电聚-l-乳酸膜通过调节PCK2/AMPK/mTOR信号通路来促进M2巨的极化
Daiyuan Tang1, Bing Han2, Chengkai He3
1Department of Orthopedics, Kunming Medical University Affiliated Qujing Hospital, Qujing, 655000, China.
Advanced healthcare materials
|April 23, 2024
概括
具有特定表面形态的电聚-l-乳酸膜促进M2巨细胞的两极化. 这通过PCK2/AMPK/mTOR信号通路发生,为组织工程支架提供了洞察力.
科学领域:
- 生物材料科学 生物材料科学
- 免疫学 免疫学 免疫学
- 组织工程是组织工程.
背景情况:
- 电膜在组织工程中至关重要,但它们在调节巨细胞激活和免疫反应方面的精确作用需要进一步研究.
- 了解表面形态如何影响巨细胞极化是设计再生医学有效生物材料的关键.
研究的目的:
- 为了研究电聚-l-乳酸 (PLLA) 膜的不同表面形态对M2巨细胞极化的影响.
- 阐明潜在的分子机制,包括信号通路,这些机制调解了对巨细胞的观察效应.
主要方法:
- 制造具有不同对齐 (对齐和随机) 和直径 (纳米和微尺度) 的PLLA膜.
- 在这些膜上培养巨细胞并评估M2极化.
- 利用转录组,蛋白质组和蛋白质组测序来分析调节机制.
主要成果:
- 所有电的PLLA膜都表现出良好的生物相容性和调节的巨细胞表型和功能.
- 在特定的PLLA膜形态上培养的巨细胞 (A600组) 呈现出明显更高的M2极化.
- 该研究确定了增强的AMP激活蛋白激酶 (AMPK) /哺乳动物目标的拉巴胺素 (mTOR) 信号激活,由上调的PCK2表达介导,对于M2极化至关重要.
结论:
- 电的PLLA膜可以通过表面形态修饰有效地促进M2巨的极化.
- 在这个过程中,PCK2/AMPK/mTOR信号通路是关键的调节器.
- 这些发现为设计具有针对组织工程和临床应用的定制免疫调节性质的先进电支架提供了理论基础.
更多相关视频
相关概念视频
mTOR Signaling and Cancer Progression
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...
Amplifying Signals via Second Messengers
Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
PI3K/mTOR/AKT Signaling Pathway
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 rapamycin-insensitive companion...
cAMP-dependent Protein Kinase Pathways
Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
IP3/DAG Signaling Pathway
Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...


