Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion†

  1. Jin-Ku Kim1,
  2. Evan A. Scott2,
  3. Donald L. Elbert2,*

Article first published online: 4 AUG 2005

DOI: 10.1002/jbm.a.30424

Issue

Journal of Biomedical Materials Research Part A

Journal of Biomedical Materials Research Part A

Volume 75A, Issue 1, pages 199–209, 1 October 2005

Additional Information

How to Cite

Kim, J.-K., Scott, E. A. and Elbert, D. L. (2005), Proteomic analysis of protein adsorption: Serum amyloid P adsorbs to materials and promotes leukocyte adhesion. Journal of Biomedical Materials Research Part A, 75A: 199–209. doi: 10.1002/jbm.a.30424

Author Information

  1. 1

    Department of Chemical Engineering, Washington University, St. Louis, Missouri 63130

  2. 2

    Department of Biomedical Engineering and Center for Materials Innovation, Washington University, Campus Box 1097, One Brookings Drive, St. Louis, Missouri 63130

*Department of Biomedical Engineering and Center for Materials Innovation, Washington University, Campus Box 1097, One Brookings Drive, St. Louis, Missouri 63130

  1. †

    No benefit of any kind will be received either directly or indirectly by the author(s).

Publication History

  1. Issue published online: 25 AUG 2005
  2. Article first published online: 4 AUG 2005
  3. Manuscript Accepted: 10 MAR 2005
  4. Manuscript Revised: 9 MAR 2005
  5. Manuscript Received: 10 AUG 2004

Funded by

  • Barnes-Jewish Foundation. Grant Number: 5681-01

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Keywords:

  • protein adsorption;
  • proteomics;
  • serum amyloid P;
  • leukocyte

Abstract

Serum and plasma protein adsorption on materials was analyzed using gel electrophoresis and ion trap mass spectrometry. Following incubation of polypropylene, polyethylene terephthalate (PET), or polydimethylsiloxane (PDMS) with 5% serum for longer than 4 h, we found unexpectedly high amounts of the pentraxin serum amyloid P. It was previously shown that serum amyloid P is constitutively expressed in humans, functions as an opsonin, and interacts with the Fcγ receptors on leukocytes. We demonstrate that serum amyloid P adsorbed to tissue culture polystyrene, PDMS, and PET promotes the adhesion of granulocytes and monocytes in the presence of calcium. The methods developed for these studies may be useful for the large-scale study of protein adsorption and do not rely on radiolabeling or the availability of antibodies. © 2005 Wiley Periodicals, Inc. J Biomed Mater Res, 2005

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