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创新与拿来主义

(2007-11-11 06:59:10)
标签:

健康/保健

创新

拿来主义

分类: 闲情逸致
 
创新与拿来主义看似一对不可调和的矛盾,仔细分析,二者之间存在着必然的联系!这就好像造房子,你不可能不要打地基,直接砌上去就得了!
 
运用到科研领域,就显得有点说不清了:全部拿来,完全照搬,当然不行!那是在剽窃!一味创新,完全自主,那是在裤裆里面拉二胡!
 
学习和借鉴是必不可少的环节,拿来的目的是为了创新!解决了二者的位置关系,也就明确了如何拿来,如何创新的问题了!
 
下面这篇文献,与我们课题组的关系比较密切,其中可能有许多我们目前亟待解决,而又不得要领的问题,仔细研读可能会给我们提供一些有益的思路!
 
Oxidative stress-induced phosphorylation, degradation and aggregation of [alpha]-synuclein are linked to upregulated CK2 and cathepsin D
 
Takahashi, Makio; Ko, Li-wen; Kulathingal, Jayanarayan; Jiang, Peizhou; Sevlever, Daniel; Yen, Shu-Hui C.
 
European Journal of Neuroscience. 26(4):863-874, August 2007
 
Intracellular accumulation of [alpha]-synuclein ([alpha]-Syn) as filamentous aggregates is a pathological feature shared by Parkinson's disease, dementia with Lewy bodies and multiple system atrophy, referred to as synucleinopathies. To understand the mechanisms underlying [alpha]-Syn aggregation, we established a tetracycline-off inducible transfectant (3D5) of neuronal lineage overexpressing human wild-type [alpha]-Syn. [alpha]-Syn aggregation was initiated by exposure of 3D5 cells to FeCl2. The exposure led to formation of [alpha]-Syn inclusions and oligomers of 34, 54, 68 kDa and higher molecular weights. The oligomers displayed immunoreactivity with antibodies to the amino-, but not to the carboxyl(C)-, terminus of [alpha]-Syn, indicating that C-terminally truncated [alpha]-Syn is a major component of oligomers. FeCl2 exposure also promoted accumulation of S129 phosphorylated monomeric [alpha]-Syn (P[alpha]-Syn) and casein kinase 2 (CK2); however, G-protein-coupled receptor kinase 2 was reduced. Treatment of FeCl2-exposed cells with CK2 inhibitors (DRB or TBB) led to decreased formation of [alpha]-Syn inclusions, oligomers and P[alpha]-Syn. FeCl2 exposure also enhanced the activity/level of cathepsin D. Treatment of the FeCl2-exposed cells with pepstatin A or NH4Cl led to reduced formation of oligomers/inclusions as well as of ~ 10 and 12 kDa truncated [alpha]-Syn. Our results indicate that [alpha]-Syn phosphorylation caused by FeCl2 is due to CK2 upregulation, and that lysosomal proteases may have a role in producing truncated [alpha]-Syn for oligomer assembly.

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