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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CPHPC efficiently reduces SAP concentration in serum (58.5% reduction) and bone marrow (95% reduction) in aged mice.
“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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“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].”
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“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].”
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“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…”
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“1884 amyloid deposits, with a fully humanized monoclonal antibody.(192) Another approach under development is to target specifically the LC fibrils.”
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“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].”
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“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].”
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“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
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“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].”
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“Clinical trials of doxycycline plus tauroursodeoxycholic acid (23) and immunotherapies (24, 25), which aim to disrupt amyloid fibrils, are also being carried out.”
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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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“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].”
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“…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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“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…”
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“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 · see citing works
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 · see citing works
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 · see citing works
Wolfson, A., Shah, K., & Patel, J. (2019) · Current Cardiology Reports · doi:10.1007/s11886-019-1230-9 · Cited by 10 · see citing works
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 · see citing works
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 · see citing works
GlycoTAIL and FlexiTAIL as Half-Life Extension Modules for Recombinant Antibody Fragments
Seifert, O., & Kontermann, R. (2022) · Molecules · doi:10.3390/molecules27103272 · Cited by 9 · see citing works
Klotz, S., Bradley, N., & Lipke, P. (2022) · Pathogens · doi:10.3390/pathogens11091000 · Cited by 8 · see citing works
“In combination with anti-SAP antibodies, miridesap has successfully cleared human amyloid deposits [12].”
BackgroundImmunotherapy in AL Amyloidosis
Zhang, Y., & Comenzo, R. (2022) · Current Treatment Options in Oncology · doi:10.1007/s11864-021-00922-4 · Cited by 8 · see citing works
“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 · see citing works
Richards, D., Millns, H., Cookson, L., & Lukas, M. (2021) · Orphanet Journal of Rare Diseases · doi:10.1186/s13023-022-02405-7 · Cited by 7 · see citing works
“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., Nienhuis, H., Bijzet, J., Roeloffzen, W. W., Vellenga, E., & Hazenberg, B. (2020) · Amyloid: Journal of Protein Folding Disorders · doi:10.1080/13506129.2020.1714581 · Cited by 7
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 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
“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., Taheri, S., Lee, J.-Y., Diamond, D., Kirstein, C., & Kindy, M. S. (2026) · International Journal of Molecular Sciences · doi:10.3390/ijms27052281 · Cited by 3 · see citing works
“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 · see citing works
“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 · see citing works
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., 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 3 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
Chen, H.-X., Yang, Q., & He, G.-W. (2026) · Clinical Proteomics · doi:10.1186/s12014-026-09606-3 · Cited by 1 · see citing works
“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 · see citing works
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Amyloidosis: Diagnosis, Treatment, Outcomes
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Physiology › 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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