ELISA for quantitation of L-selectin shed from leukocytes in vivo

J Immunol Methods. 1992 Nov 25;156(1):115-23. doi: 10.1016/0022-1759(92)90017-n.


L-selectin is a cell surface receptor on granulocytes, lymphocytes and monocytes that is responsible for the initial attachment of leukocytes to endothelium. The extracellular domain of L-selectin is proteolytically shed from leukocytes following cellular activation in vitro. The shed form of L-selectin (SL-selectin) is functionally active and at high concentrations can inhibit leukocyte attachment to endothelium. Therefore, an ELISA was developed to quantitate the levels of SL-selectin in biological fluids, biopsy specimens and during recombinant protein production. This simple, quantitative sandwich ELISA uses two monoclonal antibodies directed against the extracellular domain of SL-selectin. The assay has a detection range of 5-1300 ng/ml, is precise and sensitive. The ability of this assay to detect SL-selectin in serum, plasma, and culture supernatant fluid was demonstrated and it was used to quantitate circulating SL-selectin in normal and patient sera. Patients with sepsis and HIV infection showed markedly elevated SL-selectin levels in serum. Thus, the ELISA should prove useful both for laboratory purposes as well as in the diagnostic evaluation of patients with inflammatory diseases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Cell Adhesion Molecules / blood*
  • Cells, Cultured
  • Culture Media / analysis
  • Enzyme-Linked Immunosorbent Assay / methods*
  • Freezing
  • Humans
  • In Vitro Techniques
  • L-Selectin
  • Leukocytes / metabolism*
  • Swine


  • Antibodies, Monoclonal
  • Cell Adhesion Molecules
  • Culture Media
  • L-Selectin