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Annexin I is an endogenous ligand that mediates apoptotic cell engulfment.

Engulfment of apoptotic cells requires presentation of new cell surface ligands by the dying cells. Using a differential proteomics technology, we identify that annexin I is a caspase-dependent engulfment ligand; it is recruited from the cytosol and exported to the outer plasma membrane leaflet, colocalizes with phosphatidylserine, and is required for efficient clearance of apoptotic cells. Furthermore, phosphatidylserine receptor (PSR) clustering around apoptotic cells indicates a requirement for annexin I. In the nematode Caenorhabditis elegans, downregulation of the annexin homolog prevents efficient engulfment of pharyngeal cell corpses. These results provide novel mechanistic insights into how apoptotic cells are removed and may explain a pathogenic mechanism of chronic inflammatory diseases where annexin I autoantibodies have been described.

Pubmed ID: 12689596


  • Arur S
  • Uche UE
  • Rezaul K
  • Fong M
  • Scranton V
  • Cowan AE
  • Mohler W
  • Han DK


Developmental cell

Publication Data

April 11, 2003

Associated Grants

  • Agency: NHLBI NIH HHS, Id: P01 HL070694-010004
  • Agency: NHLBI NIH HHS, Id: P01 HL070694-019003
  • Agency: NHLBI NIH HHS, Id: P01 HL070694-036744
  • Agency: NHLBI NIH HHS, Id: P01 HL70694
  • Agency: NIGMS NIH HHS, Id: P20 GM065764-010003
  • Agency: NHLBI NIH HHS, Id: R01 HL 67569
  • Agency: NHLBI NIH HHS, Id: R01 HL067569-01
  • Agency: NHLBI NIH HHS, Id: R01 HL067569-02
  • Agency: NHLBI NIH HHS, Id: R01 HL067569-03
  • Agency: NHLBI NIH HHS, Id: R01 HL067569-04
  • Agency: NCRR NIH HHS, Id: RR13186

Mesh Terms

  • Animals
  • Annexin A1
  • Annexins
  • Apoptosis
  • Caenorhabditis elegans
  • Caenorhabditis elegans Proteins
  • Calcium Signaling
  • Caspases
  • Cell Membrane
  • Cell Membrane Structures
  • Down-Regulation
  • Eukaryotic Cells
  • Helminth Proteins
  • Humans
  • Jumonji Domain-Containing Histone Demethylases
  • Jurkat Cells
  • Ligands
  • Membrane Proteins
  • Peptide Fragments
  • Phagocytosis
  • Protein Transport
  • Receptors, Cell Surface
  • Signal Transduction
  • Up-Regulation