Localization and characterization of the N-terminal fragment of atrial natriuretic factor (ANF) precursor in the frog heart

Peptides ◽  
1990 ◽  
Vol 11 (2) ◽  
pp. 199-204 ◽  
Author(s):  
J. Gilles ◽  
P. Netchitailo ◽  
F. Leboulenger ◽  
M. Cantin ◽  
G. Pelletier ◽  
...  
1986 ◽  
Vol 7 (1) ◽  
pp. 35-38 ◽  
Author(s):  
MASASHI SHINJO ◽  
YUKIO HIRATA ◽  
HIROMI HAGIWARA ◽  
FUMIAKI AKIYAMA ◽  
KAZUO MURAKAMI ◽  
...  

Biochemistry ◽  
1989 ◽  
Vol 28 (13) ◽  
pp. 5599-5605 ◽  
Author(s):  
Bin Liu ◽  
Sylvain Meloche ◽  
Normand McNicoll ◽  
Christine Lord ◽  
Andre De Lean

1993 ◽  
Vol 11 (5) ◽  
pp. 499-508 ◽  
Author(s):  
Hector De Le??n ◽  
Guillemette Gauquelin ◽  
Ga??tan Thibault ◽  
Raul Garcia

FEBS Letters ◽  
1985 ◽  
Vol 189 (1) ◽  
pp. 57-61 ◽  
Author(s):  
R.M. Arendt ◽  
E. Stangl ◽  
J. Zähringer ◽  
D.C. Liebisch ◽  
A. Herz

Physiology ◽  
1986 ◽  
Vol 1 (1) ◽  
pp. 3-5
Author(s):  
J Genest ◽  
C Marc

The discovery of the atrial natriuretic factor is a major breakthrough for our understanding of the regulation of body fluid volume. It plays a major role in vasorelaxation and in hypertensive and edematous states. The progress made in the last two years is a testimony to the powers of the new analytical techniques for isolation and characterization of peptides.


1988 ◽  
Vol 251 (1) ◽  
pp. 301-304 ◽  
Author(s):  
R B Marala ◽  
R K Sharma

Studies with isolated adrenal cells and mouse testicular cells have supported a mediatory role of cyclic GMP in ANF (atrial natriuretic factor)-dependent steroidogenic signal transduction. This concept has been strengthened by the purification and biochemical characterization of a 180 kDa protein, which appears to contain both ANF receptor and guanylate cyclase activities, from rat adrenocortical carcinoma cells. Utilizing the antibody to 180 kDa membrane guanylate cyclase as a probe, we now demonstrate the direct presence of ANF-dependent membrane guanylate cyclase in mouse and rat testes. The antibody blocks the ANF-dependent guanylate cyclase activity in isolated membranes, and Western-blot analysis of the partially purified enzyme reveals a single 180 kDa protein. The presence of this enzyme in mouse and rat testes, together with its previous demonstration in rat adrenocortical carcinoma, represent an important potential biochemical role for this enzyme in receptor-mediated steroidogenic signal transduction.


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