MG53’s non-physiologic interaction with insulin receptor: lack of effect on insulin-stimulated Akt phosphorylation in muscle, heart and liver tissues
Overall, our data suggest that rhMG53 can bind to the IR-ECD, however has a low likelihood of a physiologic role, as the K<sub>d</sub> for binding is ~10,000 higher than the physiologic level of MG53 present in the serum of rodents and humans (~10 pM). Our findings question the notion proposed by Xiao and colleagues - whether targeting circulating MG53 opens a new therapeutic avenue for type 2 diabetes mellitus and its complications.
Authors
- Miyuki Nishi (ORCID: https://orcid.org/0000-0001-6055-7845)
- Hiroshi Takeshima (ORCID: https://orcid.org/0000-0003-4525-3725)
- Takashi Murayama (ORCID: https://orcid.org/0000-0002-3845-2980)
- Chuanxi Cai (ORCID: https://orcid.org/0000-0003-0532-7435)
- Xinyu Zhou (ORCID: https://orcid.org/0000-0002-1606-5816)
- Zachary D. Dawson (ORCID: https://orcid.org/0000-0002-3804-1241)
- Xiaoliang Wang (ORCID: https://orcid.org/0000-0002-7870-2729)
- Jong-Soo Kim
- Tao Tan (ORCID: https://orcid.org/0000-0003-0231-9309)
- Ki Ho Park (ORCID: https://orcid.org/0000-0002-6193-9826)
- Kyung Eun Lee (ORCID: https://orcid.org/0000-0001-6689-2759)
Institutions
- Kyoto University (JP)
- Kyoto Pharmaceutical University (JP)
- Juntendo University (JP)
- University of Virginia (US)
Publication Details
- Journal
- Frontiers in Endocrinology
- Published
- 2024-09-17
- DOI
- https://doi.org/10.3389/fendo.2024.1425426
- Primary Topic
- Muscle Physiology and Disorders
- Type
- article
- Field-Weighted Citation Impact
- 0.00
Funders
- National Institutes of Health