursor also contains a signal peptide sequence expected of a secretory protein17. We now describe the complete structure and sequence of the human gene for this novel hormone precursor that we call pronatriodilatin12. More... »

PAGES

654-656

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/312654a0

DOI

http://dx.doi.org/10.1038/312654a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1047242844

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/6095118


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