Structure-activity relationships of atrial natriuretic factor (ANF). II. Effect of chain-length modifications on vascular reactivity.

Abstract:

:The effect of the length of ANF peptides on the inhibition of the norepinephrine-induced contraction was studied. Starting from the 26 residues ANF (Arg101-Tyr126), shorter N- and/or C-terminal fragments were produced, either by N-terminal chemical cleavage or C-terminal enzymatic digestion of ANF or both respectively. The N-terminal removal of Arg101 did not modify the inhibitory response. Further N-terminal truncation up to des-Arg101-Arg102-Ser103-Ser104 ANF still produced a marked inhibitory effect on norepinephrine. In contrast C-terminal cleavage had a much more pronounced effect. Since des-Tyr126 ANF, des-Arg125-Tyr126 ANF and des-Phe124-Arg125-Tyr126 ANF exhibit much lower activities than the parent ANF. Finally, when the 5 residues C-terminal to Cys121 are removed, the resulting molecule is almost inactive. These data indicate that the C-terminal segment of ANF may modulate the binding of ANF to its receptor(s). Relatively, the N-terminal region seems to be much less important.

authors

Garcia R,Thibault G,Seidah NG,Lazure C,Cantin M,Genest J,Chrétien M

doi

10.1016/0006-291x(85)90588-1

subject

Has Abstract

pub_date

1985-01-16 00:00:00

pages

178-84

issue

1

eissn

0006-291X

issn

1090-2104

pii

0006-291X(85)90588-1

journal_volume

126

pub_type

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