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Antibodies to human serum amyloid P component eliminate visceral amyloid deposits

Author

Listed:
  • Karl Bodin

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Stephan Ellmerich

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Melvyn C. Kahan

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Glenys A. Tennent

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Andrzej Loesch

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Janet A. Gilbertson

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Winston L. Hutchinson

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Palma P. Mangione

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus
    Università di Pavia, Via Taramelli 3b, 27100 Pavia, Italy)

  • J. Ruth Gallimore

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • David J. Millar

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Shane Minogue

    (Centre for Molecular Cell Biology, University College London, Royal Free Campus)

  • Amar P. Dhillon

    (University College London, Royal Free Campus)

  • Graham W. Taylor

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Arthur R. Bradwell

    (The Medical School, University of Birmingham
    The Binding Site Ltd)

  • Aviva Petrie

    (Biostatistics Unit, UCL Eastman Dental Institute)

  • Julian D. Gillmore

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Vittorio Bellotti

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus
    Università di Pavia, Via Taramelli 3b, 27100 Pavia, Italy)

  • Marina Botto

    (Rheumatology Section, Faculty of Medicine, Imperial College London, Hammersmith Campus)

  • Philip N. Hawkins

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

  • Mark B. Pepys

    (Centre for Amyloidosis and Acute Phase Proteins, University College London, Royal Free Campus)

Abstract

Dual attack on amyloidosis Systemic amyloidosis is a serious disease caused by accumulation of amyloid fibrils in the viscera and connective tissues. Serum amyloid P (SAP) is a normal plasma protein that concentrates within the amyloid deposits. Working in a mouse model of the disease, Mark Pepys and colleagues find that a combination of a drug that depletes circulating SAP and an antibody that targets residual SAP within the deposits results in clearance of amyloid deposits. A humanized version of the anti-SAP antibody has been developed with a view to clinical evaluation of this dual approach.

Suggested Citation

  • Karl Bodin & Stephan Ellmerich & Melvyn C. Kahan & Glenys A. Tennent & Andrzej Loesch & Janet A. Gilbertson & Winston L. Hutchinson & Palma P. Mangione & J. Ruth Gallimore & David J. Millar & Shane Mi, 2010. "Antibodies to human serum amyloid P component eliminate visceral amyloid deposits," Nature, Nature, vol. 468(7320), pages 93-97, November.
    • Handle: RePEc:nat:nature:v:468:y:2010:i:7320:d:10.1038_nature09494
    DOI: 10.1038/nature09494
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