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10.4161/auto.27832

http://scihub22266oqcxt.onion/10.4161/auto.27832
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C4091151!4091151 !24458007
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suck abstract from ncbi


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pmid24458007
      Autophagy 2014 ; 10 (4 ): 642-51
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  • Dissection of autophagy in human platelets #MMPMID24458007
  • Feng W ; Chang C ; Luo D ; Su H ; Yu S ; Hua W ; Chen Z ; Hu H ; Liu W
  • Autophagy 2014[Apr]; 10 (4 ): 642-51 PMID24458007 show ga
  • Continuous turnover of intracellular components by autophagy is necessary to preserve cellular homeostasis in all tissues. Despite recent advances in identifying autophagy-related genes and understanding the functions of autophagy in developmental and pathological conditions, so far, the role of autophagy in platelet, a specific anucleate cell type, is poorly understood. In this study, we showed that human platelets express the autophagy-related proteins ATG5, ATG7, and LC3. The same as in nucleated mammalian cells, autophagy was stimulated by cell starvation or the MTOR inhibitor rapamycin in a phosphatidylinositol 3-kinase (PtdIns3K)-dependent manner. Disruption of autophagic flux led to impairment of platelet aggregation and adhesion. Furthermore, Becn1 heterozygous knockout mice displayed a prolonged bleeding time and reduced platelet aggregation. These results suggest a potential role of autophagy in the regulation of platelet function, and imply that gene transcription may not be an essential prerequisite for adaptive autophagy.
  • |Animals [MESH]
  • |Apoptosis Regulatory Proteins/*metabolism [MESH]
  • |Autophagy/*physiology [MESH]
  • |Beclin-1 [MESH]
  • |Bleeding Time [MESH]
  • |Blood Platelets/cytology/*metabolism [MESH]
  • |Heterozygote [MESH]
  • |Humans [MESH]
  • |Mice [MESH]
  • |Phosphatidylinositol 3-Kinases/metabolism [MESH]
  • |Signal Transduction/*physiology [MESH]
  • |TOR Serine-Threonine Kinases/antagonists & inhibitors/metabolism [MESH]


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