Atrial natriuretic peptide (ANP) is a high-affinity substrate for rat insulin-degrading enzyme.
A cytosolic protein specifically binding to and degrading atrial natriuretic peptide (ANP) was purified from rat brain homogenate. Based on partial amino acid sequences and enzymatic properties, this protein with an apparent molecular mass of 112 kDa has been identified as the rat insulin-degrading enzyme (IDE). In addition to the known substrates, insulin and transforming-growth-factor alpha IDE binds also with high affinity (apparent Kd 60 nM) to ANP. Competition studies with structural variants of ANP demonstrate that both the C terminus and the disulfide loop of the molecule are essential for high-affinity binding. The data suggest that IDE might be involved in the cellular processing and/or metabolic clearance of ANP.
Müller
D
D
Institut für Zellbiochemie und klinische Neurobiologie, UKE, Universität Hamburg, Federal Republic of Germany.
Baumeister
H
H
Buck
F
F
Richter
D
D
D000345:Affinity Labels; D000595:Amino Acid Sequence; D000818:Animals; D009320:Atrial Natriuretic Factor / Q000378:metabolism*; D001667:Binding, Competitive; D001921:Brain / Q000378:metabolism; D002855:Chromatography, Thin Layer; D003432:Cross-Linking Reagents; D004591:Electrophoresis, Polyacrylamide Gel; D007328:Insulin / Q000378:metabolism; D007339:Insulysin / Q000302:isolation & purification / Q000378:metabolism*; D008969:Molecular Sequence Data; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity; D016211:Transforming Growth Factor alpha / Q000378:metabolism
D000345:Affinity Labels; D003432:Cross-Linking Reagents; D007328:Insulin; D016211:Transforming Growth Factor alpha; D009320:Atrial Natriuretic Factor; D007339:Insulysin