JOURNAL OF SHANDONG UNIVERSITY (HEALTH SCIENCES) ›› 2013, Vol. 51 ›› Issue (10): 15-18.

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Glial fibrillary acid protein lysine acetylated modification in ALS mouse

LI Jun-qiang1, GUO Ji-sheng1, WANG Xiao-yue1, WANG Dao-guang1, ZHAO Zuo-hui2, YANG Jing-hua1   

  1. 1. Department of Cancer Research Center, School of Medicine, Shandong University, Jinan 250012, China;
    2. Department of Urology, Shandong Provincial Hospital Affiliated to Shandong University, Jinan 250021, China
  • Received:2013-03-04 Online:2013-10-10 Published:2013-10-10

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Abstract:

Objective  To investigate glial fibrillary acidic protein (GFAP) lysine acetylated modification in the spinal cord tissue of amyotrophic lateral sclerosis (ALS) model mouse.  Methods  After 3 ALS mice about 4 months old were sacrificed with anesthesia, total protein was extracted by RIPA lysis buffer; GFAP and Pan-AC protein expression were identified by immunoprecipitation and western blotting. Then IP-purified GFAP protein was analyzed using liquid chromatography-tandem mass spectrometry (LC-MS/MS). Results  IP-purified GFAP protein from ALS mice was acetylated in lysine residues, and the GFAP 394 and 402 lysine residues were confirmed by LC-MS/MS. Conclusion  The lysine residue of GFAP can be modified by acetylation, which may participate in the occurrence of ALS.

Key words: Glial fibrillary acidic protein; Acetylated modification; Amyotrophic lateral sclerosis; LC-MS/MS

CLC Number: 

  • R34
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