Non-glycosylated IGF2 prohormones are more mitogenic than native IGF2
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F23%3A00574400" target="_blank" >RIV/61388963:_____/23:00574400 - isvavai.cz</a>
Alternative codes found
RIV/67985823:_____/23:00574400 RIV/00216208:11310/23:10471746
Result on the web
<a href="https://doi.org/10.1038/s42003-023-05239-6" target="_blank" >https://doi.org/10.1038/s42003-023-05239-6</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s42003-023-05239-6" target="_blank" >10.1038/s42003-023-05239-6</a>
Alternative languages
Result language
angličtina
Original language name
Non-glycosylated IGF2 prohormones are more mitogenic than native IGF2
Original language description
Insulin-like Growth Factor-2 (IGF2) is important for the regulation of human embryonic growth and development, and for adults’ physiology. Incorrect processing of the IGF2 precursor, pro-IGF2(156), leads to the formation of two IGF2 proforms, big-IGF2(87) and big-IGF2(104). Unprocessed and mainly non-glycosylated IGF2 proforms are found at abnormally high levels in certain diseases, but their mode of action is still unclear. Here, we found that pro-IGF2(156) has the lowest ability to form its inactivating complexes with IGF-Binding Proteins and has higher proliferative properties in cells than IGF2 and other IGF prohormones. We also showed that big-IGF2(104) has a seven-fold higher binding affinity for the IGF2 receptor than IGF2, and that pro-IGF2(87) binds and activates specific receptors and stimulates cell growth similarly to the mature IGF2. The properties of these pro-IGF2 forms, especially of pro-IGF2(156) and big-IGF2(104), indicate them as hormones that may be associated with human diseases related to the accumulation of IGF-2 proforms in the circulation.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Communications Biology
ISSN
2399-3642
e-ISSN
2399-3642
Volume of the periodical
6
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
15
Pages from-to
863
UT code for WoS article
001050714300002
EID of the result in the Scopus database
2-s2.0-85168337649