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Amyloid P component. A critical review
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“To examine the effects of CPHPC on age-associated bone changes, male and female mice aged 18 months were treated with CPHPC (miridesap) at a concentration of 5 mg ml−1 in drinking water, which is an established dose for SAP depletion from the body62–65,67,68,84.”
From Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis (2025) · cites this paper as [84]
In the citing paper
“It has been well established that SAP is universally present in all human amyloid deposits68,84.”
From Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis (2025) · cites this paper as [84]
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Tsui, C., Copeland, N., Gilbert, D., Jenkins, N., Barnes, C., & Worley, P. (1996) · The Journal of Neuroscience · doi:10.1523/jneurosci.16-08-02463.1996 · Cited by 315
Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene
Botto, M., Hawkins, P. N., Bickerstaff, M. C. M., Herbert, J., Bygrave, A. E., Mcbride, A., Hutchinson, W. L., Tennent, G. A., Walportz, M. J., & Pepys, M. B. (1997) · Nature Medicine · doi:10.1038/nm0897-855 · Cited by 266
Self-citationLiver‐specific and high‐level expression of human serum amyloid P component gene in transgenic mice
Iwanaga, T., Wakasugi, S., Inomoto, T., Uehira, M., Ohnishi, S., Nishiguchi, S., Araki, K., Uno, M., Miyazaki, J., Maeda, S., et al. (1989) · Developmental Genetics · doi:10.1002/dvg.1020100504 · Cited by 20
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Items 101–167 of 167
Normal circulating serum amyloid P component concentration in systemic sclerosis.
Tennent, G., Dziadzio, M., Triantafillidou, E., Davies, P., Gallimore, J., Denton, C., & Pepys, M. (2007) · Arthritis & Rheumatism · doi:10.1002/art.22694 · Cited by 16
Self-citationInfluenza Virus Infection is not Affected by Serum Amyloid P Component
Herbert, J., Hutchinson, W., Carr, J., Ives, J., Jakob-Roetne, R., Yamamura, K., Suzuki, M., & Pepys, M. (2002) · Molecular Medicine · doi:10.1007/bf03401998 · Cited by 16
Self-citationWeiss, N., Jarvis, J. W., Nelson, R., & Hayes, M. A. (2010) · Proteomics · doi:10.1002/pmic.201000310 · Cited by 15
“Human serum amyloid P component (SAP) is a member of the pentraxin protein family and is well known for its calcium-dependent binding properties and presence in amyloid plaques [1].”
Safadi, S., Saad, A., Quint, P., Sethi, S., Leung, N., Kurtin, P. J., & Nasr, S. (2015) · Nephrology, Dialysis and Transplantation · doi:10.1093/ndt/gfv018 · Cited by 14
“In vitro studies have shown that SAP prevents proteolytic degradation of amyloid mediated by the physical presence of SAP coating of fibrils [11, 14].”
BackgroundInvasive candidiasis: new insights presaging new therapeutic approaches?
Pepys, M. (2012) · Journal of Infectious Diseases · doi:10.1093/infdis/jis521 · Cited by 14
“Amyloid deposits also always contain serum amyloid P component (SAP), a normal plasma protein of the pentraxin family that shows avid specific calcium dependent binding to amyloid fibrils of all types [2].”
BackgroundSelf-citationHuman Serum Amyloid P Component Binds to Peripheral Blood Monocytes
Macdonald, S., & Kilpatrick, D. C. (2006) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2006.01774.x · Cited by 12
Genetic evidence for serum amyloid P component as a drug target in neurodegenerative disorders
Schmidt, A. F., Finan, C., Chopade, S., Ellmerich, S., Rossor, M. N., Hingorani, A. D., & Pepys, M. B. (2024) · Open Biology · doi:10.1098/rsob.230419 · Cited by 11
“SAP is named for its universal presence in all human amyloid deposits, which reflects the avid but reversible calcium-dependent binding of SAP to all types of amyloid fibrils regardless of their protein composition [5,6].”
Self-citationKarhadkar, T. R., Pilling, D., & Gomer, R. H. (2021) · PLoS ONE · doi:10.1371/journal.pone.0245924 · Cited by 15
Amyloids in Site-Specific Autoimmune Reactions and Inflammatory Responses
Huang, Y., Hong, X., Shen, J. X., Geng, L.-J., Pan, Y.-H., Ling, W., & Zhao, H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02980 · Cited by 16
“Increased Prevalence of Autoimmunity Disorders in the Absence of Serum Amyloid P SAP component is confirmed as a minor constituent binding to specific determinants shared by all types of amyloid fibrils (190).”
BackgroundGondek, M., Herosimczyk, A., Knysz, P., Ozgo, M., Lepczyński, A., & Szkucik, K. (2020) · Pathogens · doi:10.3390/pathogens9010055 · Cited by 10
“Serum amyloid P component (SAP) is synthesized in the liver, then released into the bloodstream, and its half-life is approximately 24 hours [96,97].”
BackgroundNuclear Imaging of Amyloidosis
Cytawa, W., Teodorczyk, J., & Lass, P. (2014) · Polish Journal of Radiology · doi:10.12659/pjr.890147 · Cited by 11
Kaur, S., & Singh, P. (2004) · Scandinavian Journal of Immunology · doi:10.1111/j.0300-9475.2004.01412.x · Cited by 11
Decline in the expression of C4 binding protein alpha-chain gene during ageing of the rat liver
Lavery, L. W., & Goyns, M. (2004) · Biogerontology (Dordrecht) · doi:10.1023/a:1016251929165 · Cited by 11
“This is interesting because of the association of SAP with amyloid deposits, including those in Alzheimer’s disease (Pepys et al. 1997).”
BackgroundMonoclonal Gammopathies and the Kidney
Touchard, G., Aucouturier, P., Hermine, O., & Ronco, P. (2003) · Springer Netherlands · doi:10.1007/978-94-017-0191-4 · Cited by 11
Yang, J., Zhou, J., Zhou, J. L., Wang, H., Sun, Z., Zhu, X., He, Y., Wong, A. H. C., Liu, F., & Wang, G. (2021) · Journal of Psychiatric Research · doi:10.1016/j.jpsychires.2021.12.051 · Cited by 12
Methylated BSA Mimics Amyloid-Related Proteins and Triggers Inflammation
Domizio, J. D., Dorta-Estremera, S. M., & Cao, W. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063214 · Cited by 8
Evidence for an extended interacting surface between beta-amyloid and serum amyloid P component.
Likó, I., Mâk, M., Klement, É., Hunyadi-Gulyás, É., Pázmány, T., Medzihradszky, K., & Urbányi, Z. (2007) · Neuroscience Letters · doi:10.1016/j.neulet.2006.10.052 · Cited by 10
Monoclonal antibody-based sensitive enzyme-linked immunosorbent assay for murine serum amyloid A.
Yamada, T., Fukuda, T., Wada, A., & Itoh, Y. (1999) · Journal of Immunoassay · doi:10.1080/01971529909349352 · Cited by 10
Choi, S.-A., Yun, J., Park, H.-S., & Choi, J. (2013) · Molecular Biology Reports · doi:10.1007/s11033-012-2229-0 · Cited by 9
“Plasma SAP concentrations are tightly regulated and are best known as universal constituents of amyloid deposits, which are characteristic of systemic amyloidosis, including cerebral amyloid deposits in Alzheimer’s disease and in T2DM [43].”
BackgroundInfluentialOmtvedt, L., Wien, T., Myran, T., Sletten, K., & Husby, G. (2004) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506120410001728063 · Cited by 9
Serological evidence for an inflammatory response in murine scrapie.
Coe, J., Race, R., & Ross, M. J. (2001) · Journal of Infectious Diseases · doi:10.1086/317922 · Cited by 9
“Perhaps the continued formation of PrP amyloid is responsible for SAP leaving the blood, because SAP binds avidly to amyloid fibrils and is a constituent of all amyloids [25].”
BackgroundAbdominal CT findings in nephropathic amyloidosis of familial Mediterranean fever
Apter, S., Zemer, D., Terhakopian, A., Gayer, G., Langevitz, P., Amitai, M., Schwartz, T., Atar, E., Hertz, M., Pras, M., et al. (2001) · Amyloid: Journal of Protein Folding Disorders · doi:10.3109/13506120108993815 · Cited by 9
Merlini, G., Bellotti, V., Andreola, A., Palladini, G. O., Obici, L. P., Casarini, S., & Perfetti, V. (2001) · Clinical Chemistry and Laboratory Medicine (CCLM) · doi:10.1515/cclm.2001.172 · Cited by 31
“Since some of these constituents can play a role in fibril formation (proteoglycans, (59, 60)) and in the stabilization and resistance to proteolysis of amyloid deposits (as reported for SAP (54), and proteoglycans (61)), they became therapeutic targets (62, 63).”
BackgroundInfluentialImmunoradiometric assay for human serum amyloid P component.
Millar, D., Hutchinson, W., & Pepys, M. (2011) · JIM - Journal of Immunological Methods · doi:10.1016/j.jim.2011.06.010 · Cited by 8
Self-citationConserved Domains, Conserved Residues, and Surface Cavities of C-reactive Protein (CRP)
Kumar, S. V., Ravunny, R. K., & Chakraborty, C. (2011) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-011-9270-7 · Cited by 9
Molecular and Cellular Mechanisms Associated with Autoimmune Diseases
Ayensu, W. K., Tchounwou, P. B., & McMurray, R. W. (2004) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph2004010039 · Cited by 9
“Enhanced production of these molecules occurs with increasing age from 3-months [98-115] and results in severe GN similar to findings in patients with SLE disease.”
Characterization of Proteoglycans and Glycosaminoglycans in Splenic AA Amyloid Induced in Mink
Wien, T., Omtvedt, L., Landsverk, T., & Husby, G. (2000) · Scandinavian Journal of Immunology · doi:10.1111/j.1365-3083.2000.00823.x · Cited by 8
Exploring Intrinsic Disorder in Human Synucleins and Associated Proteins
Venati, S. R., & Uversky, V. N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25158399 · Cited by 6
Brynge, M., Gardner, R. M., Sjöqvist, H., Karlsson, H., & Dalman, C. (2022) · Translational Psychiatry · doi:10.1038/s41398-022-01907-z · Cited by 7
“Their exact function is not known, but they are both evolutionarily conserved proteins that bind common molecular patterns on the surface of pathogens and induce complement activation [40, 44].”
BackgroundSerum amyloid P component and cardiovascular disease: is there a sensible link?
Koenig, W. (2007) · Arteriosclerosis, Thrombosis and Vascular Biology · doi:10.1161/01.atv.0000259353.77404.e0 · Cited by 7
Use of genetically altered mice to study the role of serum amyloid P component in amyloid deposition
Maeda, S. (2003) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2003.12088563 · Cited by 7
Homozygous serum amyloid P component-deficiency does not enhance regression of AA amyloid deposits
Usui, I., Kawano, H., Ito, S., Hamada, Y., Ishihara, T., & Maeda, S. (2001) · Amyloid: Journal of Protein Folding Disorders · doi:10.3109/13506120109007351 · Cited by 7
Jung, J., Cha, M., Lee, H., Ko, M., Lee, J.-A., Lee, S.-M., & Lee, M. (2016) · doi:10.1016/j.eujim.2016.02.010 · Cited by 6
Magy-Bertrand, N. (2016) · La Revue de medecine interne · doi:10.1016/j.revmed.2015.12.029 · Cited by 6
“[3] Pepys MB, Booth DR, Hutchinson WR, Gallimore JL, Collins PM, Hohenester E.”
Searching for an in vivo site for nascent amyloid fibril formation
Ali-Khan, Z. (2002) · Journal of Alzheimer s Disease · doi:10.3233/jad-2002-4205 · Cited by 6
“Pepys et al. suggested that amyloidogen-induced sustained inflammation, causing “extreme stimulation”, may account for both the shorter latent period and relatively high incidence of AA amyloidosis in mice [47].”
Pentraxins: The L-Type Lectins and the C-Reactive Protein as a Cardiovascular Risk
Gupta, G. (2012) · Springer eBooks · doi:10.1007/978-3-7091-1065-2_8 · Cited by 8
Bittner, P., Kuhne, F., Pruška, A., Harrison, J. A., Preiss, N., Haberger, M., Reusch, D., & Zenobi, R. (2025) · Angewandte Chemie · doi:10.1002/anie.202505077 · Cited by 5
Karhadkar, T. R., Pilling, D., & Gomer, R. (2020) · bioRxiv · doi:10.1101/2020.08.26.269183 · Cited by 5
“SAP binds to a variety of molecules including DNA and apoptotic debris, bacterial polysaccharides, amyloid deposits, and bacterial and viral proteins (21-23).”
BackgroundAntibody‐based immunotherapy for treatment of immunoglobulin light‐chain amyloidosis
Parrondo, R. D., Majeed, U., & Sher, T. (2020) · British Journal of Haematology · doi:10.1111/bjh.16697 · Cited by 6
“Human serum amyloid P component (SAP) from the plasma is present in all human amyloid deposits due to its binding to amyloid fibrils of all types.(50) Miridesap, is a small molecule that depletes SAP from the plasma but leaves some SAP in amyloid deposits that can be specifically targeted by anti-SAP antibodies.”
BackgroundHärtig, W., Leifsson, P., & Nielsen, O. L. (2005) · Journal of veterinary medicine. A, Physiology, pathology, clinical medicine · doi:10.1111/j.1439-0442.2005.00754.x · Cited by 5
“It is stated that normal tissue AP is found in man (spleen, liver and kidney), but not in any other species (Pepys et al., 1997).”
BackgroundAmylose AA : données actuelles sur la physiopathologie
Magy, N. (2004) · La Revue de Médecine Interne · doi:10.1016/s0248-8663(03)00251-0 · Cited by 5
Splenic ellipsoids: an early target for deposition of AA amyloid induced in mink
Wien, T., Sarby, R., Espenes, A., Gunnes, G., Nordstoga, K., Landsverk, T., & Husby, G. (2003) · Amyloid: Journal of Protein Folding Disorders · doi:10.3109/13506120309041741 · Cited by 5
Serum Amyloid P‐Component‐Induced Colony‐Stimulating Factors Production by Macrophages
Singh, S., & Singh, P. (2001) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.2001.00850.x · Cited by 5
Perkins, S. J., Ullman, C. G., Brissett, N. C., Chamberlain, D., & Boehm, M. K. (1998) · Immunological Reviews · doi:10.1111/j.1600-065x.1998.tb01200.x · Cited by 5
Serum amyloid P component accumulates and persists in neurones following traumatic brain injury
Yip, P. K., Liu, Z., Hasan, S., Pepys, M. B., & Uff, C. E. G. (2023) · Open Biology · doi:10.1098/rsob.230253 · Cited by 6
“SAP is named for its universal presence in all human amyloid deposits, which reflects the avid but reversible calcium dependent binding of SAP to all types of amyloid fibrils regardless of their protein composition [28,29].”
BackgroundSelf-citationOzawa, D., Nomura, R., Mangione, P., Hasegawa, K., Okoshi, T., Porcari, R., Bellotti, V., & Naiki, H. (2017) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2017.1295943 · Cited by 4
“SAP is present universally in all extracellular amyloid deposits [2].”
BackgroundCharacterization of proteoglycans and glycosaminoglycans in splenic AA amyloid induced in mink.
Wien, T., Omtvedt, L., Landsverk, T., & Husby, G. (2000) · doi:10.1046/j.1365-3083.2000.00823.x · Cited by 4
Petrakis, I., Mavroeidi, V., Stylianou, K., Efthymiou, G., Perakis, K., Vardaki, E., Stratigis, S., Giannakakis, K., Kourouniotis, K., Amoiridis, G., et al. (2012) · Transgenic research · doi:10.1007/s11248-012-9632-0 · Cited by 4
“Interestingly high barrier conditions (SPF) were associated with lower NPHS1 content compared to low barrier conditions.”
BackgroundBiomarkers in the diagnosis of neurodegenerative diseases
Haque, S. (2022) · RUDN Journal of Medicine · doi:10.22363/2313-0245-2022-26-4-431-440 · Cited by 6
“and macrophages then bind the SAP, CRP and engulf the debris or other material the pentraxin has bound [53].”
BackgroundIsoforms of Murine and Human Serum Amyloid P Component
Nybo, M., Hackler, R., Kold, B., Nielsen, E. H., Steinmetz, A., & Svehag, S. (1998) · Scandinavian Journal of Immunology · doi:10.1046/j.1365-3083.1998.00404.x · Cited by 3
Schmidt, A. F., Finan, C., Chopade, S., Ellmerich, S., Rossor, M. N., Hingorani, A. D., & Pepys, M. B. (2023) · medRxiv · doi:10.1101/2023.08.15.23293564 · Cited by 4
“SAP is named for its universal presence in all human amyloid deposits, which reflects the avid but reversible calcium dependent binding of SAP to all types of amyloid fibrils regardless of their protein composition 5,6 .”
Self-citationRepeat-Dose and Embryo-Fetal Developmental Toxicity of Zinpentraxin Alfa.
Rao, G. K., Santagostino, S. F., Wong, L., Inoue, A., Arjomandi, A., Yadav, R., & Halpern, W. G. (2023) · Reproductive Toxicology · doi:10.1016/j.reprotox.2023.108526 · Cited by 1
Emerging Molecular Targets in the Therapy of Dialysis‐Related Amyloidosis
Esposito, G., & Bellotti, V. (2010) · doi:10.1002/9780470572702.ch38 · Cited by 1
Localization of injected anti-serum amyloid A antibody to the lesions in murine reactive amyloidosis
Yamada, T., Itoh, K., & Igari, J. (2000) · Modern Rheumatology · doi:10.3109/s101650070005 · Cited by 1
“This was based on the nature of SAP, since it binds preferentially to amyloid fibrils regardless of the amyloidosis type.(8) In spite of its practical utility,(9) the method is not yet available in areas outside Europe.”
BackgroundMorioka, T., Joh, K., Shimizu, F., & Oite, T. (2000) · Clinical and Experimental Nephrology · doi:10.1007/s101570050060 · Cited by 1
“SAP/Amyloid P binds to a variety of ligands, including pyruvate acetal galactose, isolated amyloid fibrils, keratin filament aggregates, and glycosaminoglycans.(24) SAP has been found in all of the vertebrates investigated so far, including plaice, dog, marine toad, chicken, mouse, and humans.”
BackgroundMouse Models of Transthyretin Amyloidosis
Ito, S., & Maeda, S. (2009) · Springer eBooks · doi:10.1007/978-3-642-00646-3_16 · Cited by 1
Uzunhan, Y., Rech, J., Jeny, F., Brillet, P., Kambouchner, M., Arnulf, B., Nunes, H., & Valeyre, D. (2026) · EMC - Pneumologie · doi:10.1016/s1155-195x(25)44652-0
Bittner, P., Kuhne, F., Pruška, A., Harrison, J. A., Preiss, N., Haberger, M., Reusch, D., & Zenobi, R. (2025) · Angewandte Chemie · doi:10.1002/ange.202505077
Hardy, E., Sarker, H., & Fernández-Patrón, C. (2023) · Cells · doi:10.3390/cells12131699
Rech, J.-S., Brillet, P., Jeny, F., Kambouchner, M., Nunes, H., Arnulf, B., Valeyre, D., & Uzunhan, Y. (2019) · Pulmonary Manifestations of Systemic Diseases · doi:10.1183/2312508x.10021719
Liuu, S. (2014) · theses.fr (ABES) · doi:10.70675/642a4f47zb5b3z47e2z9df9z60914a927595
“Le composant P est reconnu par la communauté comme un marqueur des amyloses et est un constituant majeur (jusqu'à 20%) dans tous les dépôts amyloïdes [22,23,39].”
BackgroundHelmfors, L. (2014) · Linköping University Electronic Press eBooks · doi:10.3384/diss.diva-106647
“No deficiency of SAP has been reported in humans (60).”
Biocompatibility and Gene Expression Associated with Streptococcus Infection in Myocarditis
Abdou, S., Ramadan, K., Abumourad, I. M. K., & Hassan, R. E. (2012) · doi:10.5923/j.ijge.20120201.01
Serum amyloid P: A novel antifibrotic agent with therapeutic potential
Lupher, M., & Willett, W. (2010) · Progress in respiratory research/Progress in research in emphysema and chronic bronchitis/Progress in respiration research · doi:10.1159/000320829
Abedini, A., & Raleigh, D. P. (2010) · Wiley eBooks · doi:10.1002/9780470572702.ch23 · Cited by 5
Hagmeyer, L., Hegenbart, U., Schönland, S., Kleibrink, B., & Teschler, H. (2022) · Seltene Lungenerkrankungen · doi:10.1007/978-3-662-63651-0_21
New Blood Biomarkers of Inflammation and Atherosclerosis
Khuseyinova, N., & Koenig, W. (2011) · Humana Press eBooks · doi:10.1007/978-1-60327-179-0_9
Metadata
- Authors
- Pepys, M. B., Booth, D. R., Hutchinson, W. L., Gallimore, J. R., Collins, I. M., & Hohenester, E.
- Affiliations
- Birkbeck, University of London (GB)
- Corresponding author
- Pepys, M B.
- Venue
- Amyloid
- Publisher
- Informa UK Limited
- Published
- 1997-01
- Volume
- 4
- Issue
- 4
- Pages
- 274-295
- ISSN
- 1350-6129 (ISSN-L)
- 1744-2818
- OpenAlex
- W2019288511
- Cited by
- 181
- References
- 0
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 5 · 2023: 4 · 2022: 4 · 2021: 5 · 2020: 5 · 2019: 3 · 2018: 2 · 2017: 2 · 2016: 7 · 2015: 3 · 2014: 5 · 2013: 7 · 2012: 12
- FWCI
- 2.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Amyloid (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Biomarkers in Disease Mechanisms
- Life Sciences › Immunology and Microbiology › Immunology › Complement system in diseases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Inflammasome and immune disorders
- Keywords
- serum amyloid P component, amyloidosis, amyloidosis classification
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