Posts Tagged ‘Mitochondrial’

Iranocichla persa, a new cichlid species from southern Iran (Teleostei, Cichlidae)

ZooKeys 636: 141-161
DOI: 10.3897/zookeys.636.10571
Authors: Hamid Reza Esmaeili, Golnaz Sayyadzadeh, Ole Seehausen
Abstract: Iranocichla persa sp. n. is described from the Shur, Hasanlangi and Minab River drainages flowing into th…

Cell biology: Double agents for mitochondrial division

Mitochondrial organelles — the energy powerhouses of the cell — must divide and fuse dynamically to function. It emerges that two distinct dynamin enzymes enable mitochondrial division.

The next frontier in reproductive tourism? Genetic modification

Rosa Castro, Duke University The birth of the first baby born using a technique called mitochondrial replacement, which uses DNA from three people to “correct” an inherited genetic mutation, was announced on Sept. 27. Mitochondrial replacement or d…

Thermal sensitivity and phenotypic plasticity of cardiac mitochondrial metabolism in European perch, Perca fluviatilis [RESEARCH ARTICLE]

Andreas Ekström, Erik Sandblom, Pierre U. Blier, Bernard-Antonin Dupont Cyr, Jeroen Brijs, and Nicolas PichaudCellular and mitochondrial metabolic capacity of the heart has been suggested to limit performance of fish at warm temperatures. We i…

Control of mitochondrial function and cell growth by the atypical cadherin Fat1

Mitochondrial products such as ATP, reactive oxygen species, and aspartate are key regulators of cellular metabolism and growth. Abnormal mitochondrial function compromises integrated growth-related processes such as development and tissue repair, as well as homeostatic mechanisms that counteract ageing and neurodegeneration, cardiovascular disease, and cancer. Physiologic mechanisms that control mitochondrial activity in such settings remain incompletely understood. Here we show that the atypical Fat1 cadherin acts as a molecular ‘brake’ on mitochondrial respiration that regulates vascular smooth muscle cell (SMC) proliferation after arterial injury. Fragments of Fat1 accumulate in SMC mitochondria, and the Fat1 intracellular domain interacts with multiple mitochondrial proteins, including critical factors associated with the inner mitochondrial membrane. SMCs lacking Fat1 (Fat1KO) grow faster, consume more oxygen for ATP production, and contain more aspartate. Notably, expression in Fat1KO cells of a modified Fat1 intracellular domain that localizes exclusively to mitochondria largely normalizes oxygen consumption, and the growth advantage of these cells can be suppressed by inhibition of mitochondrial respiration, which suggest that a Fat1-mediated growth control mechanism is intrinsic to mitochondria. Consistent with this idea, Fat1 species associate with multiple respiratory complexes, and Fat1 deletion both increases the activity of complexes I and II and promotes the formation of complex-I-containing supercomplexes. In vivo, Fat1 is expressed in injured human and mouse arteries, and inactivation of SMC Fat1 in mice potentiates the response to vascular damage, with markedly increased medial hyperplasia and neointimal growth, and evidence of higher SMC mitochondrial respiration. These studies suggest that Fat1 controls mitochondrial activity to restrain cell growth during the reparative, proliferative state induced by vascular injury. Given recent reports linking Fat1 to cancer, abnormal kidney and muscle development, and neuropsychiatric disease, this Fat1 function may have importance in other settings of altered cell growth and metabolism.

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