Owing to lack of the structural basis, a-synuclein may not be able to direct mitochondrial fission or fusion. Although Kamp et al. described that a-synuclein could inhibit protein-free model membrane fusion in vitro, but the concentration of a-synuclein in these reactions was much higher than in normal cells. Therefore, it is difficult to rule out a possibility that it may be the result of a simple physical action. a-Synuclein protein is specific to the vertebrate and expresses at high levels in the brain, especially within developing neurons, suggesting its roles in the development of central nervous system. Supposing that a-synuclein directly regulates mitochondrial dynamics, mitochondrial fission/fusion machinery in vertebrate neurons would be very different from that in other types of cells in vertebrate or in non vertebrate neurons, yet there is no evidence to support this hypothesis. When cells become malignant, some of them, such as Hela cells, start to express a-synuclein while the normal cells would not, nonetheless, no data indicate that excessive mitochondrial fission was found in the malignant cells. Additionally, mitochondria are shorter in immature cells than in mature cells, and mitochondrial fission is essential for embryonic development. Mice lacking the mitochondrial fission GTPase Drp1 have developmental abnormalities and die after embryonic day 12.5 and neural cell-specific Drp1 null mice die shortly after birth. Although a-synuclein expression levels are pretty higher in embryos or infants than in adults, mice lacking a-synuclein show only subtle Arctiin abnormalities in neurotransmission, lending an evidence to support that asynuclein expression levels may not affect mitochondrial morphogenesis directly. Since suppression of a-synuclein has potential values for therapy of PD and related diseases, it is of great biological importance that a-synuclein would not play a key role in essential physiological functions. In conclusion, our results demonstrate that neither a-synuclein expression levels nor its localization to mitochondria affects mitochondrial dynamics. But, this does not mean that a-synuclein is in no way involved in regulation of mitochondrial dynamics. In fact, we found that a-synuclein participates in MPP+ induced mitochondrial fragmentation, suggesting that environmental risk factors may be essential for a-synuclein to gain a function to be involved into mitochondrial dynamics,Naringin dihydrochalcone which required further studies. Recently, genetic contributions in PD pathology have received much attention, but cross-sectional twin studies found that even within families affected by monogenic PD, the age of onset, symptoms and end-stage pathology may be quite variable. More than that, no obvious connections were found in PD patients between a-synuclein expression and neuronal damage. In fact, a-synuclein protein levels are far higher during early human development than late when PD usually occurs, and a-synuclein mRNA label is strong in both affected and unaffected neurons in PD. A possible explanation is that certain environmental exposure is necessary for wild-type asynuclein to gain its toxicity in PD patients, and our results may lend evidences to support the hypothesis. Magnetite biomineralization occurs at ambient temperature, pressure, and pH in a variety of organisms, including magnetotactic bacteria, honeybees, chitons, trouts, and homing pigeons. One of the best understood examples of magnetite biomineralization is in magnetotactic bacteria, which carry out magnetite biomineralization in magnetosomes. Magnetotactic bacteria are a diverse group of microorganisms with the ability to use geomagnetic fields for orientation.