通过IL-22介导的microRNA-124-3p/GRB2轴调节了牛皮的角质细胞的高增殖和炎症反应
Jiaqi Li1,2, Wenjuan Chang2, Junqin Li2
1School of Public Health, Shanxi Medical University, Taiyuan, China.
Archives of dermatological research
|January 10, 2025
概括
介质素-22 (IL-22) 通过降低微RNA-124-3p (miR-124-3p) 的调节触发牛皮,这会增加皮肤细胞中的生长因子受体结合蛋白2 (GRB2). 这导致质细胞过度增殖和炎症.
科学领域:
- 皮肤病学 皮肤病学
- 分子生物学分子生物学
- 免疫学 免疫学 免疫学
背景情况:
- 牛皮是一种慢性炎症性皮肤疾病,其特征是角质细胞的过度增殖.
- 介质素-22 (IL-22) 涉及到牛皮病原,可能通过微RNA调节.
- 微RNA可以向多个基因,这表明miR-124可能会影响IL-22-诱导的角质细胞功能障碍中的其他途径.
研究的目的:
- 调查miR-124-3p及其潜在标增长因子受体结合蛋白2 (GRB2) 在牛皮中IL-22介导的角质细胞反应中的作用.
- 通过miR-124-3p在角质细胞中阐明GRB2的调节机制.
- 评估GRB2对角质细胞增殖和炎症的影响.
主要方法:
- 生物信息查发现GRB2是miR-124-3p的潜在目标.
- 在牛皮病变和对照皮肤中分析了GRB2和miR-124-3p的表达水平.
- 在体外实验中使用了IL-22-刺激的HaCaT细胞,这些细胞被miR-124-3p模仿剂或GRB2抑制剂感染.
- 评估了细胞增殖,炎症媒介表达和蛋白质水平 (Ki67,PCNA,K16).
主要成果:
- 在牛皮病变中,GRB2表达升高,而miR-124-3p降低.
- 在角质细胞中,miR-124-3p的过度表达降低了GRB2水平.
- 高GRB2表达促进了角质细胞的增殖和炎症标志物;低GRB2表达抑制了这些效应.
- 抑制GRB2证明了对角质细胞增殖和炎症的剂量依赖作用.
- 对GRB2和miR-124-3p的过度表达表明miR-124-3p可以逆转GRB2诱导的过度增殖和炎症.
结论:
- 通过IL-22,对miR-124-3p的降低调节通过增加角质细胞中的GRB2表达来促进牛皮.
- GRB2在促进角质细胞过度增殖和牛皮炎炎症反应方面发挥着重要作用.
- 准miR-124-3p/GRB2轴代表了牛皮的潜在治疗策略.
相关概念视频
T Cell Types and Functions
946
When T cells with CD4 markers are activated, they give rise to two types of effector cells: helper T cells and regulatory T cells. Meanwhile, T cells with CD8 markers differentiate into effector cytotoxic T cells. The differentiation of CD4 T cells into helper T cell subsets, such as Th1, Th2, and Th17 cells, is dependent on the antigen type, antigen-presenting cell, and regulatory cytokines.
Th1 cells stimulate dendritic cells to express necessary co-stimulatory molecules on their surfaces for...
Th1 cells stimulate dendritic cells to express necessary co-stimulatory molecules on their surfaces for...
946
PI3K/mTOR/AKT Signaling Pathway
3.4K
The mammalian target of rapamycin (mTOR) is a serine/threonine kinase that regulates growth, proliferation, and cell survival in response to hormones, growth factors, or nutrient availability. This kinase exists in two structurally and functionally distinct forms: mTOR complex 1 (mTORC1) and mTOR complex 2 (mTORC2). The first form (mTORC1) is composed of a rapamycin-sensitive Raptor and proline-rich Akt substrate, PRAS40. In contrast, mTORC2 consists of a...
3.4K
MicroRNAs
3.0K
MicroRNA (miRNA) are short, regulatory RNA transcribed from introns (non-coding regions of a gene) or intergenic regions (stretches of DNA present between genes). Several processing steps are required to form biologically active, mature miRNA. The initial transcript, called primary miRNA (pri-mRNA), base-pairs with itself, forming a stem-loop structure. Within the nucleus, an endonuclease enzyme, called Drosha, shortens the stem-loop structure into hairpin-shaped pre-miRNA. After the pre-miRNA...
3.0K
Abnormal Proliferation
4.4K
Under normal conditions, most adult cells remain in a non-proliferative state unless stimulated by internal or external factors to replace lost cells. Abnormal cell proliferation is a condition in which the cell's growth exceeds and is uncoordinated with normal cells. In such situations, cell division persists in the same excessive manner even after cessation of the stimuli, leading to persistent tumors. The tumor arises from the damaged cells that replicate to pass the damage to the...
4.4K
mTOR Signaling and Cancer Progression
3.7K
The mammalian target of rapamycin or mTOR protein was discovered in 1994 due to its direct interaction with rapamycin. The protein gets its name from a yeast homolog called TOR. The mTOR protein complex in mammalian cells plays a major role in balancing anabolic processes such as the synthesis of proteins, lipids, and nucleotides and catabolic processes, such as autophagy in response to environmental cues, such as availability of nutrients and growth factors.
The mTOR pathway or the...
The mTOR pathway or the...
3.7K
The JAK-STAT Signaling Pathway
8.7K
Several cytokine receptors have tightly bound Janus kinase or JAK proteins attached at their cytosolic tail. Small signaling molecules such as cytokines, growth hormones, or prolactins bind to the cytokine receptors and initiate their dimerization. The dimerization brings the cytosolic JAKs together that trans-phosphorylate and activates each other. The activated JAKs now phosphorylate cytosolic tails of the cytokine receptors, which serve as binding sites for adaptor proteins such as SH2...
8.7K


