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Structure-Activity Relationships of Atrial Natriuretic Peptides

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Atrial Hormones and Other Natriuretic Factors

Part of the book series: Clinical Physiology Series ((CLINPHY))

Abstract

since the initial observation of de Bold and co-workers (1), the atrial natriuretic factor (ANF) has been developed into a new hormonal system that appears to play an important role in salt and water homeostasis and blood pressure. The primary structure of this factor is now well characterized. Its precursor is composed of 126 amino acids and contains a disulfide bridge between Cys105 and Cys121. The 28 amino acids at the COOH-terminal sequence represent the circulating form. In the rat, rabbit, and mouse, ANF peptides contain isoleucine in position 110, which is substituted by methionine in the human, dog, and bovine sequences.

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Authors and Affiliations

  1. Clinical Research Institute of Montreal, Montreal, Canada

    Gaétan Thibault, Raul Garcia, Ernesto L. Schiffrin, Andre De Léan, Peter W. Schiller, Jolanta Gutkowska, Jacques Genest & Marc Cantin

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  1. Gaétan Thibault
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  2. Raul Garcia
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  3. Ernesto L. Schiffrin
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  4. Andre De Léan
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  5. Peter W. Schiller
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  6. Jolanta Gutkowska
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  7. Jacques Genest
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  8. Marc Cantin
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Editor information

Editors and Affiliations

  1. Department of Medicine, Medical College of Ohio, Toledo, Ohio, USA

    Patrick J. Mulrow

  2. Department of Medicine Health Science Center, University of Colorado, Denver, Colorado, USA

    Robert Schrier

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© 1987 American Physiological Society

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Thibault, G. et al. (1987). Structure-Activity Relationships of Atrial Natriuretic Peptides. In: Mulrow, P.J., Schrier, R. (eds) Atrial Hormones and Other Natriuretic Factors. Clinical Physiology Series. Springer, New York, NY. https://doi.org/10.1007/978-1-4614-7529-3_7

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  • DOI: https://doi.org/10.1007/978-1-4614-7529-3_7

  • Publisher Name: Springer, New York, NY

  • Online ISBN: 978-1-4614-7529-3

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