Structure-activity study of LVV-hemorphin-7: angiotensin AT4 receptor ligand and inhibitor of insulin-regulated aminopeptidase

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 am...

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Veröffentlicht in:	The Journal of pharmacology and experimental therapeutics Jg. 305; H. 1; S. 205
Hauptverfasser:	Lee, Joohyung, Mustafa, Tomris, McDowall, Sharon G, Mendelsohn, Frederick A O, Brennan, Michelle, Lew, Rebecca A, Albiston, Anthony L, Chai, Siew Yeen
Format:	Journal Article
Sprache:	Englisch
Veröffentlicht:	United States 01.04.2003
Schlagworte:	Alanine - genetics Alanine - metabolism Amino Acid Motifs Amino Acid Substitution Aminopeptidases - metabolism Angiotensin Receptor Antagonists Cells, Cultured Drug Interactions Gene Deletion Hemoglobins - chemistry Hemoglobins - genetics Hemoglobins - pharmacology Humans Insulin - pharmacology Interleukin 1 Receptor Antagonist Protein Ligands Peptide Fragments - chemistry Peptide Fragments - genetics Peptide Fragments - pharmacology Peptides - pharmacology Receptors, Angiotensin Recombinant Proteins - metabolism Sialoglycoproteins - metabolism Structure-Activity Relationship
ISSN:	0022-3565
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