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Serum amyloid P component (not Serum Amyloid Protein)

Nature Medicine volume 5, pages 852–853 (1999)Cite this article

To the editor—We enjoyed reading the June issue News & Views article1 by Paul and Carroll that accompanied our paper2 reporting the development of anti-nuclear autoimmunity in mice with targeted deletion of the gene for serum amyloid P component (abbreviated as SAP, according to the World Health Organization–International Union of Immunological Societies nomenclature of disease). It is, however, important to identify this protein correctly. There is no such thing as "serum amyloid protein," which appears on the cover of the journal and in the article by Paul and Carroll. This is not a trivial point, as most of the proteins in amyloid deposits are serum proteins. It is also important to recognize that far from just suffering 'guilt by association' with amyloid deposits, SAP contributes to the pathogenesis of amyloidosis in vivo3,4.

Although it is tempting to link our findings in the SAP knockout mice to the human disease of systemic lupus erythematosus (SLE), as Paul and Carroll sought to do, SLE patients do not have SAP deficiency and there is no robust evidence for structural polymorphism of the human SAP gene, protein or glycan. A genetic polymorphism linked to, but not within, the human SAP gene has no effect on the structure, function or in vivo metabolism of SAP (ref. 5). Human SAP has one of the most invariant glycans of any known glycoprotein6, although it has not yet been studied specifically in SLE. It seems more likely that the pentraxin protein abnormality, which is potentially related to pathogenesis of anti-nuclear autoimmunity in human SLE, is the well-recognized failure of SLE patients to mount substantial acute phase responses of C-reactive protein to non-infective autologous tissue damage2,7.

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References

  1. Paul, E. & Carroll, M.C. SAP-less chromatin triggers systemic lupus erythematosus. Nature Med. 5, 607–608 (1999).

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  2. Bickerstaff, M.C.M. et al. Serum amyloid P component controls chromatin degradation and prevents anti-nuclear autoimmunity. Nature Med. 5, 694–697 (1999).

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  3. Botto, M. et al. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nature Med. 3, 855–859 (1997).

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  4. Togashi, S. et al. Serum amyloid P component enhances induction of murine amyloidosis. Lab. Invest. 77, 525–531 (1997).

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  5. Hawkins, P.N., Tennent, G.A., Woo, P. & Pepys, M.B. Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis. Clin. Exp. Immunol. 84, 308–316 (1991).

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  6. Pepys, M.B. et al. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc. Natl. Acad. Sci. USA 91, 5602–5606 1994).

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  7. Pepys, M.B., Lanham, J.G. & de Beer, F.C. in Clinics in the Rheumatic Diseases (ed. Hughes, G.R.V.) 91–103 (W.B. Saunders, Eastbourne, UK, 1982).

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  1. Immunological Medicine Unit, Hammersmith Hospital, London, W12 0NN

    M.B. Pepys

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Pepys, M. Serum amyloid P component (not Serum Amyloid Protein). Nat Med 5, 852–853 (1999). https://doi.org/10.1038/11272

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