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Review
. 2024 Jul 19;30(1):103.
doi: 10.1186/s10020-024-00874-z.

Myeloid-derived growth factor in diseases: structure, function and mechanisms

Affiliations
Review

Myeloid-derived growth factor in diseases: structure, function and mechanisms

Peng Chen et al. Mol Med. .

Abstract

Myeloid-derived growth factor (MYDGF) is a novel secreted protein with potent antiapoptotic and tissue-repairing properties that is present in nearly 140 human tissues and cell lines, with the highest abundance in the oral epithelium and skin. Initially, MYDGF was found in bone marrow-derived monocytes and macrophages for cardioprotection and repair after myocardial infarction. Subsequent studies have shown that MYDGF plays an important role in other cardiovascular diseases (e.g., atherosclerosis and heart failure), metabolic disorders, renal disease, autoimmune/inflammatory disorders, and cancers. Although the underlying mechanisms have not been fully explored, the role of MYDGF in health and disease may involve cell apoptosis and proliferation, tissue repair and regeneration, anti-inflammation, and glycolipid metabolism regulation. In this review, we summarize the current progress in understanding the role of MYDGF in health and disease, focusing on its structure, function and mechanisms. The graphical abstract shows the current role of MYDGF in different organs and diseases (Fig. 1).

Keywords: Autoimmune/inflammatory disorders; Cancers; Cardiovascular diseases; Metabolic disorders; Myeloid-derived growth factor; Renal disease.

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Conflict of interest statement

The authors have no relevant financial or non-financial interests to disclose.

Figures

Fig. 1
Fig. 1
Graphical abstract showing the role of MYDGF in different organs and diseases
Fig. 2
Fig. 2
MYDGF structure and topology diagram. a The structure is made up of ten β-strands (β1–β10) that comprise three antiparallel β-sheets (β1–10) and an α-helical turn (α1). b Topology diagram of β-strand connectivity. Each arrow represents a β-sheet (β1–10). β1 and β10 connect the N and C peptide termini, respectively. β1 and β2 form loop 1 (5 amino acids in length), β2 and β3 form loop 2 (5 amino acids in length), β3 and β4 form loop 3 (3 amino acids in length), β4 and β5 form loop 4 (5 amino acids in length), β5 and β6 form loop 5 (8 amino acids in length), β6 and β7 form loop 6 (6 amino acids in length), β7 and β8 form loop 7 (18 amino acids in length), β8 and β9 form loop 8 (3 amino acids in length), and β9 and β10 form loop 9 (10 amino acids in length)
Fig. 3
Fig. 3
Mechanisms and signaling pathways affected by MYDGF in disease

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