Pleiotropic action of insulin-like peptides of mollusk, Anodonta cygnea.
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.
Shipilov
V N
VN
Sechenov Institute of Evolutionary Physiology and Biochemistry, St. Petersburg, Russia. valshipilov@yandex.ru
Shpakov
A O
AO
Rusakov
Yu I
YI
D000818:Animals; D049877:Anodonta / Q000737:chemistry / Q000378:metabolism*; D007328:Insulin / Q000235:genetics / Q000378:metabolism*; D036341:Intercellular Signaling Peptides and Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D017526:Receptor, IGF Type 1 / Q000737:chemistry / Q000378:metabolism*
D007328:Insulin; D036341:Intercellular Signaling Peptides and Proteins; D017526:Receptor, IGF Type 1