Skip NavigationSkip to Content
Return Return to Search Results

Serum amyloid A is a chemotactic agonist at FPR2, a low-affinity N-formylpeptide receptor on mouse neutrophils

  1. Author:
    Liang, T. S.
    Wang, J. M.
    Murphy, P. M.
    Gao, J. L.

  2. Author Address

    Gao JL NIAID, Host Def Lab, NIH Bldg 10,Room 11N113 Bethesda, MD 20892 USA NIAID, Host Def Lab, NIH Bethesda, MD 20892 USA NCI, Frederick Canc Res & Dev Ctr, Mol Immunoregulat Lab, NIH Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Biochemical and Biophysical Research Communications
    1. 270
    2. 2
    3. Pages: 331-335
  4. Type of Article: Article
  1. Abstract:

    Serum amyloid A (SAA) is an acute-phase plasma protein and the source of amyloid A, which accumulates in lesions of secondary amyloidosis. SAA can induce phagocyte migration in vitro and in vivo, and is a specific chemotactic agonist for the human low-affinity N-formylpeptide receptor FPRL1R, a G-protein-coupled receptor expressed on phagocytes. Here we show that FPR2, a mouse counterpart of FPRL1R, is also an SAA receptor. SAA selectively induced calcium flux and chemotaxis in mouse PMN, which express FPR2, as well as in HEK 293 cells expressing recombinant FPR2 but not in HEK 293 cells expressing FPR, a closely related high affinity N-formylpeptide receptor. Consistent with this, SAA activity on PMN from FPR+/+ and FPR-/- mice was indistinguishable. Moreover, the prototype N-formylpeptide fMLF desensitized SAA-induced calcium flux in a dose-dependent manner in both mouse neutrophils and HEK 293/FPR2 transfectants. Our results suggest that FPRB specifically mediates mouse neutrophil migration in response to SAA. (C) 2000 Academic Press. [References: 22]

    See More

  1. Keywords:

External Sources

  1. No sources found.

Library Notes

  1. No notes added.
NCI at Frederick

You are leaving a government website.

This external link provides additional information that is consistent with the intended purpose of this site. The government cannot attest to the accuracy of a non-federal site.

Linking to a non-federal site does not constitute an endorsement by this institution or any of its employees of the sponsors or the information and products presented on the site. You will be subject to the destination site's privacy policy when you follow the link.

ContinueCancel