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Distinct cell surface proteome profiling by biotin labeling and glycoprotein capturing.

Kohji Nagano1, Takashi Shinkawa, Kuniyasu Kato

  • 1Discovery Science & Technology Dept., Chugai Pharmaceutical Co. Ltd., Kanagawa, 247-8530, Japan. naganokuj@chugai-pharm.co.jp

Journal of Proteomics
|May 31, 2011
PubMed
Summary

Mass spectrometry identified cell surface proteins using biotin labeling and glycoprotein capturing. Different methods revealed unique and overlapping plasma membrane proteins, influenced by glycosylation and expression levels.

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Area of Science:

  • Proteomics
  • Cell Biology
  • Cancer Research

Background:

  • Cell surface proteins are crucial for cellular functions and interactions.
  • Understanding the cell surface proteome is vital for identifying potential biomarkers and therapeutic targets.
  • HCT-116 cells are a widely used model for colorectal cancer research.

Purpose of the Study:

  • To perform mass spectrometry (MS)-based cell surface proteome profiling of HCT-116 cells.
  • To compare the efficacy of two distinct methods: biotin labeling and glycoprotein capturing.
  • To identify plasma membrane proteins expressed in both cell culture and xenograft models.

Main Methods:

  • MS-based proteome profiling of HCT-116 cells.
  • Biotin labeling of cell surface proteins.

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  • Glycoprotein capturing for N-glycosylated proteins.
  • Ingenuity Pathway Analysis for protein localization.
  • Comparison of protein identification between cell culture and xenograft samples.

    • Main Results:

    • Identified 742 biotinylated and 219 glycosylated proteins.
    • 224 and 138 plasma membrane proteins were identified by biotin labeling and glycoprotein capturing, respectively.
    • 104 plasma membrane proteins were common to both methods; 154 were unique to one method.
    • Identified 312 N-glycosylated proteins from xenograft samples, with 135 known plasma membrane proteins.
    • Observed both common and unique plasma membrane protein expression between cultured and xenograft cells.

    Conclusions:

    • Biotin labeling and glycoprotein capturing yield distinct, yet complementary, cell surface proteomes.
    • Discrepancies in identified proteins may relate to glycosylation site number, expression, and glycosylation levels.
    • Culture and xenograft environments drive differential expression of cell surface proteins.
    • Identified proteins may play roles in adaptation to different growth environments.