Amyloid P component. A critical review
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CPHPC (miridesap) at a concentration of 5 mg ml−1 in drinking water is an established dose for SAP depletion from the body.
“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]
SAP is universally present in all human amyloid deposits.
“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]
Cites
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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 · see citing works
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 · see citing works
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Molecular Mechanisms of Amyloidosis
Merlini, G., & Bellotti, V. (2003) · New England Journal of Medicine · doi:10.1056/nejmra023144 · Cited by 1,927 · see citing works
Review: history of the amyloid fibril.
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“CRP is a member of the evolutionarily ancient and stably conserved pentraxin family that includes serum amyloid P component (SAP) [3], an important constituent of the amyloid deposits that underlie a range of human diseases including Alzheimer’s [4,5].”
BackgroundSelf-citationIslet Amyloid: A Critical Entity in the Pathogenesis of Type 2 Diabetes
Hull, R. L., Westermark, G. T., Westermark, P., & Kahn, S. E. (2004) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.2004-0405 · Cited by 580 · see citing works
Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity
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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 · see citing works
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Therapeutic Clearance of Amyloid by Antibodies to Serum Amyloid P Component.
Richards, D. B., Cookson, L., Berges, A., Barton, S. V., Lane, T., Ritter, J., Fontana, M., Moon, J., Pinzani, M., Gillmore, J., et al. (2015) · New England Journal of Medicine · doi:10.1056/nejmoa1504942 · Cited by 342 · see citing works
Self-citationInhibition of Fibrocyte Differentiation by Serum Amyloid P 1
Pilling, D., Buckley, C., Salmon, M., & Gomer, R. (2003) · Journal of Immunology · doi:10.4049/jimmunol.171.10.5537 · Cited by 331 · see citing works
Antibodies to human serum amyloid P component eliminate visceral amyloid deposits
Bodin, K., Ellmerich, S., Kahan, M., Tennent, G. A., Loesch, A., Gilbertson, J. A., Hutchinson, W. L., Mangione, P. P., Gallimore, J. R., Millar, D. J., et al. (2010) · Nature · doi:10.1038/nature09494 · Cited by 336 · see citing works
“Serum amyloid P component (SAP) is selectively concentrated in amyloid deposits by its avid binding to all amyloid fibril types 2 , 3 .”
Self-citationPivotal Advance: Th‐1 cytokines inhibit, and Th‐2 cytokines promote fibrocyte differentiation
Shao, D., Suresh, R., Vakil, V., Gomer, R., & Pilling, D. (2008) · Journal of Leukocyte Biology · doi:10.1189/jlb.1107782 · Cited by 288 · see citing works
“Immunohistochemical staining of SAP has shown that SAP is associated with extracellular tissues, especially reticulin and elastic fibers, found in kidney, skin, and blood vessels, but whether SAP, once bound to ECM, is still biologically active is unclear, and the actual concentration of biologically active SAP presen…”
BackgroundC-reactive protein and cardiovascular disease: new insights from an old molecule
Hirschfield, G. M., & Pepys, M. B. (2003) · QJM · doi:10.1093/qjmed/hcg134 · Cited by 249 · see citing works
Self-citationAmyloid 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 · see citing works
Self-citationAmyloidosis: a convoluted story
Kyle, R. (2001) · British Journal of Haematology · doi:10.1046/j.1365-2141.2001.02999.x · Cited by 239 · see citing works
“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 · see citing works
Self-citationPathology, diagnosis and pathogenesis of AA amyloidosis
Röcken, C., & Shakespeare, A. (2002) · Virchows Archiv · doi:10.1007/s00428-001-0582-9 · Cited by 213 · see citing works
Bellotti, V., Mangione, P., & Merlini, G. (2000) · Journal of Structural Biology · doi:10.1006/jsbi.2000.4248 · Cited by 198 · see citing works
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 201 · see citing works
“amyloid P component (SAP), apolipoprotein E (apoE), and the heparan sulfate proteoglycan (HSPG) perlecan [49–52].”
BackgroundHazenberg, 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
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 · see citing works
“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-citationGillmore, 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-citationSensitive 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.”
BackgroundBellotti, 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 · see citing works
“Amyloid P, derived from serum amyloid P, is frequently observed in association with amyloid deposits in vivo [55].”
BackgroundExtrahepatic 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
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Self-citationAggregated IgG inhibits the differentiation of human fibrocytes
Pilling, D., Tucker, N. M., & Gomer, R. (2006) · Journal of Leukocyte Biology · doi:10.1189/jlb.0805456 · Cited by 116 · see citing works
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 · see citing works
“In vivo, human amyloid deposits often contain SAP together with a primary amyloid component such as A (74).”
BackgroundBiological activity and pathological implications of misfolded proteins
Bellotti, V., Mangione, P., & Stoppini, M. (1999) · Cellular and Molecular Life Sciences (CMLS) · doi:10.1007/s000180050348 · Cited by 114 · see citing works
Pathophysiology and treatment of systemic amyloidosis
Gillmore, J., & Hawkins, P. (2013) · Nature Reviews Nephrology · doi:10.1038/nrneph.2013.171 · Cited by 113 · see citing works
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 · see citing works
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 · see citing works
Self-citationBourgault, S., Solomon, J. P., Reixach, N., & Kelly, J. (2011) · Biochemistry · doi:10.1021/bi101822y · Cited by 102 · see citing works
“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.”
BackgroundRamirez-Alvarado, M., Kelly, J. W., & Dobson, C. M. (2010) · Wiley eBooks · doi:10.1002/9780470572702 · Cited by 79 · see citing works
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 · see citing works
“SAP is made by hepatocytes and secreted into the blood (1, 2).”
BackgroundMollee, P., Renaut, P., Gottlieb, D., & Goodman, H. (2014) · Internal medicine journal (Print) · doi:10.1111/imj.12288 · Cited by 88
The beta-slip: a novel concept in transthyretin amyloidosis.
Eneqvist, T., Andersson, K., Olofsson, A., Lundgren, E., & Sauer-Eriksson, A. (2000) · Molecules and Cells · doi:10.1016/s1097-2765(00)00117-9 · Cited by 88 · see citing works
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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.”
BackgroundMethodLachmann, 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”
BackgroundMolecular 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 · see citing works
“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-citationGillmore, 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 · see citing works
Self-citationImmunotherapy 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 · see citing works
“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 · see citing works
“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-citationHazenberg, 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).”
BackgroundApolipoproteins 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 · see citing works
“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).”
BackgroundArmstrong, 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 · see citing works
“have been strictly calcium dependent [14], but we found avid”
BackgroundSelf-citationOsteo-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”
BackgroundCutis 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 · see citing works
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 51 · see citing works
“tic and autoimmune material [24, 28].”
BackgroundA 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.”
BackgroundNew 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 · see citing works
“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…”
BackgroundC-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 · see citing works
Self-citationEmerging treatment approaches for the systemic amyloidoses.
Dember, L. (2005) · Kidney International · doi:10.1111/j.1523-1755.2005.00535.x · Cited by 45 · see citing works
“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].”
BackgroundSerum Amyloid P Component as a Biomarker in Mild Cognitive Impairment and Alzheimer’s Disease
Verwey, N., Schuitemaker, A., van der Flier, W. M., Mulder, S., Mulder, C., Hack, C., Scheltens, P., Blankenstein, M., & Veerhuis, R. (2008) · Dementia and Geriatric Cognitive Disorders · doi:10.1159/000178756 · Cited by 43 · see citing works
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 · see citing works
“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).”
BackgroundBotelho, 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 43 · see citing works
Linke, R. (2006) · Springer eBooks · doi:10.1007/0-387-25919-8_12 · Cited by 42 · see citing works
“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…”
BackgroundMethodZandman-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
Nettleship, J., Watson, P., Rahman-Huq, N., Fairall, L., Posner, M., Upadhyay, A., Reddivari, Y., Chamberlain, J., Kolstoe, S., Bagby, S., et al. (2015) · Methods in molecular biology · doi:10.1007/978-1-4939-2205-5_11 · Cited by 41 · see citing works
“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).”
BackgroundRenz, 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.”
BackgroundPepys, M., Gallimore, J., Lloyd, J., Li, Z., Graham, D., Taylor, G., Ellmerich, S., Mangione, P., Tennent, G., Hutchinson, W., et al. (2012) · JIM - Journal of Immunological Methods · doi:10.1016/j.jim.2012.07.013 · Cited by 38 · see citing works
Self-citationSharma, S., Bhatnagar, R., & Gaur, D. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00462 · Cited by 37 · see citing works
“MA5-17061) and mouse antihuman SAP monoclonal antibodies (Thermo Fisher, Cat.”
MethodInfluentialDrug Insight: emerging therapies for amyloidosis
Gillmore, J. D., & Hawkins, P. N. (2006) · Nature Reviews Nephrology · doi:10.1038/ncpneph0169 · Cited by 40 · see citing works
Mikolajek, H., Kolstoe, S., Pye, V. E., Mangione, P., Pepys, M., & Wood, S. P. (2011) · Journal of Molecular Recognition · doi:10.1002/jmr.1090 · Cited by 36 · see citing works
“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-citationThompson, D., Pepys, M., Tickle, I., & Wood, S. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00514-4 · Cited by 35 · see citing works
Self-citationMicro-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 · see citing works
“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…”
BackgroundSystemic 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 · see citing works
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 34 · see citing works
“TTR amyloid deposits contain serum amyloid P (SAP), proteoglycans [41], and clusterin [42], which is also present in other types of amyloid deposits [43].”
BackgroundCrawford, J. R., Bjorklund, N. L., Taglialatela, G., & Gomer, R. H. (2011) · Neurochemical Research · doi:10.1007/s11064-011-0674-0 · Cited by 28 · see citing works
“SAP is a pattern recognition protein that binds components of pathogens as well as apoptotic and autoimmune material [12,13].”
BackgroundSAP 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 · see citing works
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 · see citing works
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 · see citing works
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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 · see citing works
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“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].”
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Self-citationThe amyloid proteome: a systematic review and proposal of a protein classification system
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Serum amyloid P component induces neuronal apoptosis and beta-amyloid immunoreactivity.
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“In vivo, human amyloid deposits often contain SAP together with a primary amyloid component such as A (74).”
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“The model-based simulations illustrated in Figure 5 clearly show the impact of the selected covariates on predicted plasma profiles of CPHPC and SAP.”
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“It has been well established that SAP is universally present in all human amyloid deposits 68,84 .”
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- 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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