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Pruss RM, Zamiri N. Regulated expression of atrial natriuretic peptide-like immunoreactivity in cultured bovine adrenomedullary chromaffin cells. Neurochem Int. 1987;11(3):299-304doi: 10.1016/0197-0186(87)90050-7.
Pruss, R. M., & Zamiri, N. (1987). Regulated expression of atrial natriuretic peptide-like immunoreactivity in cultured bovine adrenomedullary chromaffin cells. Neurochemistry international, 11(3), 299-304. https://doi.org/10.1016/0197-0186(87)90050-7
Pruss, R M, and Zamiri, N. "Regulated expression of atrial natriuretic peptide-like immunoreactivity in cultured bovine adrenomedullary chromaffin cells." Neurochemistry international vol. 11,3 (1987): 299-304. doi: https://doi.org/10.1016/0197-0186(87)90050-7
Pruss RM, Zamiri N. Regulated expression of atrial natriuretic peptide-like immunoreactivity in cultured bovine adrenomedullary chromaffin cells. Neurochem Int. 1987;11(3):299-304. doi: 10.1016/0197-0186(87)90050-7. PMID: 20501175.
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Neurochem Int. 1987;11(3):299-304. doi: 10.1016/0197-0186(87)90050-7.

Regulated expression of atrial natriuretic peptide-like immunoreactivity in cultured bovine adrenomedullary chromaffin cells.

Neurochemistry international

R M Pruss, N Zamiri

Affiliations

  1. Merrell Dow Research Institute, 2110 E. Galbraith Rd, Cincinnati, OH45215, U.S.A.

PMID: 20501175 DOI: 10.1016/0197-0186(87)90050-7

Abstract

We show that cultured bovine adrenal chromaffin cells can be stimulated to produce atrial natriuretic peptide-like immunoreactivity (ANP). ANP levels increased 5-fold in response to either forskolin or phorbol ester treatment, and 17-fold after depolarization by 40 mM potassium. These agents appear to act through distinct second messenger mediated pathways to cause increased accumulation of ANP. When forskolin and phorbol ester were added simultaneously, their effects were synergistic: ANP levels increased 30-fold, more than the product of the increases achieved by treatment with either drug alone. The ANP present in bovine chromaffin cell extracts appeared immunologically identical to human ANP(1-28). By gel filtration, the immunoreactive ANP extracted from chromaffin cells was in a high molecular weight form, although HPLC fractionation revealed that a portion of the total immunoreactivity could be eluted with the same retention time as synthetic ANP standards.

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