Abstract
Myeloid‐derived growth factor (MYDGF) is a novel protein secreted by bone marrow cells that features important physiological functions. In recent years, MYDGF has gained considerable interest due to their extensive beneficial effect on cardiac repair and protects cardiomyocytes from cell death. However, its precise molecular mechanisms have not been well elucidated. The purpose of this study was to produce sufficient amount of biologically active recombinant human (rh) MYDGF more economically and effectively by using in vitro molecular cloning techniques to study its clinical application. The prokaryotic expression system of Escherichia coli was established for the preparation of rhMYDGF. Finally, a large amount of high biologically active and purified form of recombinant protein was obtained. Moreover, we investigated the potential mechanism of rhMYDGF‐mediated proliferation and survival in human coronary artery endothelial cells (HCAECs). Mechanistically, the results suggested that MAPK/STAT3 and the cyclin D1 signalling pathways are indispensable for rhMYDGF‐mediated HCAEC proliferation and survival. Therefore, this study successfully established a preparation protocol for biologically active rhMYDGF and it may be a most economical way to produce high‐quality active rhMYDGF for future clinical application.
Highlights
According to the statistics of the World Health Organization, acute myocardial infarction (MI) has become one of the major diseases that threaten people's health, and several millions of patients lose their lives due to MI each year.[1]
Recent reports have revealed a protein encoded by open reading frame 10 on chromosome 19 (C19orf10) and named as myeloid-derived growth factor (MYDGF), which is mainly secreted by bone marrow– derived monocytes and murine fibroblasts during adipocyte differentiation.[12]
Recent studies demonstrated that MYDGF is secreted from murine fibroblasts during adipocyte differentiation.[12]
Summary
Develop more effective treatment options for myocardial tissue regeneration and effectively promote the healing of the patient after ischaemia-reperfusion. Recent reports have revealed a protein encoded by open reading frame 10 on chromosome 19 (C19orf10) and named as myeloid-derived growth factor (MYDGF), which is mainly secreted by bone marrow– derived monocytes and murine fibroblasts during adipocyte differentiation.[12]. This protein has been shown to be capable of promoting cardiac recovery after MI.[13-15]. The problem of high-efficiency production of bioactive recombinant human MYDGF is still unsolved, which may seriously limit the application of MYDGF in fundamental research and clinical treatment Taking into account this background, the present study aimed to develop an economical method to obtain large amounts of bioactive rhMYDGF. This study demonstrates a more economical method to produce high biologically active form of rhMYDGF, and that would be beneficial for the clinical transformation of MYDGF as a promising therapeutic molecule for the future treatment of patients with ischaemia-reperfusion injury
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