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Repeat doses of antibody to serum amyloid P component clear amyloid deposits in patients with systemic amyloidosis
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Repeat cycles of miridesap, to deplete circulating serum amyloid P component (SAP), followed by the anti-SAP antibody, dezamizumab, cleared visceral amyloid deposits in patients with systemic amyloidosis.
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“Our data demonstrated that CPHPC (miridesap), developed by Pepys’ team at University College London90–92, efficiently reduces SAP concentration in serum (58.5% reduction) and bone marrow (95% reduction) in aged mice.”
From Serum amyloid P secreted by bone marrow adipocytes drives skeletal amyloidosis (2025) · cites this paper as [91]
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Moon, J., Messroghli, D., Kellman, P., Piechnik, S. K., Robson, M. D., Ugander, M., Gatehouse, P. D., Arai, A. E., Friedrich, M. G., Neubauer, S., et al. (2013) · Journal of Cardiovascular Magnetic Resonance · doi:10.1186/1532-429x-15-92 · Cited by 1,140
Self-citationComplement Is Activated by IgG Hexamers Assembled at the Cell Surface
Diebolder, C. A., Beurskens, F. J. M., de Jong, R. N., Koning, R. I., Strumane, K., Lindorfer, M. A., Voorhorst, M., Ugurlar, D., Rosati, S., Heck, A. J. R., et al. (2014) · Science · doi:10.1126/science.1248943 · Cited by 797
Pepys, M. B. (2005) · Annual Review of Medicine · doi:10.1146/annurev.med.57.121304.131243 · Cited by 566
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
Self-citationTherapeutic 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
Self-citationQuantification of Myocardial Extracellular Volume Fraction in Systemic AL Amyloidosis
Banypersad, S. M., Sado, D. M., Flett, A. S., et al. (2012) · Circulation Cardiovascular Imaging · doi:10.1161/circimaging.112.978627 · Cited by 337
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
Self-citationHuman plasma fibrinogen is synthesized in the liver
Tennent, G. A., Brennan, S. O., Stangou, A. J., O'Grady, J., Hawkins, P. N., & Pepys, M. B. (2007) · Blood · doi:10.1182/blood-2006-08-040956 · Cited by 304
Self-citationAmyloid 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 · Cited by 181 · cited 1×
“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-citationMilde, R., Ritter, J. M., Tennent, G. A., Loesch, A., Martínez, F. O., Gordon, S., Pepys, M. B., Verschoor, A., & Helming, L. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.10.065 · Cited by 162
Self-citation
Research works printed but not linked: 5
- M. A. Gertz, H. J. Landau, B. M. Weiss, Organ response in patients with AL amyloidosis treated with NEOD001, an amyloid-directed monoclonal antibody. Am. J. Hematol. 91, E506–E508 (2016). · DOI
- V. Loustaud-Ratti, A. Cypierre, A. Rousseau, F. Yagoubi, J. Abraham, A.-L. Fauchais, P. Carrier, A. Lefebvre, D. Bordessoule, E. Vidal, D. Sautereau, A. Jaccard, Non-invasive detection of hepatic amyloidosis: FibroScan, a new tool. Amyloid 18, 19–24 (2011). · DOI
- P. N. Hawkins, J. P. Lavender, M. B. Pepys, Evaluation of systemic amyloidosis by scintigraphy with 123I-labeled serum amyloid P component. N. Engl. J. Med. 323, 508–513 (1990). · DOI
- D. F. Hutt, T. Lane, J. D. Gillmore, H. J. Lachmann, S. D. J. Gibbs, P. T. Sattianayagam, D. Gopaul, A. M. Quigley, P. N. Hawkins, A. D. Wechalekar, Role of dual modality I123 serum amyloid P component SPECT-CT imaging in amyloidosis. Amyloid 17 (suppl. 1), 57 (2010).
- D. F. Hutt, A.-M. Quigley, J. Page, M. L. Hall, M. Burniston, D. Gopaul, T. Lane, C. J. Whelan, H. J. Lachmann, J. D. Gillmore, P. N. Hawkins, A. D. Wechalekar, Utility and limitations of 3,3-diphosphono-1,2-propanodicarboxylic acid scintigraphy in systemic amyloidosis. Eur. Heart J. Cardiovasc. Imaging 15, 1289–1298 (2014). · DOI
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Emdin, M., Aimo, A., Rapezzi, C., Fontana, M., Perfetto, F., Seferovic, P. M., Barison, A., Castiglione, V., Vergaro, G., Giannoni, A., et al. (2019) · European Heart Journal · doi:10.1093/eurheartj/ehz298 · Cited by 155
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“ing with SAP scans and decreased liver stiffness as measured with the use of elastography NCT01777243.(152,153) An antibody to a cryptic”
MethodCardiac amyloidosis: the need for early diagnosis
Oerlemans, M., Rutten, K. H. G., Minnema, M., Raymakers, R., Asselbergs, F., & de Jonge, N. (2019) · Netherlands Heart Journal · doi:10.1007/s12471-019-1299-1 · Cited by 112
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Manganelli, F., Fabrizi, G. M., Luigetti, M., Mandich, P., Mazzeo, A. T., & Pareyson, D. (2020) · Neurological Sciences · doi:10.1007/s10072-020-04889-2 · Cited by 134
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Pilling, D., & Gomer, R. H. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02328 · Cited by 92
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Self-citationda Silva, D. M., Langer, H. F., & Graf, T. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20092322 · Cited by 108
Michalon, A., Hagenbuch, A., Huy, C., Varela, E., Combaluzier, B., Damy, T., Suhr, O. B., Saraiva, M. J., Höck, C., Nitsch, R. M., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-23274-x · Cited by 101
Emerging Therapies in Transthyretin Amyloidosis – A New Wave of Hope After Years of Stagnancy?
Müller, M. L., Butler, J., & Heidecker, B. (2020) · European Journal of Heart Failure · doi:10.1002/ejhf.1695 · Cited by 74
The Basic Characteristics of the Pentraxin Family and Their Functions in Tumor Progression
Wang, Z., Wang, X., Zou, H., Dai, Z., Feng, S., Zhang, M., Xiao, G., Liu, Z., & Cheng, Q. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01757 · Cited by 73
Use of biomarkers to diagnose and manage cardiac amyloidosis
Castiglione, V., Franzini, M., Aimo, A., Carecci, A., Lombardi, C., Passino, C., Rapezzi, C., Emdin, M., & Vergaro, G. (2021) · European Journal of Heart Failure · doi:10.1002/ejhf.2113 · Cited by 84
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Witteles, R., & Liedtke, M. (2019) · JACC CardioOncology · doi:10.1016/j.jaccao.2019.08.002 · Cited by 68
“The same group later included 6 cardiac patients in a follow-up study (81), but clear efficacy data for this approach in cardiac amyloidosis have yet to be demonstrated.”
BackgroundThe Pentraxins 1975–2018: Serendipity, Diagnostics and Drugs
Pepys, M. B. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02382 · Cited by 67
“Indeed abnormal liver function tests returned toward normal in all patients as their amyloid load was reduced (115, 116).”
BackgroundSelf-citationExtracellular protein homeostasis in neurodegenerative diseases
Wilson, M. R., Satapathy, S., & Vendruscolo, M. (2023) · Nature Reviews Neurology · doi:10.1038/s41582-023-00786-2 · Cited by 43
Renal Manifestations of Inflammatory Bowel Disease.
Ambruzs, J. M., & Larsen, C. P. (2018) · Rheumatic Disease Clinics of North America · doi:10.1016/j.rdc.2018.06.007 · Cited by 58
van den Berg, M. P., Mulder, B. A., Klaassen, S. H. C., Maass, A. H., van Veldhuisen, D. J., van der Meer, P., Nienhuis, H. L. A., Hazenberg, B. P. C., & Rienstra, M. (2019) · European Heart Journal · doi:10.1093/eurheartj/ehz057 · Cited by 63
“Initial results with these removers in patients with systemic amyloidosis with liver, spleen and kidney involvement are promising.(38,39) Of note, although there is currently no treatment for IAA, theoretically treatment with anti-SAP antibodies might work in”
BackgroundAA Amyloidosis: A Contemporary View
Mirioğlu, Ş., Uludağ, Ö., Hürdoğan, Ö., Kumru, G., Berke, İ., Doumas, S., Frangou, E. A., & Gül, A. (2024) · Current Rheumatology Reports · doi:10.1007/s11926-024-01147-8 · Cited by 53
“Miridesap , a serum SAP inhibitor, was initially investigated in a mixed amyloidosis population, followed by subsequent trials where it was administered in tandem with dezamizumab, a monoclonal antibody targeting SAP tissue depositions [98, 99 • , 100].”
ResultRenal AA amyloidosis: presentation, diagnosis, and current therapeutic options: a review.
Karam, S., Haidous, M., Royal, V., & Leung, N. (2022) · Kidney International · doi:10.1016/j.kint.2022.10.028 · Cited by 45
Schönfelder, J., Pfeiffer, P., Pradhan, T., Bijzet, J., Hazenberg, B., Schönland, S., Hegenbart, U., Reif, B., Haupt, C., & Fändrich, M. (2021) · bioRxiv · doi:10.1080/13506129.2021.1960501 · Cited by 45
“The second one is associated with the fact that ex vivo amyloid fibrils can contain non-fibril components of amyloid tissue deposits, such as SAP, which was previously found to protect amyloid fibrils from being degraded in vitro [33] and in vivo [32].”
BackgroundSerum amyloid P component is an essential element of resistance against Aspergillus fumigatus
Doni, A., Parente, R., Laface, I., Magrini, E. I., Cunha, C., Colombo, F., de Lacerda, J. F., Campos, A., Mapelli, S. N., Petroni, F., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24021-y · Cited by 68
Therapies for cardiac light chain amyloidosis: An update.
Aimo, A., Buda, G., Fontana, M., Barison, A., Vergaro, G., Emdin, M., & Merlini, G. (2018) · International Journal of Cardiology · doi:10.1016/j.ijcard.2018.05.018 · Cited by 40
Self-citationTargeting Amyloid Fibrils by Passive Immunotherapy in Systemic Amyloidosis
Nuvolone, M., Nevone, A., & Merlini, G. (2022) · BioDrugs · doi:10.1007/s40259-022-00550-w · Cited by 38
“However, no systematic change in left ventricular mass by cardiac MRI, or change in cardiac uptake at 3,3-diphosphono-1,2-propanodicarboxylic acid (DPD) scintigraphy (for the three ATTR cases) was documented [33].”
BackgroundDohrn, M. F., Ihne-Schubert, S. M., Hegenbart, U., Medina, J., Zuchner, S. L., Coelho, T., & Hahn, K. (2020) · Journal of Neurochemistry · doi:10.1111/jnc.15233 · Cited by 39
“By complement activation and the induction of phagocytosis, antibodies against serum amyloid A component (SAP) aimed at triggering the elimination of systemic amyloid deposits (Bodin et al., 2010; Richards et al., 2015), which seemed to be a promising approach in a previous study including patients with different type…”
ResultHerrera, G. A., Teng, J., Turbat‐Herrera, E. A., Zeng, C., & del Pozo‐Yauner, L. (2020) · Kidney International Reports · doi:10.1016/j.ekir.2020.07.013 · Cited by 38
“1884 amyloid deposits, with a fully humanized monoclonal antibody.(192) Another approach under development is to target specifically the LC fibrils.”
BackgroundTreating Protein Misfolding Diseases: Therapeutic Successes Against Systemic Amyloidoses
Nevone, A., Merlini, G., & Nuvolone, M. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.01024 · Cited by 43
“…prion diseases and hereditary systemic amyloidoses (including ATTRv amyloidosis associated to variant transthyretin, TTR) (Connors et al., 2003; Rowczenio et al., 2019), or by mutations which increase the synthesis or the proteolytic release of the amyloid-forming protein, as in the case of AA…”
BackgroundWechalekar, A., Antoni, G., Al-Azzam, W. A., Bergström, M., Biswas, S., Chen, C.-G., Cheriyan, J., Cleveland, M., Cookson, L., Galette, P., et al. (2022) · BMC Cardiovascular Disorders · doi:10.1186/s12872-021-02407-6 · Cited by 30
“Prior evaluation of this anti-SAP treatment demonstrated amyloid removal in patients with liver, spleen and kidney involvement [13, 14], and a link was seen between reduction in hepatic amyloid load and improvement in liver function [14].”
BackgroundMethodInfluentialSelf-citationPopková, T., Hájek, R., & Jelı́nek, T. (2020) · British Journal of Haematology · doi:10.1111/bjh.16436 · Cited by 28
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“SAP depletion from serum (Pepys et al. 2002) in combination with antibody-mediated activation of the innate immune response (Richards et al. 2015) enables amyloid degradation (Richards et al. 2018).”
BackgroundManagement of the elderly patient with AL amyloidosis.
Nuvolone, M., Milani, P., Palladini, G., & Merlini, G. (2018) · European journal of internal medicine · doi:10.1016/j.ejim.2018.05.004 · Cited by 25
Larsen, C. P., Sharma, S., Caza, T. N., Kenan, D., Storey, A. J., Edmondson, R. D., Herzog, C., & Arthur, J. (2019) · Kidney International · doi:10.1016/j.kint.2019.10.026 · Cited by 23
“17,18 Additionally, the mass spectrometry results indicate that therapies targeting the complement cascade might be of utility in treating this form of glomerulonephritis, given that most of the proteins that were increased in MGMID glomeruli are complement related.”
Richey, T., Foster, J. S., Williams, A. D., Williams, A., Stroh, A., Macy, S., Wooliver, C., Heidel, R., Varanasi, S., Ergen, E., et al. (2019) · American Journal of Pathology · doi:10.1016/j.ajpath.2019.01.011 · Cited by 23
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Diteepeng, T., Monte, F., & Luciani, M. (2021) · European Journal of Clinical Investigation · doi:10.1111/eci.13504 · Cited by 22
Systemic amyloidosis: moving into the spotlight
Cohen, O. C., & Wechalekar, A. D. (2020) · Leukemia · doi:10.1038/s41375-020-0802-4 · Cited by 30
“A phase 1 trial of (R)-1-[6-[(R)-2-carboxy-pyrrolidin-1yl]-6-oxo-hexanoyl]pyrrolidine-2-carboxylic acid (CPHPC) also known as miridesap, with dezamizumab, a humanised monoclonal anti-SAP antibody, demonstrated hepatic and renal clearance with reduction of the splenic amyloid load and improved hepatic function [80].”
BackgroundSelf-citationWang, H., Nie, Y., Sun, Z., He, Y., & Yang, J. (2024) · Molecular Immunology · doi:10.1016/j.molimm.2024.05.009 · Cited by 20
Wall, J., Williams, A. D., Foster, J., Richey, T., Stuckey, A., Macy, S., Wooliver, C., Campagna, S., Tague, E. D., Farmer, A., et al. (2018) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.1805515115 · Cited by 19
“To this end, a new therapeutic paradigm has been developed for the treatment of patients with systemic amyloidosis; namely, the use of amyloid-directed passive immunotherapy using the humanized mAbs NEDO001 (12, 23, 30), dezamizumab (31), and the chimeric reagent 11-1F4 (11).”
BackgroundRenal AL Amyloidosis: Updates on Diagnosis, Staging, and Management
Shafqat, A., Elmaleh, H., Mushtaq, A., Firdous, Z., Ashruf, O. S., Mukhopadhyay, D., Ahmad, M., Ahmad, M., Raza, S., & Anwer, F. (2024) · Journal of Clinical Medicine · doi:10.3390/jcm13061744 · Cited by 18
“Dezamizumab is a monoclonal antibody that triggers the immunotherapeutic clearance of amyloid fibrils after serum amyloid P (SAP), a protein covering circulating amyloid fibrils, is depleted by miridesap (parenteral) or GSK3039294 (oral) [101,102].”
BackgroundAL amyloidosis: untangling new therapies.
Bal, S., & Landau, H. (2021) · Hematology. American Society of Hematology. Education Program · doi:10.1182/hematology.2021000305 · Cited by 18
Lin, X.-Y., Pan, D., Sang, L.-X., & Chang, B. (2021) · World Journal of Gastroenterology · doi:10.3748/wjg.v27.i12.1132 · Cited by 18
Ueda, M., Okada, M., Mizuguchi, M., Kluve-beckerman, B., Kanenawa, K., Isoguchi, A., Misumi, Y., Tasaki, M., Ueda, A., Kanai, A., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.007851 · Cited by 18
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“Amyloid load reduction was reported in the liver, spleen, and kidney following its administration in AL and ATTR systemic amyloidosis [75].”
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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
How I treat elderly patients with plasma cell dyscrasias
Gavriatopoulou, M., Fotiou, D., Ntanasis‐Stathopoulos, I., Kastritis, E., Terpos, E., & Dimopoulos, M. A. (2018) · Aging · doi:10.18632/aging.101707 · Cited by 20
“Agents that target the amyloid deposits (passive immunotherapy) with the aim of accelerating removal and restoring organ function are currently being investigated in clinical trials [137-139].”
BackgroundCurrent status and prospect of anti-amyloid fibril therapy in AL amyloidosis.
Wang, J., Li, J., & Zhong, L.-Y. (2024) · Blood reviews · doi:10.1016/j.blre.2024.101207 · Cited by 15
The ASC inflammasome adapter governs SAA-derived protein aggregation in inflammatory amyloidosis
Losa, M., Emmenegger, M., Rossi, P. D., Schürch, P. M., Serdiuk, T., Pengo, N., Capron, D., Bieli, D., Bargenda, N., Rupp, N. J., et al. (2024) · EMBO Molecular Medicine · doi:10.1038/s44321-024-00107-0 · Cited by 15
“…co-localize with amyloid deposits and that Fc γ -receptor-mediated phagocytosis plays an important role in deposition, processing, and clearing of AA amyloid (Lundmark et al, 2013; Nyström and Westermark, 2012; Richards et al, 2018; Sponarova et al, 2013; Vahdat Shariat Panahi et al, 2019).”
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Ma, Y. J., Parente, R., Zhong, H., Sun, Y., Garlanda, C., & Doni, A. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.115878 · Cited by 16
Mechanisms of Organ Damage and Novel Treatment Targets in AL Amyloidosis
Lavatelli, F. (2022) · Hemato · doi:10.3390/hemato3010005 · Cited by 13
“At least three such antibodies have reached the stage of pharmaceutical production and clinical trials, namely Birtamimab (NEOD001) [28,115] and CAEL-101 [114], both targeting amyloid fibrils, and dezamizumab, targeting Serum Amyloid P (given in conjunction with miridesap, a small molecule that depletes circulating SA…”
BackgroundUse of novel therapies in the treatment of light chain amyloidosis.
Varga, C., Titus, S. E., Toskic, D., & Comenzo, R. (2019) · Blood reviews · doi:10.1016/j.blre.2019.05.005 · Cited by 13
Emerging drugs for the treatment of light chain amyloidosis
Chakraborty, R., & Lentzsch, S. (2020) · Expert Opinion on Emerging Drugs · doi:10.1080/14728214.2020.1803829 · Cited by 14
Advances in understanding the role of pentraxin-3 in lung infections
Ma, L., Li, D.-M., Wen, Y.-Y., & Shi, D.-M. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1575968 · Cited by 11
“Short-chain proteins, including C-reactive protein (CRP) and serum amyloid P component (SAP), are predominately produced by hepatocytes and act as important mediators in regulation of the human immune system (12).”
Innate immune response in acute critical illness: a narrative review
Stiel, L., Gaudet, A., Thietart, S., Vallet, H., Bastard, P., Voiriot, G., Oualha, M., Sarton, B., Kallel, H., Bréchot, N., et al. (2024) · Annals of Intensive Care · doi:10.1186/s13613-024-01355-6 · Cited by 13
Barriers to Small Molecule Drug Discovery for Systemic Amyloidosis
Morgan, G. (2021) · Molecules · doi:10.3390/molecules26123571 · Cited by 11
“therapies have used monoclonal antibodies directed at either the fibrils themselves [28,29] or the accessory protein SAP [30,31] to recruit phagocytic cells to clear the amyloid.”
BackgroundEmerging Therapies for Transthyretin Cardiac Amyloidosis
Alexander, K., Evangelisti, A., & Witteles, R. (2019) · Current Treatment Options in Cardiovascular Medicine · doi:10.1007/s11936-019-0743-2 · Cited by 11
Binding of serum-derived amyloid-associated proteins to amyloid fibrils
Misumi, Y., Tabata, Y., Tasaki, M., Obayashi, K., Yamakawa, S., Nomura, T., & Ueda, M. (2022) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2022.2120800 · Cited by 10
Monoclonal Antibody Therapies in Systemic Light-Chain Amyloidosis
Godara, A., & Palladini, G. O. (2020) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2020.08.005 · Cited by 9
Wolfson, A., Shah, K., & Patel, J. (2019) · Current Cardiology Reports · doi:10.1007/s11886-019-1230-9 · Cited by 10
Approach to a patient with cardiac amyloidosis
Strouse, C., Briasoulis, A., Fonseca, R., & Jethava, Y. (2019) · Journal of Geriatric Cardiology · doi:10.11909/j.issn.1671-5411.2019.07.010 · Cited by 10
Cardiac amyloidosis: evolving pathogenesis, multimodal diagnostics, and principles of treatment
Medarametla, G. D., Kahlon, R. S., Mahitha, L., Shariff, S., Vakkalagadda, N. P., Chopra, H., Kamal, M. A., Patel, N., Sethi, Y., & Kaka, N. (2023) · EXCLI journal · doi:10.17179/excli2023-6284 · Cited by 11
GlycoTAIL and FlexiTAIL as Half-Life Extension Modules for Recombinant Antibody Fragments
Seifert, O., & Kontermann, R. E. (2022) · Molecules · doi:10.3390/molecules27103272 · Cited by 9
Klotz, S., Bradley, N., & Lipke, P. (2022) · Pathogens · doi:10.3390/pathogens11091000 · Cited by 8
“In combination with anti-SAP antibodies, miridesap has successfully cleared human amyloid deposits [12].”
BackgroundImmunotherapy in AL Amyloidosis
Zhang, Y., & Comenzo, R. L. (2022) · Current Treatment Options in Oncology · doi:10.1007/s11864-021-00922-4 · Cited by 9
“The phase 1b part of the trial extended the study by eight additional patients [41].”
BackgroundEmerging Therapies for Transthyretin Amyloidosis
Tsoi, M. R., Lin, J., & Patel, A. R. (2023) · Current Oncology Reports · doi:10.1007/s11912-023-01397-2 · Cited by 9
Richards, D., Millns, H., Cookson, L., & Lukas, M. (2021) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-022-02405-7 · Cited by 7
“Thirteen of the fifteen subjects from Part A and eight newly enrolled subjects were included in Part B [16] to investigate the safety, tolerability and efficacy of up to three cycles of anti-SAP treatment.”
BackgroundMethodInfluentialSelf-citationAdvances in pharmacotherapy for cardiac amyloidosis
Spoladore, R., Falasconi, G., Marcatti, M., di Maio, S., Fiore, G., Slavich, M., Margonato, A., Turco, A., & Fragasso, G. (2020) · Expert Opinion on Pharmacotherapy · doi:10.1080/14656566.2020.1836159 · Cited by 7
“Infusion of antiSAP triggered transient early inflammatory cytokine release, improving organ function and with moderate side effects, in AL patients [53,54].”
BackgroundInfluentialBasset, M., Nuvolone, M., Palladini, G., & Merlini, G. (2020) · Expert Review of Hematology · doi:10.1080/17474086.2020.1803060 · Cited by 7
Brunger, A. F., Nienhuis, H. L. A., Bijzet, J., Roeloffzen, W. W. H., Vellenga, E., & Hazenberg, B. P. C. (2020) · Amyloid · doi:10.1080/13506129.2020.1714581 · Cited by 6
Role of extracellular space and matrix remodeling in cardiac amyloidosis
Lavatelli, F., Marchese, L., Mangione, P. P., Raimondi, S., Canetti, D., Verona, G., Venneri, L., Arbustini, E., Obici, L. P., Corazza, A., et al. (2025) · Matrix Biology · doi:10.1016/j.matbio.2025.07.004 · Cited by 10
Optimizing drug therapies in cardiac amyloidosis.
Younis, M. F., Ogbu, I., & Kalra, D. K. (2024) · Pharmacology and Therapeutics · doi:10.1016/j.pharmthera.2024.108758 · Cited by 6
Narrative review of pharmacotherapy for transthyretin cardiac amyloid
Rodriguez, J. C. C., & Tallaj, J. (2020) · Annals of Translational Medicine · doi:10.21037/atm-20-4636 · Cited by 6
“Transient changes in NT-proBNP were observed, although no effect on cardiac amyloid deposits were shown (93).”
BackgroundZhou, J., Li, Y., Geng, J., Zhou, H., Liu, L., & Peng, X. (2023) · Journal of Cardiovascular Pharmacology · doi:10.1097/fjc.0000000000001478 · Cited by 9
“113 Transthyretin Fiber Aggregation Interrupter EGCG, a catechin found in green tea, has been shown to inhibit the formation of amyloid fi bers in various proteins.”
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
“In the phase Ib part of the trial, which included the aforementioned 15 patients plus an additional eight patients for a total of 23 patients with systemic amyloidosis, a 2000 mg dose of dezamizumab reduced amyloid load in the liver and/or spleen in five of seven the patients who received it, confirmed by (123)I-label…”
BackgroundMethodInfluentialKidney Disease in Systemic Amyloidosis
Chowdhury, R. B., Shah, S. I., Latcha, S., & Lobato, L. (2024) · Kidney360 · doi:10.34067/kid.0000000600 · Cited by 4
“27,28 Regardless of the in fl amma-torytrigger,suppressingits activity portends better outcomes.”
Yu, J., Zhu, H., Taheri, S., Lee, J.-Y., Diamond, D., Kirstein, C., & Kindy, M. (2023) · bioRxiv · doi:10.21203/rs.3.rs-3258406/v1 · Cited by 4
Current Understanding of Systemic Amyloidosis and Underlying Disease Mechanisms.
Picken, M. (2022) · American Journal of Cardiology · doi:10.1016/j.amjcard.2022.10.057 · Cited by 4
Yu, J., Zhu, H., Saeid, T., Lee, J.-Y., Diamond, D. M., Kirstein, C. L., & Kindy, M. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052281 · Cited by 5
“In addition to stroke, the inhibition of SAAs might be a novel treatment for other neurological and neurodegenerative disorders in which disturbances in SAA homeostasis comprise a major pathogenic feature [59,60].”
In vitro and in vivo disease models of cardiac amyloidosis: progress, pitfalls, and potential
Qin, J., Qiu, Z., Fan, Y., Xiong, Q., Lei, Z., Wei, J., van der Harst, P., Minnema, M. C., Sluijter, J. P. G., van Mil, A., et al. (2025) · Cardiovascular Research · doi:10.1093/cvr/cvaf152 · Cited by 4
“206,209 In addition, the lifespan of these transgenic models has not been fully reported.”
Cong, M., Weber, R. C. G., Sakane, S., Zhang, V., Jiang, C., Taura, K., Kodama, Y., Deminicis, S., Ganguly, S., Brafman, D. A., et al. (2024) · Hepatology Communications · doi:10.1097/hc9.0000000000000557 · Cited by 3
Ihne-Schubert, S., Kircher, M., Werner, R., Lapa, C., Einsele, H., Geier, A., & Schubert, T. (2023) · PLoS ONE · doi:10.1371/journal.pone.0289921 · Cited by 3
Advancements and future trends of immunotherapy in light-chain amyloidosis
Mahadevia, H. J., Ponvilawan, B., Sharma, P., Al‐Obaidi, A., Qasim, H., Koyi, J., Anwer, F., & Raza, S. (2023) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2023.103917 · Cited by 4
The revolution of ATTR amyloidosis in cardiology: certainties, gray zones and perspectives.
Rapezzi, C., Vergaro, G., Emdin, M., Fabbri, G., Cantone, A., Sanguettoli, F., & Aimo, A. (2022) · Minerva cardiology and angiology · doi:10.23736/s2724-5683.21.05926-3 · Cited by 3
Wild-Type Transthyretin Amyloid Cardiomyopathy: The Gordian-Knot of Novel Therapeutic Regimens
Zegkos, T., Gossios, T. D., Ntelios, D., Parcharidou, D. G., Karvounis, H. I., & Efthimiadis, G. K. (2021) · Cardiology in Review · doi:10.1097/crd.0000000000000427 · Cited by 3
“It did not have, however, a significant effect on myocardial dysfunction.(74)”
BackgroundCardiac Amyloidosis Therapy: A Systematic Review
Iodice, F., Mauro, M. D., Migliaccio, M., Iannuzzi, A., Pacileo, R., Caiazza, M., & Esposito, A. (2021) · doi:10.3390/cardiogenetics11010002 · Cited by 3
“Another trial showed no significant improvement or cardiac-adverse effect after Miridesap in patients with cardiac damage [44].”
BackgroundSystemic Amyloidosis due to Monoclonal Immunoglobulins: Cardiac Involvement.
Saith, S., Maurer, M., & Patel, A. R. (2020) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2020.07.006 · Cited by 3
Richards, D., Bamford, M., Liefaard, L., Haque, N., Lewis, G., Storey, J., Fernando, D., Kumar, S., Thompson, D., & Holmes, D. S. (2019) · British Journal of Pharmacology · doi:10.1111/bph.14956 · Cited by 3
Self-citationRecent advances in the pharmacotherapy of TTR amyloidosis of the heart
Shah, R. J., Pan, S., Lanier, G., Mellela, L., Aronow, W., & Jain, D. (2021) · Vessel Plus · doi:10.20517/2574-1209.2021.76 · Cited by 3
Novel monoclonal antibodies: A really specific therapy for light chain amyloidosis
Giudice, M. L. D., Galimberti, S., & Buda, G. (2024) · Hematological Oncology · doi:10.1002/hon.3270 · Cited by 2
“45 In the subsequent phase 2 study, which focused on cardiac disease, the primary endpoint was the achievement of changes in left ventricular mass as assessed by cardiac magnetic resonance imaging from baseline to 8 ‐ week follow ‐ up and safety.”
MethodZaidel, E. J., Song, S., Sterba, J. J., Piccinato, A., Ramos, M. C., & Cacia, S. L. (2024) · Therapeutic Advances in Cardiovascular Disease · doi:10.1177/17539447241295957 · Cited by 2
The Discovery and Development of Transthyretin Amyloidogenesis Inhibitors: What are the Lessons?
Zhong, B., Huang, X., Zheng, Y., Guo, X., & Wu, L. (2021) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0248 · Cited by 2
Ino, H., Doi, Y., Liefaard, L., Cookson, L., Chen, C., Itoh, H., Igarashi, H., & Nakano, A. (2018) · Clinical pharmacology in drug development · doi:10.1002/cpdd.631 · Cited by 2
Self-citationRauf, M., Riefolo, M., Wong, E., Gilbertson, J., Petrie, A., Law, S., Razvi, Y., Mansell, J., Sheikh, A., Carruthers, J. E., et al. (2026) · Kidney International · doi:10.1016/j.kint.2026.06.036 · Cited by 1
Self-citationAMYLOID-ASSOCIATED CONDITIONS AS AN AGGRAVATING FACTOR IN ENTHESOPATHIES: A CONCEPTUAL THEORY
Shevchenko, Y., & Kokorin, V. V. (2026) · Bulletin of Pirogov National Medical & Surgical Center · doi:10.25881/20728255_2026_21_2_4 · Cited by 1
Chen, H.-X., Yang, Q., & He, G.-W. (2026) · Clinical Proteomics · doi:10.1186/s12014-026-09606-3 · Cited by 1
“Iodine-123 labelled SAP is used as a diagnostic marker for the diagnosis of systemic amyloidosis [23].”
Wang, S., Li, D.-Y., Zhang, X., Zhou, F.-D., & Wang, S.-X. (2025) · BMC Nephrology · doi:10.1186/s12882-025-04477-6 · Cited by 1
“Clinical trials targeting SAP have shown that the small-molecule drug, miridesap, which depletes circulation SAP, followed by subsequent administration of anti-SAP antibody, can progressively remove amyloid from kidneys and spleens [12–14].”
Sugita-Hamada, M., Yokoo, T., Nakajima, N., Takahashi, Y., Osaki, A., Maruyama, M., Takamura, M., Waguri, N., Isokawa, O., & Terai, S. (2025) · Journal of Personalized Medicine · doi:10.3390/jpm15070277 · Cited by 1
Metadata
- Authors
- 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., Wechalekar, A., Hawkins, P. N., & Pepys, M. B.
- Affiliations
- GlaxoSmithKline (United Kingdom) (GB)
- National Health Service (GB)
- Guy's Hospital (GB)
- St Bartholomew's Hospital (GB)
- Corresponding author
- Pepys, Mark B.
- ORCID
- Venue
- Science Translational Medicine
- Published
- 2018-01-03
- Volume
- 10
- Issue
- 422
- ISSN
- 1946-6234 (ISSN-L)
- 1946-6242
- OpenAlex
- W2782423765
- Cited by
- 136
- References
- 0
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 18 · 2023: 8 · 2022: 21 · 2021: 20 · 2020: 20 · 2019: 20 · 2018: 13
- FWCI
- 6.49
- Type
- journal article
- Language
- en
- Open access
- green
- discovery.ucl.ac.uk
- Locations
- Science Translational Medicine (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- GlaxoSmithKline (award308029, N/A)
- Topics
- Health Sciences › Medicine › Internal Medicine › Amyloidosis: Diagnosis, Treatment, Outcomes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- systemic amyloidosis, cardiac amyloidosis, serum amyloid P component, anti-amyloid antibodies, amyloid deposition, spleen, kidney, antibody therapy
- MeSH terms
- Serum Amyloid P-Component, Amyloidosis, Antibodies, Humans, Magnetic Resonance Imaging, Radionuclide Imaging, Plaque, Amyloid
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