Objective: To summarize the mechanism of long non-coding RNA (lncRNA) in signal pathways related to osteogenic differentiation.
Methods: Relevant domestic and foreign researches in recent years were consulted. The characteristics and biological functions of lncRNA were introduced, and the specific mechanism of lncRNA regulating related signal pathways in osteogenic differentiation was elaborated.
Results: The exertion and maintenance of normal function of bone requires the closed coordination of transcription networks and signal pathways. However, most of these signal pathways or networks are dysregulated under pathological conditions that affect bone homeostasis. lncRNA can regulate the differentiation of various bone cells by activating or inhibiting signal pathways to achieve the balance of bone homeostasis, thereby reversing the pathological state of bones and achieving the purpose of treating bone metabolic diseases.
Conclusion: At present, the research on the mechanism of lncRNA regulating various osteogenic differentiation pathways is still in the early stage. Its in-depth regulator mechanism, especially the cross-talk of complex signal pathways needs to be further studied. And how to apply these molecular targets to clinical treatment is also a big challenge.
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http://dx.doi.org/10.7507/1002-1892.202111098 | DOI Listing |
J Chromatogr B Analyt Technol Biomed Life Sci
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Laboratory of Molecular Translational Medicine, Center for Translational Medicine, Key Laboratory of Birth Defects and Related Diseases of Women and Children (Sichuan University), Ministry of Education, West China Second University Hospital, Sichuan University, Chengdu, Sichuan 610041, P.R. China.
Neurological disorders are the leading health threats worldwide, characterized by impairments in consciousness, cognition, movement, and sensation, and can even lead to death. UFMylation is a novel post-translational modification (PTM) that serves as an important regulatory factor, promoting the complexity of protein structures and enhancing the diversity and specificity of functions. In UFMylation, ubiquitin-fold modifier 1 (UFM1) is covalently transferred to the primary amine of a lysine residue on the target protein through the synergistic action of three enzymes: the activating enzyme E1 of UFM1, the coupling enzyme E2 of UFM1, and the ligase E3.
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