Ventura-Clapier R, Kaasik A, Veksler V
U-446 INSERM Université Paris-Sud, 5 rue Jean-Baptiste Clément, Châtenay-Malabry, France.
Mol Cell Biochem. 2004 Jan-Feb;256-257(1-2):29-41. doi: 10.1023/b:mcbi.0000009857.69730.97.
In adult mammalian muscle cells, energy consuming processes are mainly localized to the sarcolemma, sarcoplasmic reticulum (SR) and myofibrillar compartments, while energy production occurs within mitochondria or glycolytic complexes. Due to the restricted diffusion of adenine nucleotides near the active sites of ATPases involved in contractile activity and calcium homeostasis, there are multiple local systems that can locally rephosphorylate ADP and provide ATP. The creatine kinase (CK) system, with specific isoenzymes localized within each compartment, efficiently controls local adenylate pools and links energy production and utilization. However, mice lacking one or both of the MM-CK and mi-CK isoforms (CK-/-) are viable and develop almost normal cardiac and skeletal muscle function under the conditions of moderate workload, suggesting adaptations or other mechanisms that may ensure efficient energy transfer. While fixed CK is essentially important, other systems could also be involved as well, such as bound glycolytic enzymes or adenylate kinase. We have shown that, additionally, a direct functional interplay exists between mitochondria and sarcoplasmic reticulum, or between mitochondria and myofilaments in muscle cells, that catalyzes direct energy and signal transfer between organelles. In cardiac cells of CK-/- mice, marked cytoarchitectural modifications were observed, and direct adenine nucleotide channeling between mitochondria and organelles was very effective to rescue SR and myofilament functions. In fast skeletal muscles, increased oxidative capacity also indicates compensatory mechanisms. In mutant mice, mitochondrial capacity increases and a direct energy channeling occurs between mitochondria on one hand and ATP consuming sites on the other. However, these systems appear to be insufficient to fully compensate for the lack of CK at high workload. It can be concluded that local rephosphorylation of ADP is a crucial regulatory point in highly differentiated and organized muscle cells to ensure contractile diversity and efficiency and that the CK system is important to control energy fluxes and energy homeostasis.
在成年哺乳动物的肌肉细胞中,能量消耗过程主要定位于肌膜、肌浆网(SR)和肌原纤维区室,而能量产生则发生在线粒体或糖酵解复合体中。由于参与收缩活动和钙稳态的ATP酶活性位点附近腺嘌呤核苷酸的扩散受限,存在多个可在局部将ADP重新磷酸化并提供ATP的局部系统。肌酸激酶(CK)系统在每个区室中都有特定的同工酶,能有效控制局部腺苷酸库,并将能量产生与利用联系起来。然而,缺乏MM-CK和mi-CK同工型中的一种或两种(CK-/-)的小鼠是存活的,并且在中等工作负荷条件下心脏和骨骼肌功能几乎正常发育,这表明存在适应性变化或其他可能确保有效能量转移的机制。虽然固定的CK至关重要,但其他系统也可能参与其中,如结合的糖酵解酶或腺苷酸激酶。我们已经表明,此外,肌肉细胞中的线粒体与肌浆网之间,或线粒体与肌丝之间存在直接的功能相互作用,可催化细胞器之间的直接能量和信号传递。在CK-/-小鼠的心脏细胞中,观察到明显的细胞结构修饰,线粒体与细胞器之间的直接腺嘌呤核苷酸通道对挽救SR和肌丝功能非常有效。在快速收缩的骨骼肌中,氧化能力的增加也表明存在补偿机制。在突变小鼠中,线粒体能力增强,一方面线粒体与另一方面的ATP消耗位点之间发生直接的能量通道作用。然而,在高工作负荷下,这些系统似乎不足以完全补偿CK的缺乏。可以得出结论,ADP的局部重新磷酸化是高度分化和有组织的肌肉细胞中确保收缩多样性和效率的关键调节点,并且CK系统对于控制能量通量和能量稳态很重要。