Abstract:
: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.
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Shipilov VN,Shpakov AO,Rusakov YIdoi
10.1196/annals.1327.091subject
Has Abstractpub_date
2005-04-01 00:00:00pages
464-5eissn
0077-8923issn
1749-6632pii
1040/1/464journal_volume
1040pub_type
杂志文章abstract::Vaccinia virus encodes secretory proteins termed virokines. One of the major virokines encoded by the N1L open reading frame is the 13.8 kDa protein. A recombinant virus, termed vGK5, lacking this protein when injected intracranially into mice, has one of the highest levels of in vivo attenuation achieved by deletion ...
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journal_title:Annals of the New York Academy of Sciences
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journal_title:Annals of the New York Academy of Sciences
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