Cited by 181Biomarkers in Disease MechanismsComplement system in diseasesInflammasome and immune disorders

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Amyloid P component. A critical review

Pepys, M B., Booth, D. R., Hutchinson, W. L., Gallimore, J. R., Collins, I. M., Hohenester, E.·1997·Amyloid

DOI 10.3109/13506129709003838

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Narp, a novel member of the pentraxin family, promotes neurite outgrowth and is dynamically regulated by neuronal activity
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
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Liver‐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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Self-citation
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-citation
Amyloidosis: a convoluted story
Kyle, R. (2001) · British Journal of Haematology · doi:10.1046/j.1365-2141.2001.02999.x · Cited by 239
“It apparently protects amyloid fibrils from proteolytic degradation, but its physiological function is unknown (Pepys et al, 1997).”
Pathogenesis, diagnosis and treatment of systemic amyloidosis.
Pepys, M. (2001) · Philosophical transactions of the Royal Society of London. Series B, Biological sciences · doi:10.1098/rstb.2000.0766 · Cited by 233
Self-citation
Pathology, diagnosis and pathogenesis of AA amyloidosis
Röcken, C., & Shakespeare, A. (2002) · Virchows Archiv · doi:10.1007/s00428-001-0582-9 · Cited by 213
Review: immunoglobulin light chain amyloidosis--the archetype of structural and pathogenic variability.
Bellotti, V., Mangione, P., & Merlini, G. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4248 · Cited by 198
Mechanisms of islet amyloidosis toxicity in type 2 diabetes
Abedini, A., & Schmidt, A. M. (2013) · FEBS Letters · doi:10.1016/j.febslet.2013.01.017 · Cited by 206
“amyloid P component (SAP), apolipoprotein E (apoE), and the heparan sulfate proteoglycan (HSPG) perlecan [49–52].”
Background
Diagnostic performance of 123I-labeled serum amyloid P component scintigraphy in patients with amyloidosis.
Hazenberg, B., van Rijswijk, M., Piers, D., Hooge, M. L.-D., Vellenga, E., Haagsma, E., Hawkins, P., & Jager, P. (2006) · American Journal of Medicine · doi:10.1016/j.amjmed.2005.08.043 · Cited by 177
Serum amyloid P component scintigraphy for diagnosis and monitoring amyloidosis
Hawkins, P. (2002) · Current opinion in nephrology and hypertension · doi:10.1097/00041552-200211000-00013 · Cited by 147
Repeat doses of antibody to serum amyloid P component clear amyloid deposits in patients with systemic amyloidosis
Richards, D. B., Cookson, L. M., Barton, S. V., Liefaard, L., Lane, T., Hutt, D. F., Ritter, J. M., Fontana, M., Moon, J. C., Gillmore, J. D., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aan3128 · Cited by 136
“Human serum amyloid P component (SAP) from the plasma is present in all human amyloid deposits due to its avid but reversible bind ing to amyloid fibrils of all types (4).”
BackgroundSelf-citation
Sustained pharmacological depletion of serum amyloid P component in patients with systemic amyloidosis
Gillmore, J., Tennent, G., Hutchinson, W., Gallimore, J., Lachmann, H., Goodman, H., Offer, M., Millar, D., Petrie, A., Hawkins, P., et al. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.08036.x · Cited by 136
“Serum amyloid P component (SAP) is a normal, constitutive, invariant plasma glycoprotein of the pentraxin family that binds calcium-dependently to amyloid fibrils (Pepys et al, 1979, 1997) and is thereby selectively concentrated in all amyloid deposits in vivo (Pepys, 2006).”
BackgroundSelf-citation
Sensitive biosensor array using surface plasmon resonance on metallic nanoslits.
Lee, K.-L., Lee, C.-W., Wang, W.-S., & Wei, P.-K. (2007) · Journal of Biomedical Optics · doi:10.1117/1.2772296 · Cited by 132
“It was first identified as the pentagonal constituent of in vivo pathological deposits(14) and is thought to be an important contributor to the pathogenesis of a related group of diseases called the amyloidoses.(15) We applied the nanoslit array to detect the anti-SAP and SAP interactions on the gold surface.”
Background
Amyloidogenesis in its biological environment: challenging a fundamental issue in protein misfolding diseases.
Bellotti, V., & Chiti, F. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.10.001 · Cited by 121
Insulin amyloid at injection sites of patients with diabetes
Nilsson, M. R. (2016) · Amyloid · doi:10.1080/13506129.2016.1179183 · Cited by 129
“Amyloid P, derived from serum amyloid P, is frequently observed in association with amyloid deposits in vivo [55].”
Background
Extrahepatic production of acute phase serum amyloid A.
Upragarin, N., Landman, W., Gaastra, W., & Gruys, E. (2005) · Histology and Histopathology · doi:10.14670/hh-20.1295 · Cited by 118
Pentameric and decameric structures in solution of serum amyloid P component by X-ray and neutron scattering and molecular modelling analyses.
Ashton, A. W., Boehm, M., Gallimore, J., Pepys, M., & Perkins, S. J. (1997) · Journal of Molecular Biology · doi:10.1006/jmbi.1997.1271 · Cited by 118
Self-citation
Aggregated IgG inhibits the differentiation of human fibrocytes
Pilling, D., Tucker, N. M., & Gomer, R. H. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0805456 · Cited by 104
Cross-interactions between the Alzheimer Disease Amyloid-β Peptide and Other Amyloid Proteins: A Further Aspect of the Amyloid Cascade Hypothesis
Luo, J., Wärmländer, S. K. T. S., Gräslund, A., & Abrahams, J. P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.r116.714576 · Cited by 142
“In vivo, human amyloid deposits often contain SAP together with a primary amyloid component such as A (74).”
Background
Biological activity and pathological implications of misfolded proteins
Bellotti, V., Mangione, P. P., & Stoppini, M. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050348 · Cited by 116
Pathophysiology and treatment of systemic amyloidosis
Gillmore, J., & Hawkins, P. (2013) · Nature Reviews Nephrology · doi:10.1038/nrneph.2013.171 · Cited by 113
Biochemistry of Barnacle Adhesion: An Updated Review
Liang, C., Strickland, J. V., Ye, Z., Wu, W.-J., Hu, B.-R., & Rittschof, D. (2019) · Frontiers in Marine Science · doi:10.3389/fmars.2019.00565 · Cited by 110
Structural diversity of ex vivo amyloid fibrils studied by cryo-electron microscopy.
Jimenez, J. L., Tennent, G., Pepys, M., & Saibil, H. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.4863 · Cited by 109
Self-citation
Sulfated Glycosaminoglycans Accelerate Transthyretin Amyloidogenesis by Quaternary Structural Conversion
Bourgault, S., Solomon, J. P., Reixach, N., & Kelly, J. W. (2010) · Biochemistry · doi:10.1021/bi101822y · Cited by 103
“Similarly, it has been reported that the ability of GAGs to bind to Aβ(1-28) and Aβ(1-40) is also pH dependent (72) and that the binding of heparin to IAPP exhibits a higher affinity at low pH due to histidine protonation (73), supporting the importance of electrostatic interactions.”
Background
Protein Misfolding Diseases
Ramirez-Alvarado, M., Kelly, J. W., & Dobson, C. M. (2010) · Wiley eBooks · doi:10.1002/9780470572702 · Cited by 79
The Development of Serum Amyloid P as a Possible Therapeutic
Pilling, D., & Gomer, R. H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02328 · Cited by 92
“SAP is made by hepatocytes and secreted into the blood (1, 2).”
Background
How to diagnose amyloidosis
Mollee, P., Renaut, P., Gottlieb, D., & Goodman, H. (2014) · Internal medicine journal (Print) · doi:10.1111/imj.12288 · Cited by 88
The β-Slip
Eneqvist, T., Andersson, K., Olofsson, A., Lundgren, E., & Sauer-Eriksson, A. E. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)00117-9 · Cited by 90
On Typing Amyloidosis Using Immunohistochemistry. Detailled Illustrations, Review and a Note on Mass Spectrometry
LINKE, R. P. (2012) · Progress in Histochemistry and Cytochemistry · doi:10.1016/j.proghi.2012.03.001 · Cited by 97
In vivo supramolecular templating enhances the activity of multivalent ligands: A potential therapeutic against the Escherichia coli O157 AB5 toxins
Kitov, P., Mulvey, G. L., Griener, T., Lipiński, T., Solomon, D., Paszkiewicz, E., Jacobson, J. M., Sadowska, J., Suzuki, M., Yamamura, K., et al. (2008) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0804919105 · Cited by 84
“One of HuSAP’s normal physiological functions may be to bind to the cellular debris produced during apoptosis and inflammation (25), thereby redirecting potentially harmful inf lammatory by-products to the RES where they may be catabolically disposed.”
BackgroundMethod
Amyloidosis and the lung
Lachmann, H., & Hawkins, P. (2006) · Chronic Respiratory Disease · doi:10.1177/1479972306070066 · Cited by 81
“The universal presence of SAP in amyloid deposits [7] reflects its specific binding to”
Background
Molecular dissection of Alzheimer's disease neuropathology by depletion of serum amyloid P component
Kolstoe, S., Ridha, B., Bellotti, V., Wang, N., Robinson, C., Crutch, S., Keir, G., Kukkastenvehmas, R., Gallimore, J., Hutchinson, W., et al. (2009) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.0902640106 · Cited by 74
“However, the universal presence of serum amyloid P component (SAP) (1) in cerebrospinal f luid (CSF) (2) and bound to cerebral and cerebrovascular amyloid deposits and to neurofibrillary tangles in Alzheimer disease (3–9) is consistent with a role of SAP in pathogenesis.”
BackgroundSelf-citation
Autoimmunity and glomerulonephritis in mice with targeted deletion of the serum amyloid P component gene: SAP deficiency or strain combination?
Gillmore, J., Hutchinson, W., Herbert, J., Bybee, A., Mitchell, D., Hasserjian, R., Yamamura, K., Suzuki, M., Sabin, C., & Pepys, M. (2004) · Immunology · doi:10.1111/j.1365-2567.2004.01860.x · Cited by 70
Self-citation
Immunotherapy in Systemic Primary (AL) Amyloidosis Using Amyloid-Reactive Monoclonal Antibodies
Solomon, A., Weiss, D., & Wall, J. (2003) · Cancer Biotherapy and Radiopharmaceuticals · doi:10.1089/108497803322702824 · Cited by 68
“Despite the progress made in defining the structural basis of light chain amy-loidogenicity 10–14 and identifying accessory molecules that contribute to the formation of fibrillar deposits, 15,16 there is virtually no information on the pathogenesis of this disorder.”
Human Serum Amyloid P Component is a Single Uncomplexed Pentamer in Whole Serum
Hutchinson, W. L., Hohenester, E., & Pepys, M. B. (2000) · Molecular Medicine · doi:10.1007/bf03401789 · Cited by 66
“Analysis of the packing of SAP pentamers in several unrelated crystal forms suggests that Glu167, the side chain of which protrudes from the N-terminus of the -helix on the A face, is the structure responsible (18).”
BackgroundSelf-citation
Diagnostic Performance and Prognostic Value of Extravascular Retention of 123I-Labeled Serum Amyloid P Component in Systemic Amyloidosis
Hazenberg, B., van Rijswijk, M., Hooge, M. L.-D., Vellenga, E., Haagsma, E., Posthumus, M., & Jager, P. (2007) · Journal of Nuclear Medicine · doi:10.2967/jnumed.106.039313 · Cited by 66
“SAP binds in a calcium-dependent way to amyloid fibrils of all types (2,3).”
Background
Apolipoproteins and amyloid fibril formation in atherosclerosis
Teoh, C. L., Griffin, M. D. W., & Howlett, G. J. (2011) · Protein & Cell · doi:10.1007/s13238-011-1013-6 · Cited by 61
“Serum amyloid P component and apolipoprotein E SAP is a circulating serum protein which co-localizes to all amyloid deposits that have been identified in vivo (Pepys et al., 1997; Kisilevsky, 2000).”
Background
Human serum amyloid P component protects against Escherichia coli O157:H7 Shiga toxin 2 in vivo: therapeutic implications for hemolytic-uremic syndrome.
Armstrong, G., Mulvey, G. L., Marcato, P., Griener, T., Kahan, M., Tennent, G., Sabin, C., Chart, H., & Pepys, M. (2006) · Journal of Infectious Diseases · doi:10.1086/501472 · Cited by 61
“have been strictly calcium dependent [14], but we found avid”
BackgroundSelf-citation
Osteo-articular manifestations of amyloidosis.
M'bappé, P., & Grateau, G. (2012) · Baillière's Best Practice & Research : Clinical Rheumatology · doi:10.1016/j.berh.2012.07.003 · Cited by 59
“Photo 3. Typical “shoulder pad” AL amyloidosis: pseudotumoral aspect with particular thickening well visible at the right shoulder. P. M’Bappé, G. Grateau / Best Practice & Research Clinical Rheumatology 26 (2012) 459–475 465”
Background
Cutis laxa in hereditary gelsolin amyloidosis
Kiuru-Enari, S. M., Keski-oja, J., & Haltia, M. (2005) · British Journal of Dermatology · doi:10.1111/j.1365-2133.2004.06276.x · Cited by 58
The relation of proteoglycans, serum amyloid P and Apo E to amyloidosis current status, 2000
Kisilevsky, R. (2000) · Amyloid · doi:10.3109/13506120009146820 · Cited by 64
Etanercept can induce resolution of renal deterioration in patients with amyloid A amyloidosis secondary to rheumatoid arthritis
Nakamura, T., Higashi, S.-I., Tomoda, K., Tsukano, M., & Shono, M. (2010) · Clinical Rheumatology · doi:10.1007/s10067-010-1469-4 · Cited by 56
FcγRI mediates serum amyloid P inhibition of fibrocyte differentiation
Crawford, J. R., Pilling, D., & Gomer, R. H. (2012) · Journal of Leukocyte Biology · doi:10.1189/jlb.0112033 · Cited by 52
“tic and autoimmune material [24, 28].”
Background
A putative role for cathepsin K in degradation of AA and AL amyloidosis.
Röcken, C., Stix, B., Brömme, D., Ansorge, S., Roessner, A., & Bühling, F. (2001) · American Journal of Pathology · doi:10.1016/s0002-9440(10)64050-3 · Cited by 53
“Amyloid P component is probably a structural constituent of amyloid fibrils and present in the deposits of every amyloid disease studied so far.(45) The deposition of amyloid is not irreversible.”
Background
New insights into the role of serum amyloid P component, a novel lipopolysaccharide-binding protein.
de Haas, C. D. (1999) · FEMS Immunology & Medical Microbiology · doi:10.1111/j.1574-695x.1999.tb01390.x · Cited by 46
“These 'long' pentraxins with molecular masses around 40^ 50 kDa include PTX3 or TSG-14, a cytokine-inducible human protein of endothelial cells, ¢broblast, hepatocytes and mononuclear phagocytes; neuronal activity-regulated pentraxin (NARP), a neuronal pentraxin which is dynamically regulated by neuronal activity prom…”
Background
C-reactive protein is essential for innate resistance to pneumococcal infection
Simons, J., Loeffler, J. M., Al-Shawi, R., Ellmerich, S., Hutchinson, W., Tennent, G., Petrie, A., Raynes, J., de Souza, J. D., Lawrence, R., et al. (2014) · Immunology · doi:10.1111/imm.12266 · Cited by 45
Self-citation
Emerging treatment approaches for the systemic amyloidoses.
Dember, L. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00535.x · Cited by 45
“In addition, all types of amyloid deposits, irrespective of the fibril type, contain constituents including serum amyloid P (SAP) protein, heparan sulfate proteoglycan, apolipoprotein E, laminin, and type IV collagen [29, 30].”
Background
Serum Amyloid P Component as a Biomarker in Mild Cognitive Impairment and Alzheimer’s Disease
Verwey, N. A., Schuitemaker, A., van der Flier, W. M., Mulder, S. D., Mulder, C., Hack, C. E., Scheltens, P., Blankenstein, M. A., & Veerhuis, R. (2008) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000178756 · Cited by 37
Differentiation of Circulating Monocytes into Fibroblast-Like Cells
Pilling, D., & Gomer, R. (2012) · Methods in molecular biology · doi:10.1007/978-1-61779-943-3_16 · Cited by 43
“SAP is very stable in its 130 kDa pentameric form and only dissociates into its individual 27 kDa protomers when exposed to temperatures above 100°C in the presence of SDS (44, 45).”
Background
S100A6 Amyloid Fibril Formation Is Calcium-modulated and Enhances Superoxide Dismutase-1 (SOD1) Aggregation
Botelho, H. M., Leal, S. S., Cardoso, I., Yanamandra, K., Morozova‐Roche, L. A., Fritz, G., & Gomes, C. M. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.396416 · Cited by 46
Congo Red Staining of Amyloid: Improvements and Practical Guide for a More Precise Diagnosis of Amyloid and the Different Amyloidoses
Linke, R. (2006) · Springer eBooks · doi:10.1007/0-387-25919-8_12 · Cited by 42
“These and other data instigated examination for the substances consistently associated with the amyloid fi bril such as the “acid mucopolysaccarides,” the amyloid-P component, and ApoE (Snow et al., 1987; Strittmacher and Roses, 1996; Kisilevsky and Fraser, 1997; Pepys et al., 1997; Kisilevsky, 2000), which has now be…”
BackgroundMethod
Anti-serum amyloid component P antibodies in patients with systemic lupus erythematosus correlate with disease activity
Zandman-Goddard, G., Blank, M., Langevitz, P., Slutsky, L., Pras, M., Levy, Y., Shovman, O., Witte, T., Doria, A., Rovensky, J., et al. (2005) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2005.035832 · Cited by 41
Transient Expression in HEK 293 Cells: An Alternative to E. coli for the Production of Secreted and Intracellular Mammalian Proteins
Nettleship, J. E., Watson, P. J., Rahman-Huq, N., Fairall, L., Posner, M. G., Upadhyay, A., Reddivari, Y., Chamberlain, J. M. G., Kolstoe, S. E., Bagby, S., et al. (2014) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_11 · Cited by 42
“SAP is a plasma glycoprotein (9) which participates in the innate human immune system but also plays a role in the molecular pathology of diseases such as amyloidosis and amyloid associated diseases such as Alzheimer’s and Type II diabetes (10).”
Background
2A4 binds soluble and insoluble light chain aggregates from AL amyloidosis patients and promotes clearance of amyloid deposits by phagocytosis
Renz, M., Torres, R., Dolan, P., Tam, S. J., Tapia, J. R., Li, L., Salmans, J., Barbour, R., Shughrue, P., Nijjar, T., et al. (2016) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2016.1205974 · Cited by 38
“As expected because of its ubiquitous presence in amyloid deposits [22], serum amyloid-P protein (SAP) was detected by LCM-MS in all the samples tested.”
Background
Isolation and characterization of pharmaceutical grade human pentraxins, serum amyloid P component and C‐reactive protein, for clinical use
Pepys, M. B., Gallimore, J. R., Lloyd, J., Li, Z., Graham, D., Taylor, G. W., Ellmerich, S., Mangione, P. P., Tennent, G. A., Hutchinson, W. L., et al. (2012) · Journal of Immunological Methods · doi:10.1016/j.jim.2012.07.013 · Cited by 37
Self-citation
Bacillus anthracis Poly-γ-D-Glutamate Capsule Inhibits Opsonic Phagocytosis by Impeding Complement Activation
Sharma, S., Bhatnagar, R., & Gaur, D. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00462 · Cited by 37
“MA5-17061) and mouse antihuman SAP monoclonal antibodies (Thermo Fisher, Cat.”
MethodInfluential
Drug Insight: emerging therapies for amyloidosis
Gillmore, J. D., & Hawkins, P. N. (2006) · Nature Reviews Nephrology · doi:10.1038/ncpneph0169 · Cited by 40
Structural basis of ligand specificity in the human pentraxins, C‐reactive protein and serum amyloid P component
Mikolajek, H., Kolstoe, S. E., Pye, V. E., Mangione, P. P., Pepys, M. B., & Wood, S. P. (2011) · Journal of Molecular Recognition · doi:10.1002/jmr.1090 · Cited by 42
“The aggregation, which has also confused much other experimental work on interactions of human SAP (Pepys et al., 1997), results from cross-linking mediated by binding of the projecting side chain carboxylate of the A face helix residue Glu167 on one SAP molecule in the calcium dependent ligand…”
BackgroundSelf-citation
The structures of crystalline complexes of human serum amyloid P component with its carbohydrate ligand, the cyclic pyruvate acetal of galactose.
Thompson, D., Pepys, M., Tickle, I., & Wood, S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00514-4 · Cited by 35
Self-citation
Micro-imaging of amyloid in mice.
Wall, J., Paulus, M., Gleason, S., Gregor, J., Solomon, A., & Kennel, S. (2006) · Methods in Enzymology · doi:10.1016/s0076-6879(06)12011-x · Cited by 35
“Within the last two decades however, advances in clinical medical practices have made possible, by whole body scintigraphic examination [planar 2-D imaging of a bodily radiation source], the detection of amyloid deposits in patients using radioiodinated serum amyloid P-component (SAP) (Hawkins et al., 1988a; Hawkins e…”
Background
Systemic Amyloidosis: a Contemporary Overview
D'Aguanno, V., Ralli, M., Artico, M., Russo, F., Scarpa, A., Fiore, M., Tirassa, P., Severini, C., de Vincentiis, M., & Greco, A. (2019) · Clinical reviews in allergy and immunology · doi:10.1007/s12016-019-08759-4 · Cited by 33
Structural Basis for the Recognition and Cross-linking of Amyloid Fibrils by Human Apolipoprotein E
Gunzburg, M. J., Perugini, M. A., & Howlett, G. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706425200 · Cited by 28
Molecular mechanisms and emerging therapies in wild-type transthyretin amyloid cardiomyopathy
Wu, D., & Chen, W. (2024) · Heart Failure Reviews · doi:10.1007/s10741-023-10380-9 · Cited by 37
“TTR amyloid deposits contain serum amyloid P (SAP), proteoglycans [41], and clusterin [42], which is also present in other types of amyloid deposits [43].”
Background
Brain Serum Amyloid P Levels are Reduced in Individuals that Lack Dementia While Having Alzheimer’s Disease Neuropathology
Crawford, J. R., Bjorklund, N. L., Taglialatela, G., & Gomer, R. H. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0674-0 · Cited by 28
“SAP is a pattern recognition protein that binds components of pathogens as well as apoptotic and autoimmune material [12,13].”
Background
SAP Suppresses the Development of Experimental Autoimmune Encephalomyelitis in C57BL6 Mice
Ji, Z., Ke, Z.-J., & Geng, J. (2011) · Immunology and Cell Biology · doi:10.1038/icb.2011.51 · Cited by 29
A Quantitative Proteomic Approach to Prion Disease Biomarker Research: Delving into the Glycoproteome
Wei, X. L., Herbst, A. J., Ma, D., Aiken, J. M., & Li, L. (2011) · Journal of Proteome Research · doi:10.1021/pr2000495 · Cited by 29
Ligand-assisted Aggregation of Proteins
Ho, J., Kitov, P., Paszkiewicz, E., Sadowska, J., Bundle, D., & Ng, K. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504403200 · Cited by 29
Complete cDNA sequence of SAP-like pentraxin from Limulus polyphemus: implications for pentraxin evolution.
Tharia, H., Shrive, A., Mills, J. D., Arme, C., Williams, G., & Greenhough, T. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5356 · Cited by 29
Immunohistochemical characterization of novel monoclonal antibodies against the N-terminus of amyloid β-peptide
Verwey, N. A., Hoozemans, J. J. M., Korth, C., van Royen, M. R., Prikulis, I., Wouters, D., Twaalfhoven, H. A. M., van Haastert, E. S., Schenk, D., Scheltens, P., et al. (2013) · Amyloid · doi:10.3109/13506129.2013.797389 · Cited by 21
Quantitative high-resolution microradiographic imaging of amyloid deposits in a novel murine model of AA amyloidosis
Wall, J., Kennel, S., Paulus, M., Gleason, S., Gregor, J., Baba, J., Schell, M., Richey, T., O'Nuallain, B., Donnell, R., et al. (2005) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506120500222359 · Cited by 28
“This molecule, a member of the pentraxin family, had been chosen for this purpose because it is invariably associated with all types of amyloid deposits, regardless of their chemical nature, and it binds specifically and with high affinity to fibrils [29].”
Background
Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro
Ozawa, D., Nomura, R., Mangione, P. P., Hasegawa, K., Okoshi, T., Porcari, R., Bellotti, V., & Naiki, H. (2016) · Scientific Reports · doi:10.1038/srep29077 · Cited by 25
Pharmacological removal of serum amyloid P component from intracerebral plaques and cerebrovascular Aβ amyloid deposits in vivo
Al-Shawi, R., Tennent, G. A., Millar, D. J., Richard-Londt, A., Brandner, S., Werring, D. J., Simons, J. P., & Pepys, M. B. (2016) · Open Biology · doi:10.1098/rsob.150202 · Cited by 26
Self-citation
The amyloid proteome: a systematic review and proposal of a protein classification system
Gottwald, J., & Röcken, C. (2021) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409238.2021.1937926 · Cited by 26
Serum amyloid P component induces neuronal apoptosis and beta-amyloid immunoreactivity.
Urbányi, Z., Laszlo, L., Tomasi, T., Tóth, E., Mekes, É., Sass, M., & Pázmány, T. (2003) · Brain Research · doi:10.1016/s0006-8993(03)03345-6 · Cited by 26
Extension of Aβ2M amyloid fibrils with recombinant human β2-microglobulin
Yamaguchi, I., Hasegawa, K., Naiki, H., Mitsu, T., Matuo, Y., & Gejyo, F. (2001) · doi:10.3109/13506120108993812 · Cited by 26
The complement regulator C4b-binding protein analyzed by molecular modeling, bioinformatics and computer-aided experimental design.
Villoutreix, B., Blom, A., Webb, J., & Dahlbäck, B. (1999) · Immunopharmacology · doi:10.1016/s0162-3109(99)00022-3 · Cited by 26
Serum amyloid P component induces TUNEL-positive nuclei in rat brain after intrahippocampal administration
Urbányi, Z., Sass, M., Laszy, J., Takács, V., Gyertyán, I., & Pázmány, T. (2007) · Brain Research · doi:10.1016/j.brainres.2007.01.132 · Cited by 22
Cross-interactions between the Alzheimer disease amyloid-β peptide and other amyloid proteins. A FURTHER ASPECT OF THE AMYLOID CASCADE HYPOTHESIS.
Luo, J., Wärmländer, S., Gräslund, A., & Abrahams, J. (2017) · Journal of Biological Chemistry · doi:10.1074/jbc.a116.714576 · Cited by 24
“In vivo, human amyloid deposits often contain SAP together with a primary amyloid component such as A (74).”
Background
Light Chain Stabilization: A Therapeutic Approach to Ameliorate AL Amyloidosis
Morgan, G., Buxbaum, J., & Kelly, J. (2021) · Hemato · doi:10.3390/hemato2040042 · Cited by 23
Mice Lacking Serum Amyloid P Component Do Not Necessarily Develop Severe Autoimmune Disease
相馬, 真., Tamaoki, T., Kawano, H., Ito, S., Sakamoto, M., Okada, Y., Ozaki, Y., Kanba, S., Hamada, Y., Ishihara, T., et al. (2001) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2001.5364 · Cited by 21
A serum amyloid P‐binding hydrogel speeds healing of partial thickness wounds in pigs
Gomer, R. H., Pilling, D., Kauvar, L. M., Ellsworth, S. L., Ronkainen, S. D., Roife, D., & Davis, S. C. (2009) · Wound Repair and Regeneration · doi:10.1111/j.1524-475x.2009.00482.x · Cited by 20
Preferential association of serum amyloid P component with fibrillar deposits in familial British and Danish dementias: Similarities with Alzheimer's disease
Rostagno, A. A., Lashley, T., Ng, D., Meyerson, J. L., Brændgaard, H., Plant, G. T., Bojsen‐Møller, M., Holton, J. L., Frangione, B., Révész, T., et al. (2007) · Journal of the Neurological Sciences · doi:10.1016/j.jns.2007.01.050 · Cited by 22
In vitrobinding of [3H]PIB to human amyloid deposits of different types
Hellström‐Lindahl, E., Westermark, P., Antoni, G., & Estrada, S. (2013) · Amyloid · doi:10.3109/13506129.2013.860895 · Cited by 23
Target Mediated Drug Disposition Model of CPHPC in Patients with Systemic Amyloidosis
Sahota, T., Berges, A., Barton, S., Cookson, L., Zamuner, S., & Richards, D. (2015) · CPT: Pharmacometrics & Systems Pharmacology · doi:10.1002/psp4.15 · Cited by 19
“The model-based simulations illustrated in Figure 5 clearly show the impact of the selected covariates on predicted plasma profiles of CPHPC and SAP.”
BackgroundInfluential
Spontaneous, Experimentally Induced, and Transmissible AA Amyloidosis in Japanese Quail (Coturnix japonica)
Nakayama, Y., Kamiie, J., Watanabe, G., Suzuki, K., & Murakami, T. (2017) · Veterinary Pathology-Supplement · doi:10.1177/0300985817723692 · Cited by 18
“SAA is usually detected in AA deposits as a conjugated protein.(23) The anti-chicken SAA antiserum used in this study has previously been shown to react positively with amyloid deposits in chickens.”
Background
Drug targets for amyloidosis.
Kolstoe, S., & Wood, S. (2010) · Biochemical Society Transactions · doi:10.1042/bst0380466 · Cited by 18
Insoluble Proteins
García-Fruitós, E. (2015) · Methods in Molecular Biology · doi:10.1007/978-1-4939-2205-5 · Cited by 18
The Process of Amyloid Formation due to Monoclonal Immunoglobulins
Morgan, G. J., & Wall, J. S. (2020) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2020.07.003 · Cited by 19
Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis
Kumar, S., Song, K., Wang, J., Baghel, M. S., Zeng, Y., Shen, K., Zheng, J., Crane, J., Demehri, S., Gao, P., et al. (2025) · Nature Aging · doi:10.1038/s43587-025-00924-z · Cited by 16
“It has been well established that SAP is universally present in all human amyloid deposits 68,84 .”
Characterization and Stabilization of Recombinant Human Protein Pentraxin (rhPTX-2)
Liu, J., Blasie, C. A., Shi, S., Joshi, S. B., Middaugh, C. R., & Volkin, D. B. (2012) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.23360 · Cited by 15

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.
ORCID: Pepys, M B.
Booth, D. R.
Hohenester, E.
Venue: Amyloid
Publisher: Informa UK Limited
Published: 1997-01
Volume: 4
Issue: 4
Pages: 274-295
ISSN: 1350-6129 (ISSN-L)
1744-2818
DOI: 10.3109/13506129709003838
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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