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论坛首页  >  医药生命科学动态跟踪   >  精华陈列馆
该话题已被移动 - lightningwing , 2013-08-12 06:07
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【聚焦】走进细胞自噬 [精华]

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lzmjxg
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b050403
学习了
2010-12-29 11:12
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楼主,太强了!学到很多东西,我准备做肿瘤的自噬。想请教您个有关自噬的问题。希望给予帮助。
如果要用realtime-PCR来检测自噬的表达LC3,不知LC3-II的基因是哪个?我用pubmed查了一下好像有LC3A、LC3B、LC3C,而且每个基因都有变异体,应该用哪个基因呢?
2010-12-31 16:33
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楼主 tangdl2000
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J Immunol. 2010 Dec 29. [Epub ahead of print]

Autophagy Regulates Endoplasmic Reticulum Homeostasis and Calcium Mobilization in T Lymphocytes.
自噬调节内质网应激和钙稳态在T淋巴细胞


Jia W, Pua HH, Li QJ, He YW.

Department of Immunology, Duke University Medical Center, Durham, NC 27710.

Abstract
Macroautophagy (hereafter referred to as autophagy) is an evolutionarily conserved intracellular bulk degradation pathway that plays critical roles in eliminating intracellular pathogens, presenting endogenous Ags, and regulating T lymphocyte survival and proliferation. In this study, we have investigated the role of autophagy in regulating the endoplasmic reticulum (ER) compartment in T lymphocytes. We found that ER content is expanded in mature autophagy-related protein (Atg) 7-deficient T lymphocytes. Atg7-deficient T cells stimulated through the TCR display impaired influx, but not efflux, of calcium, and ER calcium stores are increased in Atg7-deficient T cells. Treatment with the ER sarco/ER Ca(2+)-ATPase pump inhibitor thapsigargin rescues the calcium influx defect in Atg7-deficient T lymphocytes, suggesting that this impairment is caused by an intrinsic defect in ER. Furthermore, we found that the stimulation-induced redistribution of stromal interaction molecule-1, a critical event for the store-operated Ca(2+) release-activated Ca(2+) channel opening, is impaired in Atg7-deficient T cells. Together, these findings indicate that the expanded ER compartment in Atg7-deficient T cells contains increased calcium stores, and the inability of these stores to be depleted causes defective calcium influx in these cells. Our results demonstrate that autophagy plays an important role in maintaining ER and calcium homeostasis in T lymphocytes.

PMID: 21191072 [PubMed - as supplied by publisher

  • jimmunol.1001822.full.pdf(1415.12k)
2011-01-01 05:25
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楼主 tangdl2000
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Autophagy. 2011 Mar 1;7(3). [Epub ahead of print]

Selective autophagy mediated by autophagic adapter proteins.
自噬适配器介导选择性自噬


Johansen T, Lamark T.

Molecular Cancer Research Group; Institute of Medical Biology; University of Troms?; Troms?, Norway.

Abstract
Mounting evidence suggests that autophagy is a more selective process than originally anticipated. The discovery and characterization of autophagic adapters, like p62 and NBR1, has provided mechanistic insight into this process. p62 and NBR1 are both selectively degraded by autophagy and able to act as cargo receptors for degradation of ubiquitinated subtstrates. A direct interaction between these autophagic adapters and the autophagosomal marker protein LC3, mediated by a so-called LIR (LC3-interacting region) motif, their inherent ability to polymerize or aggregate as well as their ability to specifically recognize substrates are required for efficient selective autophagy. These three required features of autophagic cargo receptors are evolutionarily conserved and also employed in the yeast cytoplasm-to-vacuole targeting (Cvt) pathway and in the degradation of P granules in C. elegans. Here, we review the mechanistic basis of selective autophagy in mammalian cells discussing the degradation of misfolded proteins, p62 bodies, aggresomes, mitochondria and invading bacteria. The emerging picture of selective autophagy affecting the regulation of cell signaling with consequences for oxidative stress responses, tumorigenesis and innate immunity is also addressed.

PMID: 21189453

  • JohansenAUTO7-3.pdf(2873.34k)
2011-01-01 05:31
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tangdl2000 编辑于 2011-01-01 10:36
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