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Official Full Name
Homo sapiens chromosome 19 open reading frame 10 DNA.
The protein encoded by this gene was previously thought to support proliferation of lymphoid cells and was considered an interleukin. However, this activity has not been reproducible and the function of this protein is currently unknown.
C19ORF10; chromosome 19 open reading frame 10; IL27, IL27w, interleukin 27 working designation; UPF0556 protein C19orf10; IL 25; IL 27; IL25; R33729_1; SF20; CS010_HUMAN; EUROIMAGE1875335; IL-25; IL27; IL27w; Interleukin 25; Interleukin 27 working designation; Interleukin-25; Interleukin25; R33729 1; R337291; Stromal cell derived growth factor; Stromal cell derived growth factor SF20; Stromal cell-derived growth factor SF20; Uncharacterized protein C19orf10 precursor; stromal cell-derived growth factor

Recent Research Progress

Human myeloid-derived growth factor (MYDGF, also known as C19orf10), is a paracrine-acting protein secreted by monocytes/macrophages that improves tissue repair and cardiac function after myocardial infarction. C19orf10 was selected from 42 proteins that had no obvious features and secreted too much in human embryonic kidney 293 (HEK293) cells.

Some studies have shown that C19orf10 is a resident endoplasmic reticulum protein. C19orf10 is co-located with P4HB in the nuclear envelope, including the endoplasmic reticulum (ER) of eosinophils, and Golgi’s P4HB and RCAS1. A ubiquitous c-terminal sequence BXEL (B: basic; X: variable residue; E: Glu. L: Leu) has the potential to preserve human C19orf10 and its homologues in the ER. In order to test the functionality of this sequence, Valeriu Bortnov, et al. expressed full-length human C19orf10 or MYDGF lacking the C-terminal GluLeu residues in monolayers of HEK293 cells. Full-length C19orf10 accumulates in cells, while truncated C19orf10 appears in the culture medium. These observations revealed the presence of C19orf10 in ER and Golgi and provided a new framework for studying and understanding this interesting protein.

C19orf10 is considered to be a paracrine-acting protein produced by bone-derived monocytes and macrophages. As part of the adaptive response, C19orf10 can enhance therapeutically to protect and repair the heart after myocardial infarction (MI). C19orf10 is expressed by CXCR4high BMCs in patients with acute myocardial infarction, and by inflammatory cells of CXCR4high in the heart of mice with infarction. The CXCR4low cells of mice and humans also expressed C19orf10, albeit at low levels. In the heart of infarcted mice, C19orf10 was mainly expressed by Ly6Chigh monocytes and Ly6Clow monocytes or macrophages, while other inflammatory cell types, endothelial cells and cardiomyocytes expressed much less C19orf10. Wound healing after MI involves the biphasic accumulation of Ly6Chigh monocytes and Ly6Clow monocytes or macrophages, with obvious overlapping functions. The bone marrow and spleen continue to supply Ly6Chigh monocytes through blood flow to meet the high demand for these cells in the inflammatory site. Recruited Ly6Chigh monocytes give rise to Ly6Clow macrophages that proliferate locally in the infarcted heart. The Ly6Chigh monocytes from bone marrow, spleen and peripheral blood also had strong C19orf10 expression after myocardial infarction and under sham surgical conditions. The study found that in bone marrow chimeric mice underscore the importance of inflammatory cell–derived C19orf10 for tissue repair after MI.

In addition, information on C19orf10 was found to increase in some human hepatocellular carcinoma, over-expression or addition of recombinant protein to medium resulted in phosphorylation of AKT and proliferation of a liver cancer cell line. Therefore, further research on C19orf10 is valuable.


  1. Korf-Klingebiel, M, et al. Myeloid-derived growth factor (C19orf10) mediates cardiac repair following myocardial infarction. Nature Medicine, 2015, 21(2): 52-61.
  2. Ravi C, et al. Development of an SRM method for absolute quantitation of MYDGF/C19orf10 protein. Proteomics Clinical Applications, 2016, 10:663–670.
  3. Bortnov Valeriu, et al. Myeloid-derived growth factor is a resident endoplasmic reticulum protein. The Journal of biological chemistry, 2018.

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