Atrial Natriuretic Factor: Sodium Transport in Human Erythrocytes

1984 ◽  
Vol 67 (4) ◽  
pp. 403-405 ◽  
Author(s):  
Nick C. Trippodo ◽  
Francis E. Cole ◽  
Allan A. MacPhee
Keyword(s):  
Molecular Weight ◽  
Sodium Transport ◽  
Atrial Natriuretic Factor ◽  
Gel Filtration ◽  
Human Erythrocytes ◽  
Low Molecular Weight ◽  
Sodium Efflux ◽  
Natriuretic Factor ◽  
Cotransport System ◽  
Atrial Natriuretic

1. The effect of partially purified rat atrial natriuretic factor on sodium efflux from sodium-loaded human erythrocytes was studied. 2. High molecular weight (10000–30000) and low molecular weight (3000–10000) fractions of atrial extract were prepared by gel filtration; they had natriuretic activity in rats. 3. Neither fraction affected sodium efflux in erythrocytes. 4. The results suggest that atrial natriuretic factor acts in the kidney by mechanisms other than through inhibition of the Na+-K+ exchange pump or the Na+-K+ cotransport system.

Post-translational processing of atrial natriuretic factor by adult rat atrial cardiocytes in culture

1993 ◽  
Vol 71 (7) ◽  
pp. 497-505 ◽  
Author(s):  
Gilles R. Dubé ◽  
Mercedes L. Kuroski - de Bold ◽  
Adolfo J. de Bold
Keyword(s):  
Molecular Weight ◽  
Atrial Natriuretic Factor ◽  
Average Rate ◽  
Primary Cultures ◽  
Low Molecular Weight ◽  
Nuclear Staining ◽  
Adult Rat ◽  
Natriuretic Factor ◽  
Atrial Cardiocytes ◽  
Atrial Natriuretic

Post-translational processing of the cardiac polypeptide hormone atrial natriuretic factor (ANF) was studied using primary cultures of cardiocytes derived from adult rat atria. Atrial cardiocytes attached to microcarrier beads were maintained for up to 15 days under continuous superfusion in minichromatographic columns. The cultures were characterized for their ability to store, process, and release ANF and by immunofluorescence microscopy for ANF, desmin, and myosin. Nuclear staining using the fluorescent DNA stain Hoechst 33258 was carried out to determine the total number of cells in culture. Column eluates were assayed for ANF by radioimmunoassay and analyzed by reverse phase high-performance liquid chromatography. For comparison purposes, superfusion experiments using freshly isolated cardiocytes supported in Bio-Gel P2 were carried out. Freshly isolated atrial cardiocytes stored high molecular weight ANF (5.2 ± 1.9 pmol/μg DNA) and released mostly (83.3 ± 6.7%) low molecular weight ANF, at an average rate of 97 ± 18 fmol∙min−1∙μg−1 DNA. The cell content and the rate of release of ANF after 15 days in culture were 1.3 ± 0.4 pmoi/μg DNA and 1.7 ± 0.4 fmol∙min−1∙μg−1 DNA, respectively, and 62.7 ± 6.3% of the released peptide was of a low molecular weight. There was no correlation between changes in cell population and the extent of processing. Cultures of noncardiocytes, superfused with exogenous proANF, did not significantly process proANF to a lower molecular weight peptide. The present investigation shows that adult rat atrial cardiocytes, maintained superfused in microcarrier culture and in a serum-supplemented medium for up to 15 days, retain phenotypic and biochemical characteristics normally associated with the dual contractile–endocrine nature of mammalian atrial cardiocytes in vivo. The results obtained in the present work strongly support the view that ANF post-translational processing is an intrinsic property of the atrial cardiocytes and is independent of any other cell type.Key words: atrial natriuretic factor, post-translation processing, cardyocytes, adult rats, cell cultures.

Lack of effect of synthetic atrial natriuretic factor on rubidium uptake by human erythrocytes

1985 ◽  
Vol 130 (3) ◽  
pp. 1066-1071 ◽  
Author(s):  
Natividad Hernando ◽  
Carlos Caramelo ◽  
Alberto Tejedor ◽  
Arturo Fernandez-Cruz ◽  
JoséM. López-Novoa
Keyword(s):  
Atrial Natriuretic Factor ◽  
Human Erythrocytes ◽  
Rubidium Uptake ◽  
Natriuretic Factor ◽  
Atrial Natriuretic

Atrial natriuretic factor inhibits sodium transport in medullary collecting duct

1986 ◽  
Vol 250 (6) ◽  
pp. F963-F966 ◽  
Author(s):  
H. Sonnenberg ◽  
U. Honrath ◽  
C. K. Chong ◽  
D. R. Wilson
Keyword(s):  
Sodium Transport ◽  
Intravenous Infusion ◽  
Atrial Natriuretic Factor ◽  
Collecting Duct ◽  
Inhibitory Effect ◽  
Sodium Permeability ◽  
Natriuretic Factor ◽  
Tubular Lumen ◽  
Medullary Collecting Duct ◽  
Atrial Natriuretic

Characteristics of sodium transport in the inner medullary collecting duct were determined in anesthetized rats before and during intravenous infusion of synthetic atrial natriuretic factor (atriopeptin II). Infusion of the factor was associated with increased sodium delivery and reduced fractional reabsorption in the duct. Increasing delivery to the same extent by KCl infusion had no effect on fractional reabsorption. The results demonstrate that atrial natriuretic factor has a specific inhibitory effect on net sodium transport in this part of the nephron. The mechanism of this inhibition may involve induction of sodium permeability and consequent backflux into the tubular lumen.

Big ANF: large-molecular-weight ANF in plasma. I. Gel filtration and affinity chromatography studies

1991 ◽  
Vol 261 (4) ◽  
pp. E516-E524
Author(s):  
N. Wilson ◽  
V. Yakoleff ◽  
R. Keeler
Keyword(s):  
Molecular Weight ◽  
Affinity Chromatography ◽  
Gel Electrophoresis ◽  
Atrial Natriuretic Factor ◽  
Molecular Form ◽  
Gel Filtration ◽  
Gel Chromatography ◽  
Natriuretic Factor ◽  
Large Molecular Weight ◽  
High Concentrations

A large molecular form of immunoreactive atrial natriuretic factor (irANF) was demonstrated in plasma of rabbit and rat on the basis of gel filtration experiments. This big ANF was not retained by octadecylsilane cartridges and cross-reacted with four anti-ANF antisera of different specificities. Gel filtration in acid, but not in 8 M urea, resulted in material with elution characteristics of irANF. Affinity chromatography and gel electrophoresis of big ANF suggested that the material was similar to albumin. However, high concentrations of big ANF were found in analbuminemic rats, with characteristics similar to those seen in rabbit and normal rats (affinity and gel chromatography and gel electrophoresis). We thus conclude that big ANF represents a bound form of ANF in circulation and that the carrier is similar to but not identical with albumin.

Atrial Natriuretic Factor Receptors

1987 ◽  
Vol 16 (1) ◽  
pp. 63-77 ◽  
Author(s):  
John W. Jacobs ◽  
George P. Vlasuk ◽  
Michael Rosenblatt
Keyword(s):  
Atrial Natriuretic Factor ◽  
Natriuretic Factor ◽  
Atrial Natriuretic
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