Journal article

Structure-activity study of LVV-hemorphin-7: Angiotensin AT(4) receptor ligand and inhibitor of insulin-regulated aminopeptidase

J Lee, T Mustafa, SG McDowall, FAO Mendelsohn, M Brennan, RA Lew, AL Albiston, SY Chai

JOURNAL OF PHARMACOLOGY AND EXPERIMENTAL THERAPEUTICS | AMER SOC PHARMACOLOGY EXPERIMENTAL THERAPEUTICS | Published : 2003

Abstract

The decapeptide LVV-hemorphin-7 binds with high affinity to the angiotensin IV (Ang IV) receptor (AT(4) receptor), eliciting a number of physiological effects, including cellular proliferation and memory enhancement. We have recently shown that the AT(4) receptor is identical to insulin-regulated aminopeptidase (IRAP) and that both LVV-hemorphin-7 and Ang IV inhibit the catalytic activity of IRAP. In the current study, a series of alanine-substituted and N- or C-terminally modified analogs of LVV-hemorphin-7 were evaluated for their abilities to compete for (125)I-Ang IV binding in sheep adrenal and cerebellar membranes. Selected analogs were also analyzed for binding to recombinant human IR..

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