Pleiotropic Action of Insulin-like Peptides of Mollusk, Anodonta cygnea

• Published in: Annals of the New York Academy of Sciences Vol. 1040; no. 1; pp. 464 - 465
• Main Authors: SHIPILOV, V.N, SHPAKOV, A O, RUSAKOV, YU I
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01-04-2005
• Subjects: Affinity; Animals; Anodonta - chemistry; Anodonta - metabolism; Anodonta cygnea; functions; IGF-I; Insulin; Insulin - genetics; Insulin - metabolism; Intercellular Signaling Peptides and Proteins - chemistry; Intercellular Signaling Peptides and Proteins - metabolism; IRP; Molecular structure; Mollusca; mollusk; Mollusks; Peptides; Protein Binding - physiology; Receptor, IGF Type 1 - chemistry; Receptor, IGF Type 1 - metabolism; Receptors; Slopes
• ISSN: 0077-8923; 1749-6632
• DOI: 10.1196/annals.1327.091

: Insulin‐related peptides (IRPs) from ganglions of mollusk, Anodonta cygnea, were purified and characterized (IRP1‐IRP13) using insulin and insulin‐like growth factor‐I (IGF‐I) radioreceptor test systems. The IRPs were able to bind to insulin and IGF‐I receptors. Dose‐dependent curve slopes indicated that most IRPs bind with higher affinity to IGF‐I receptors than to insulin receptors. The IRP regulatory action on the activity of the adenylyl cyclase signal system showed that these peptides stimulated adenylyl cyclase and GTP‐binding activity of G‐proteins to the same extent as insulin and IGF‐I. The data obtained suggest polyfunctional IRP action that apparently is determined by the molecular structure of individual isoforms.