后调节抑制了线粒体透性过渡的发生
Laurent Argaud1, Odile Gateau-Roesch, Olivier Raisky
1INSERM E 0226, Université Claude Bernard Lyon I, France.
Circulation
|January 12, 2005
概括
后调节,在再注射期间进行的一次简短干预,通过抑制线粒体透性过渡孔 (mPTP) 来显著减少心脏病发作的大小. 这种保护作用提供了强大的抗胰岛素益处.
科学领域:
- 心血管研究研究心血管研究
- 线粒体生物学 线粒体生物学
- 缺血性损伤 缺血性损伤
背景情况:
- 重灌期间的短暂缺血,称为后调节,可以限制心脏病发作的大小.
- 线粒体透性过渡孔 (mPTP) 的开放与致命的再输液损伤有关.
- 该研究调查了后调节是否影响mPTP开放.
研究的目的:
- 为了确定后调节是否调节线粒体透性过渡孔 (mPTP) 开放.
- 评估后调节对缺血-再输液损伤的保护作用.
主要方法:
- 开放胸部的子经历了30分钟的缺血和4小时的再输血.
- 后调节包括在初始回流后短暂的缺血和再输循环.
- 测量了线粒体Ca2+诱导的mPTP开口和心脏病发作的大小.
主要成果:
- 与对照组相比,后调节,预调和mPTP抑制剂NIM811显著降低了心脏病发作的大小 (29%,18%,20%与61%相比).
- 开启mPTP所需的Ca2+负载在后条件,预条件和NIM811治疗组 (41,47,67μmol/L CaCl2/mg) 与对照组 (16μmol/L CaCl2/mg) 相比显著更高.
结论:
- 后调节有效地抑制了线粒体透性过渡孔 (mPTP) 的开放.
- 这种抑制赋予了显著的抗缺血性保护,减少了心脏病发作的大小.
更多相关视频
08:43Simultaneous Measurement of Mitochondrial Calcium and Mitochondrial Membrane Potential in Live Cells by Fluorescent Microscopy
Published on: January 24, 2017
18.6K
07:35Assessment of Open Probability of the Mitochondrial Permeability Transition Pore in the Setting of Coenzyme Q Excess
Published on: June 1, 2022
1.9K
相关概念视频
Feedback Inhibition
44.2K
Biochemical reactions are occurring constantly in cells, converting starting substances to different products, usually with the help of enzymes that speed the reactions. Without enzymes, it would take far too long for most reactions to occur to be useful to the cell!
44.2K
The Electron Transport Chain
13.9K
The electron transport chain or oxidative phosphorylation is an exothermic process in which free energy released during electron transfer reactions is coupled to ATP synthesis. This process is a significant source of energy in aerobic cells, and therefore inhibitors of the electron transport chain can be detrimental to the cell's metabolic processes.
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
Inhibitors of the electron transport chain
Rotenone, a widely used pesticide, prevents electron transfer from Fe-S cluster to ubiquinone or Q...
13.9K
Mitochondrial Protein Sorting
4.4K
Mitochondria are double-membrane organelles of the eukaryotes involved in cellular metabolism, signaling, ATP synthesis, and programmed cell death. Each of these processes requires specific proteins and enzymes that must be correctly sorted to the right mitochondrial subcompartment for the proper functioning of the organelle.
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
Most of these mitochondrial proteins are encoded by the nucleus and imported to the mitochondria as unfolded or loosely folded precursors. Mitochondrial precursors...
4.4K
Mitochondrial Precursor Proteins
2.9K
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...
Most of the mitochondrial...
2.9K
Translocation of Proteins into the Mitochondria
8.9K
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,...
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,...
8.9K
Energy to Drive Translocation
2.0K
Mitochondrial protein import is powered by two distinct energy sources: ATP hydrolysis and electrochemical potential across the inner membrane. Newly synthesized precursors are bound by cytosolic chaperones of the Hsp70 family, which guide them to the import receptors on the mitochondrial surface. Utilizing the energy of ATP hydrolysis, Hsp70 chaperones transfer these precursors to the TOM receptors on the mitochondrial outer membrane.
Generally, polypeptides are unfolded by two distinct...
Generally, polypeptides are unfolded by two distinct...
2.0K
