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Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.
Open accessAbstract
Human serum amyloid P component (SAP) is a normal plasma protein and the precursor of amyloid P component (AP), a universal constituent of the abnormal tissue deposits in amyloidosis, including Alzheimer disease. We show here that its single N-linked biantennary oligosaccharide does not display the microheterogeneity usually characteristic of glycoproteins. The protein and the glycan structures of AP were also invariant, their resistance to degradation suggesting a role in persistence of amyloid deposits. Asialo-SAP was rapidly cleared from the circulation in mice by a mechanism dependent on terminal galactose residues and was catabolized in hepatocytes. However blockade of this pathway did not affect the clearance of native SAP. Rapid hepatic uptake and catabolism of human asialo-SAP in man were also directly demonstrated. The protein and glycan homogeneity of SAP and the integrity of AP suggest that the complete glycoprotein structure is important for the normal and the pathophysiological functions of this molecule.
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Citations
Cited by
Alzheimer’s amyloid fibrils: structure and assembly
Serpell, L. C. (2000) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/s0925-4439(00)00029-6 · Cited by 959
Mullins, R. F., Russell, S. R., Anderson, D. H., & Hageman, G. S. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.7.835 · Cited by 937
Garlanda, C., Bottazzi, B., Bastone, A., & Mantovani, A. (2005) · Annual Review of Immunology · doi:10.1146/annurev.immunol.23.021704.115756 · Cited by 836
Pepys, M. B. (2006) · Annual Review of Medicine · doi:10.1146/annurev.med.57.121304.131243 · Cited by 559
Self-citationTargeted pharmacological depletion of serum amyloid P component for treatment of human amyloidosis
Pepys, M. B., Herbert, J., Hutchinson, W. L., Tennent, G. A., Lachmann, H. J., Gallimore, J. R., Lovat, L. B., Bartfai, T., Alanine, A., Hertel, C., et al. (2002) · Nature · doi:10.1038/417254a · Cited by 540
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Metadata
- Authors
- Pepys, M. B., Rademacher, T. W., Amatayakul-Chantler, S., Williams, P., Noble, G. E., Hutchinson, W. L., Hawkins, P. N., Nelson, S. R., Gallimore, J. R., & Herbert, J.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1994-06-07
- Volume
- 91
- Issue
- 12
- Pages
- 5602-5606
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2132470450
- Cited by
- 214
- References
- 0
- FWCI
- 3.43
- Type
- journal article
- Language
- en
- Open access
- green
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- Pepys, M. B., Rademacher, T. W., Amatayakul-Chantler, S., Williams, P., Noble, G. E., Hutchinson, W. L., Hawkins, P. N., Nelson, S. R., Gallimore, J. R., & Herbert, J. (1994). Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.91.12.5602
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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