Mass Spectrometry and Computer Simulation Predict the Interactions of AGPS and HNRNPK in Glioma.

Ether lipids are overexpressed in malignant tumor and play an important role in tumor process. Glioma is the most common malignant central nervous system tumor, and the content of ether lipids is higher than that of normal tissues. Alkylglycerone phosphate synthase (AGPS) is a key enzyme in the synt...

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Published in:BioMed Research International pp. 1 - 15
Main Authors: Zhou, Wei, Liu, Ying, Li, Honglian, Song, Zhaoyu, Ma, Ying, Zhu, Yu
Format: pictorial research tables/charts Journal Article
Published: Wiley-Blackwell 9/28/2021
Online Access:View this record in EBSCOhost
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      dt: 9/28/2021
      pid: 480
      pub: Wiley-Blackwell
      place: Malden, Massachusetts
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        152681258
        152681258
        152681258
        10.1155/2021/6181936
        152681258
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        atl: Mass Spectrometry and Computer Simulation Predict the Interactions of AGPS and HNRNPK in Glioma.
      aug:
        au:
          Zhou, Wei
          Liu, Ying
          Li, Honglian
          Song, Zhaoyu
          Ma, Ying
          Zhu, Yu
        affil: Department of Neurology, Tianjin People's Hospital, Tianjin 300191, China
      sug:
        subj:
          Mass Spectrometry
          Computer Simulation
          Glioma
          Carrier Proteins Metabolism
          Enzymes Metabolism
          Cell Line, Tumor Metabolism
          Phospholipids Metabolism
          Human
          Cell Proliferation
          Precipitin Tests
          Blotting, Western
          Microscopy
          Chemistry, Physical
          Gene Expression
      ab: Ether lipids are overexpressed in malignant tumor and play an important role in tumor process. Glioma is the most common malignant central nervous system tumor, and the content of ether lipids is higher than that of normal tissues. Alkylglycerone phosphate synthase (AGPS) is a key enzyme in the synthesis of ether esters and plays a vital role in maintaining the morphology and pathogenic properties of tumor cells. The cell proliferation and the content of tumor-related lipid such as monoalkylglycerol ether (MAGe), lysophosphatidic acid ether (LPAe), lysophosphatidylcholine ether (LPCe), lysophosphatidylethanolamine ether (LPEe), phosphatidyl inositol (PI), phosphatidylcholine (PC), and phosphatidylserine (PS) were suppressed after AGPS silencing in U251, H4, and TJ905 cells; however, heterogeneous nuclear ribonucleoprotein K (HNRNPK) could reverse the above phenomenon such as cellar proliferation and ether lipid secretion. We found that HNRNPK was the target protein of AGPS by coimmunoprecipitation and mass spectrometry assay and verified by western blot assay in U251 cells. It confirmed that AGPS and HNRNPK are coexpressed in the cellular nucleus by a confocal laser microscope. The main protein-protein interaction mechanism between AGPS and HNRNPK is hydrogen bond, conjugation bond, hydrophobic bond, and electrostatic force by computer simulation prediction.
      pubtype: Academic Journal
      doctype:
        pictorial
        research
        tables/charts
        Journal Article
      ougenre: Article
    language: English
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