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Review
. 2021 Apr 22;13(8):12258-12272.
doi: 10.18632/aging.202881. Epub 2021 Apr 22.

Growth differentiation factor 11: a "rejuvenation factor" involved in regulation of age-related diseases?

Yuting Ma  1   2 , Yongping Liu  1   2 , Fang Han  3 , Hongyan Qiu  1   2 , Junfeng Shi  1   2 , Na Huang  1 , Ningning Hou  1 , Xiaodong Sun  1   2
Affiliations
Review

Growth differentiation factor 11: a "rejuvenation factor" involved in regulation of age-related diseases?

Yuting Ma et al. Aging (Albany NY). .

Abstract

Growth differentiation factor 11 (GDF11), a member of the transforming growth factor β superfamily of cytokines, is a critical rejuvenation factor in aging cells. GDF11 improves neurodegenerative and neurovascular disease outcomes, increases skeletal muscle volume, and enhances muscle strength. Its wide-ranging biological effects may include the reversal of senescence in clinical applications, as well as the ability to reverse age-related pathological changes and regulate organ regeneration after injury. Nevertheless, recent data have led to controversy regarding the functional roles of GDF11, because the underlying mechanisms were not clearly established in previous studies. In this review, we examine the literature regarding GDF11 in age-related diseases and discuss potential mechanisms underlying the effects of GDF11 in regulation of age-related diseases.

Keywords: GDF11; age-related diseases; aging; growth differentiation factor 11; regeneration; transforming growth factor.

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Conflict of interest statement

CONFLICTS OF INTEREST: The authors declare that they have no conflicts of interest.

Figures

Figure 1
Figure 1
Structure and Maturation process of GDF11. GDF11 is cleaved by PCSK5 to form an inactive latent complex, which contains an N-terminal inhibitory pro-domain and two disulfide-linked carboxyl-terminal active domains. Then, members of the BMP1/Tolloid family of metalloproteinases cleave the latent complex at a single specific site to form the mature GDF11 and pro-peptide.
Figure 2
Figure 2
Overall structure of homodimeric human GDF11.
Figure 3
Figure 3
The signal transduction of GDF11. The figure displays the canonical signal transduction mediated by R-SMAD (SMAD 2/3, SMAD 1,5,8), assisted by the Co-SMAD (SMAD4). The non-canonical pathway is driven mainly by TGF-β activated kinase 1 (TAK1) and Ras.
Figure 4
Figure 4
GDF11 protein expression data. The color-coding is based on tissues with common functional features. The mouse-over function shows protein score for analyzed cell types found in a selected tissue (http://www.proteinatlas.org/ENSG00000135414-GDF11/tissue).
See this image and copyright information in PMC

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