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相关概念视频

Mitochondrial Precursor Proteins01:39

Mitochondrial Precursor Proteins

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Mitochondrial precursors are partially unfolded or loosely folded polypeptide chains. Newly synthesized precursors are inhibited from spontaneously folding into their native conformation by the cytosolic chaperones, heat shock proteins 70 (Hsp70), and mitochondrial import stimulation factors (MSFs). Precursors bound to MSFs are guided to the TOM70-TOM37 receptors, while precursors bound to Hsp70  chaperones are targetted to TOM20-TOM22 receptor complexes.
Most of the mitochondrial...
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Animal Mitochondrial Genetics02:59

Animal Mitochondrial Genetics

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Among all the organelles in an animal cell, only mitochondria have their own independent genomes. Animal mitochondrial DNA is a double-stranded, closed-circular molecule with around 20,000 base pairs. Mitochondrial DNA is unique in that one of its two strands, the heavy, or H, -strand is guanine rich, whereas the complementary strand is cytosine rich and called the light, or L, -strand. Compared to nuclear DNA, mitochondrial DNA has a very low percentage of non-coding regions and is marked by...
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Translocation of Proteins into the Mitochondria01:19

Translocation of Proteins into the Mitochondria

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Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
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Porin Insertion in the Outer Mitochondrial Membrane01:12

Porin Insertion in the Outer Mitochondrial Membrane

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Porins are beta-barrel proteins translocated to the mitochondrial outer membrane through the TOM complex into the intermembrane space. Porin precursors bind TIM chaperones within the intermembrane space and are guided to the Sorting and Assembly Machinery complex or SAM complex on the outer mitochondrial membrane.
Three models describe the assembly of porins by the SAM complex and their insertion into the outer membrane. Model 1 suggests that porins are assembled outside the SAM channel as the...
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The Inner Mitochondrial Membrane01:28

The Inner Mitochondrial Membrane

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The inner mitochondrial membrane is the primary site of ATP synthesis. The inner membrane domain that forms a smooth layer adjacent to the outer membrane is called the inner boundary membrane. This domain contains membrane transporters that drive metabolites in and out of the mitochondria.  In contrast, the inner membrane network that invaginates into the matrix space is called the cristae membrane. This domain accounts for principle mitochondrial function as it accommodates the protein...
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Mitochondrial Membranes01:45

Mitochondrial Membranes

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A single mitochondrion is a bean-shaped organelle enclosed by a double-membrane system. The outer membrane of mitochondria is smooth and contains many porins - the integral membrane transporters. Porins enable free diffusion of ions and small uncharged molecules through the outer mitochondrial membrane but limit the transport of molecules larger than 5000 Daltons. Further, the outer mitochondrial membrane forms a unique structure called membrane contact sites with other subcellular organelles,...
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相关实验视频

Updated: Jun 8, 2025

Author Spotlight: New Insights into PBMC Mitochondrial Responses Using Fluorespirometry
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Author Spotlight: New Insights into PBMC Mitochondrial Responses Using Fluorespirometry

Published on: May 24, 2024

952

阿迪波R1通过FUNDC1调节线粒体功能,促进致病的Th17分化.

Hui Wang1, Qian Zhang1, Yuankai Sun1

  • 1Department of Rheumatology, the First Affiliated Hospital of Nanjing Medical University, Nanjing, Jiangsu 210029, China.

Journal of biomedical research
|November 7, 2024
PubMed
概括

亚迪波涅丁受体1 (Adipor1) 缺乏症通过FUNDC1影响线粒体功能,从而损害致病的Th17细胞分化. 这一发现为自身免疫和炎症性疾病提供了新的治疗点.

关键词:
在 AdipoR1 的情况下.FUNDC1 是一个基金.线粒体功能 线粒体功能在pTh17中,pTh17是

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Measuring Mitochondrial Function of Naïve and Effector CD8 T Cells
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Measuring Mitochondrial Function of Naïve and Effector CD8 T Cells

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Author Spotlight: Semi-Automated Isolation of the Stromal Vascular Fraction from Murine White Adipose Tissue Using a Tissue Dissociator
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Author Spotlight: Semi-Automated Isolation of the Stromal Vascular Fraction from Murine White Adipose Tissue Using a Tissue Dissociator

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Author Spotlight: Semi-Automated Isolation of the Stromal Vascular Fraction from Murine White Adipose Tissue Using a Tissue Dissociator
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科学领域:

  • 免疫学 免疫学 免疫学
  • 细胞生物学 细胞生物学
  • 线粒体生物学 线粒体生物学

背景情况:

  • 致病性Th17 (pTh17) 细胞在自身免疫性疾病中至关重要.
  • 亚迪波涅丁受体1 (Adipor1) 缺乏抑制了Th17分化,并减少了关节炎.
  • 阿迪波1影响线粒体功能和pTh17分化.

研究的目的:

  • 研究Adipor1在pTh17细胞分化和线粒体功能中的作用.
  • 探索涉及FUNDC1.1的潜在分子机制.

主要方法:

  • 在体外分化Th17细胞.
  • 线粒体功能测试.线粒体功能测试.
  • RNA测序 (RNA-seq) 的分析.
  • 基因干扰研究.

主要成果:

  • 在体外,阿迪波1缺乏抑制了pTh17的分化.
  • 在pTh17细胞中的Adipor1删除减少了线粒体功能.
  • 缺少阿迪波1会增加CD4+T细胞中的FUNDC1表达.
  • FUNDC1干扰部分扭转了Adipor1缺乏的影响.

结论:

  • 阿迪波1通过FUNDC1调节线粒体功能,促进pTh17细胞分化.
  • 这项研究确定了AdipoR1在免疫调节中的新机制.
  • 阿迪波R1和FUNDC1是自身免疫和炎症性疾病的潜在治疗点.