Umeå University's logo

umu.sePublications
Change search
Link to record
Permanent link

Direct link
Alternative names
Publications (10 of 186) Show all publications
Anan, I., Suhr, O. B., Liszewska, K., Baranda, J. M., Pilebro, B., Wixner, J. & Ihse, E. (2022). Amyloid fibril composition type is consistent over time in patients with Val30Met (p. Val50Met) transthyretin amyloidosis. PLOS ONE, 17(3), Article ID e0266092.
Open this publication in new window or tab >>Amyloid fibril composition type is consistent over time in patients with Val30Met (p. Val50Met) transthyretin amyloidosis
Show others...
2022 (English)In: PLOS ONE, E-ISSN 1932-6203, Vol. 17, no 3, article id e0266092Article in journal (Refereed) Published
Abstract [en]

Background: We have previously shown that transthyretin (TTR) amyloidosis patients have amyloid fibrils of either of two compositions; type A fibrils consisting of large amounts of C-terminal TTR fragments in addition to full-length TTR, or type B fibrils consisting of only full-length TTR. Since type A fibrils are associated with an older age in ATTRVal30Met (p.Val50Met) amyloidosis patients, it has been discussed if the TTR fragments are derived from degradation of the amyloid deposits as the patients are aging. The present study aimed to investigate if the fibril composition type changes over time, especially if type B fibrils can shift to type A fibrils as the disease progresses.

Material and methods: Abdominal adipose tissue biopsies from 29 Swedish ATTRVal30Met amyloidosis patients were investigated. The fibril type in the patients initial biopsy taken for diagnostic purposes was compared to a biopsy taken several years later (ranging between 2 and 13 years). The fibril composition type was determined by western blot.

Results: All 29 patients had the same fibril composition type in both the initial and the follow-up biopsy (8 type A and 21 type B). Even patients with a disease duration of more than 12 years and an age over 75 years at the time of the follow-up biopsy had type B fibrils in both biopsies.

Discussion: The result clearly shows that the amyloid fibril composition containing large amounts of C-terminal fragments (fibril type A) is a consequence of other factors than a slow degradation process occurring over time.

Place, publisher, year, edition, pages
Public Library of Science, 2022
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:umu:diva-193805 (URN)10.1371/journal.pone.0266092 (DOI)000799828800066 ()35358243 (PubMedID)2-s2.0-85127435798 (Scopus ID)
Funder
Erik, Karin och Gösta Selanders Foundation
Available from: 2022-05-06 Created: 2022-05-06 Last updated: 2023-09-05Bibliographically approved
Unéus, E. I., Wilhelmsson, C., Bäckström, D., Anan, I., Wixner, J., Pilebro, B., . . . Sundström, T. (2022). Cerebellar and Cerebral Amyloid Visualized by [18F]flutemetamol PET in Long-Term Hereditary V30M (p.V50M) Transthyretin Amyloidosis Survivors. Frontiers in Neurology, 13, Article ID 816636.
Open this publication in new window or tab >>Cerebellar and Cerebral Amyloid Visualized by [18F]flutemetamol PET in Long-Term Hereditary V30M (p.V50M) Transthyretin Amyloidosis Survivors
Show others...
2022 (English)In: Frontiers in Neurology, E-ISSN 1664-2295, Vol. 13, article id 816636Article in journal (Refereed) Published
Abstract [en]

Introduction: Hereditary transthyretin (ATTRv) amyloidosis caused by the V30M (p. V50M) mutation is a fatal, neuropathic systemic amyloidosis. Liver transplantation has prolonged the survival of patients and central nervous system (CNS) complications, attributed to amyloid angiopathy caused by CNS synthesis of variant transthyretin, have emerged. The study aimed to ascertain amyloid deposition within the brain in long-term ATTRv amyloidosis survivors with neurological symptoms from the CNS.

Methods: A total of 20 patients with ATTR V30M having symptoms from the CNS and a median disease duration of 16 years (8–25 years) were included in this study. The cognitive and peripheral nervous functions were determined for 18 patients cross-sectionally at the time of the investigation. Amyloid brain deposits were examined by [18F]flutemetamol PET/CT. Five patients with Alzheimer's disease (AD) served as positive controls.

Result: 60% of the patients with ATTRv had a pathological Z-score in the cerebellum, compared to only 20% in the patients with AD. 75% of the patients with transient focal neurological episodes (TFNEs) displayed a pathological uptake only in the cerebellum. Increased cerebellar uptake was related to an early age of onset of the ATTRv disease. 55% of the patients with ATTRv had a pathological Z-score in the global cerebral region compared to 100% of the patients with AD.

Conclusion: Amyloid deposition within the brain after long-standing ATTRv amyloidosis is common, especially in the cerebellum. A cerebellar amyloid uptake profile seems to be related to TFNE symptoms.

Place, publisher, year, edition, pages
Frontiers Media S.A., 2022
Keywords
amyloid angiopathy, amyloidosis-hereditary, positron emission tomography, transthyretin, [18F]flutemetamol
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-193803 (URN)10.3389/fneur.2022.816636 (DOI)000773941500001 ()35317351 (PubMedID)2-s2.0-85127418033 (Scopus ID)
Funder
Swedish Heart Lung Foundation, 20160787Region VästerbottenThe Swedish Brain Foundation
Available from: 2022-05-06 Created: 2022-05-06 Last updated: 2023-08-28Bibliographically approved
Wixner, J., Anan, I., Pilebro, B., Uneus, E., Mejia Baranda, J., Liszewska, K., . . . Suhr, O. B. (2022). Hereditary transthyretin amyloidosis - from symptomatic to curative treatment?: [Ärftlig transtyretinamyloidos – från lindring till potentiell bot]. Läkartidningen, 119, 26-30, Article ID 21202.
Open this publication in new window or tab >>Hereditary transthyretin amyloidosis - from symptomatic to curative treatment?: [Ärftlig transtyretinamyloidos – från lindring till potentiell bot]
Show others...
2022 (English)In: Läkartidningen, ISSN 0023-7205, E-ISSN 1652-7518, Vol. 119, p. 26-30, article id 21202Article in journal (Refereed) Published
Abstract [en]

Hereditary transthyretin (ATTRv) amyloidosis is a rare but life-threatening multi-systemic disease with clustering areas in, for example, northern Sweden. Until the 1990s, only symptomatic treatments were available but liver transplantation has, in selected patients, been a good therapeutic option since. The first disease-modifying drug for ATTRv amyloidosis was approved in 2011 and since then, the development of new therapeutic drugs has been rapid and successful. Two gene silencing therapies were approved for the disease in 2018, both showing a robust reduction in serum transthyretin levels and a satisfactory safety profile. Recently, CRISPR-Cas9 gene editing has also shown promising results in patients with ATTRv amyloidosis. The recent developments have had a paramount effect on the management of these patients, and will probably also have a significant positive effect on their life expectancy. However, treatment costs have skyrocketed, which implies future challenges.

Place, publisher, year, edition, pages
Stockholm: Sveriges Läkarförbund, 2022
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-196519 (URN)35670119 (PubMedID)2-s2.0-85131338415 (Scopus ID)
Note

Lakartidningen.se 2022-06-03

Available from: 2022-06-15 Created: 2022-06-15 Last updated: 2023-05-26Bibliographically approved
Michalon, A., Hagenbuch, A., Huy, C., Varela, E., Combaluzier, B., Damy, T., . . . Grimm, J. (2021). A human antibody selective for transthyretin amyloid removes cardiac amyloid through phagocytic immune cells. Nature Communications, 12(1), Article ID 3142.
Open this publication in new window or tab >>A human antibody selective for transthyretin amyloid removes cardiac amyloid through phagocytic immune cells
Show others...
2021 (English)In: Nature Communications, E-ISSN 2041-1723, Vol. 12, no 1, article id 3142Article in journal (Refereed) Published
Abstract [en]

Transthyretin amyloid (ATTR) cardiomyopathy is a debilitating disease leading to heart failure and death. It is characterized by the deposition of extracellular ATTR fibrils in the myocardium. Reducing myocardial ATTR load is a therapeutic goal anticipated to translate into restored cardiac function and improved patient survival. For this purpose, we developed the selective anti-ATTR antibody NI301A, a recombinant human monoclonal immunoglobulin G1. NI301A was cloned following comprehensive analyses of memory B cell repertoires derived from healthy elderly subjects. NI301A binds selectively with high affinity to the disease-associated ATTR aggregates of either wild-type or variant ATTR related to sporadic or hereditary disease, respectively. It does not bind physiological transthyretin. NI301A removes ATTR deposits ex vivo from patient-derived myocardium by macrophages, as well as in vivo from mice grafted with patient-derived ATTR fibrils in a dose- and time-dependent fashion. The biological activity of ATTR removal involves antibody-mediated activation of phagocytic immune cells including macrophages. These data support the evaluation of safety and tolerability of NI301A in an ongoing phase 1 clinical trial in patients with ATTR cardiomyopathy.

Place, publisher, year, edition, pages
Nature Publishing Group, 2021
National Category
Other Clinical Medicine
Identifiers
urn:nbn:se:umu:diva-184199 (URN)10.1038/s41467-021-23274-x (DOI)000658774600014 ()2-s2.0-85106879802 (Scopus ID)
Available from: 2021-06-14 Created: 2021-06-14 Last updated: 2023-09-05Bibliographically approved
Löfbacka, V., Axelsson, J., Pilebro, B., Suhr, O. B., Lindqvist, P. & Sundström, T. (2021). Cardiac transthyretin amyloidosis 99mTc-DPD SPECTcorrelates with strain echocardiography and biomarkers. European Journal of Nuclear Medicine and Molecular Imaging, 48, 1822-1832
Open this publication in new window or tab >>Cardiac transthyretin amyloidosis 99mTc-DPD SPECTcorrelates with strain echocardiography and biomarkers
Show others...
2021 (English)In: European Journal of Nuclear Medicine and Molecular Imaging, ISSN 1619-7070, E-ISSN 1619-7089, Vol. 48, p. 1822-1832Article in journal (Refereed) Published
Abstract [en]

Purpose: Hereditary transthyretin-amyloid amyloidosis (ATTRv) is an underdiagnosed condition commonly manifesting as congestive heart failure. Recently, scintigraphy utilizing DPD as a tracer was shown to identify ATTRv and wild-type ATTR cardiomyopathy. The aim of this study was to determine the value of quantified scintigraphy utilizing 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid (DPD) single-photon emission computed tomography (SPECT)/CT, and to correlate its uptake with well-established cardiac functional parameters.

Methods: Forty-eight patients with genetically verified ATTRv type-A fibril composition, positive 99mTc-DPD SPECT/CT, were retrospectively analyzed. Manual mapping of volumes of interest (VOIs) on DPD SPECT/CT examinations was used to quantify heart uptake. DPD mean and maximum uptake together with a calculated DPD-based amyloid burden (DPDload) was correlated with echocardiographic strain values and cardiac biomarkers.

Results: Statistically significant correlations were seen in VOIs between DPD uptakes and the corresponding echocardiographic strain values. Furthermore, DPDload had a strong correlation with echocardiographic strain parameters and also correlated with biomarkers troponin T and logarithmic NT-ProBNP.

Conclusions: In patients with ATTRv cardiomyopathy, DPD SPECT/CT measures the amyloid distribution and provides information on cardiac amyloid load. DPD amyloid load correlates with functional cardiac parameters.

Place, publisher, year, edition, pages
Springer, 2021
Keywords
Amyloidosis-hereditary, Cardiomyopathy, Transthyretin amyloidosis, Tc-99m-DPD scintigraphy, 2D speckle tracking strain, SPECT
National Category
Radiology, Nuclear Medicine and Medical Imaging
Identifiers
urn:nbn:se:umu:diva-178531 (URN)10.1007/s00259-020-05144-8 (DOI)000602293500001 ()33367948 (PubMedID)2-s2.0-85098069527 (Scopus ID)
Funder
Swedish Heart Lung Foundation, 20160787
Available from: 2021-01-15 Created: 2021-01-15 Last updated: 2023-03-24Bibliographically approved
Löfbacka, V., Suhr, O. B., Pilebro, B., Wixner, J., Sundström, T., Lindmark, K., . . . Lindqvist, P. (2021). Combining ECG and echocardiography to identify transthyretin cardiac amyloidosis in heart failure. Clinical Physiology and Functional Imaging, 41(5), 408-416
Open this publication in new window or tab >>Combining ECG and echocardiography to identify transthyretin cardiac amyloidosis in heart failure
Show others...
2021 (English)In: Clinical Physiology and Functional Imaging, ISSN 1475-0961, E-ISSN 1475-097X, Vol. 41, no 5, p. 408-416Article in journal (Refereed) Published
Abstract [en]

AIMS/BACKGROUND: Transthyretin amyloid (ATTR) amyloidosis cardiomyopathy is an underdiagnosed, causatively treatable cause of heart failure. The aim of this study was to evaluate the efficacy of electrocardiography (ECG) and echocardiography on patients with increased interventricular septum diameter (IVSd) to identify ATTR cardiac amyloidosis (ATTR-CA) patients.

METHODS: We investigated 58 patients with heart failure and an IVSd >14mm. Included were 33 ATTR-CA patients and 25 controls that consisted of non-amyloidosis heart failure (HF) patients with negative 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid (DPD) scintigraphy. We used echocardiography including 2D speckle tracking strain and a 12-lead ECG to test the accuracy to differentiate the groups.

RESULTS: We found high diagnostic accuracy (98%) for differentiating ATTR-CA from HF controls using a combination of R amplitude in -aVR from ECG and relative wall thickness acquired from echocardiography. With this combined model (RWT/ R in -aVR), the sensitivity was 100% and specificity was 95% using a cut off value of 0.90. Furthermore, the area under the curve was 99% and the negative predictive value was 100%.

CONCLUSION: We found that a simple combination of ECG and echocardiographic parameters used in clinical settings was able to differentiate ATTR-CA from other etiologies of HF with increased interventricular septum thickness. The high sensitivity and negative predictive value render the algorithm useful for selection of patients for further diagnostic procedures for ATTR-CA.

Place, publisher, year, edition, pages
John Wiley & Sons, 2021
Keywords
Cardiac amyloidosis, ECG, Echocardiography, Heart failure, Transthyretin amyloidosis
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:umu:diva-183897 (URN)10.1111/cpf.12715 (DOI)000661468500001 ()34033209 (PubMedID)2-s2.0-85107933221 (Scopus ID)
Funder
Swedish Heart Lung Foundation, 20160787Swedish Heart Lung Foundation, 20200160Swedish Research Council, 2019-01338
Available from: 2021-06-03 Created: 2021-06-03 Last updated: 2022-03-04Bibliographically approved
Adams, D., Ando, Y., Beirão, J. M., Coelho, T., Gertz, M. A., Gillmore, J. D., . . . Merlini, G. (2021). Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy. Journal of Neurology, 268(6), 2109-2122
Open this publication in new window or tab >>Expert consensus recommendations to improve diagnosis of ATTR amyloidosis with polyneuropathy
Show others...
2021 (English)In: Journal of Neurology, ISSN 0340-5354, E-ISSN 1432-1459, Vol. 268, no 6, p. 2109-2122Article, review/survey (Refereed) Published
Abstract [en]

Amyloid transthyretin (ATTR) amyloidosis with polyneuropathy (PN) is a progressive, debilitating, systemic disease wherein transthyretin protein misfolds to form amyloid, which is deposited in the endoneurium. ATTR amyloidosis with PN is the most serious hereditary polyneuropathy of adult onset. It arises from a hereditary mutation in theTTRgene and may involve the heart as well as other organs. It is critical to identify and diagnose the disease earlier because treatments are available to help slow the progression of neuropathy. Early diagnosis is complicated, however, because presentation may vary and family history is not always known. Symptoms may be mistakenly attributed to other diseases such as chronic inflammatory demyelinating polyradiculoneuropathy (CIDP), idiopathic axonal polyneuropathy, lumbar spinal stenosis, and, more rarely, diabetic neuropathy and AL amyloidosis. In endemic countries (e.g., Portugal, Japan, Sweden, Brazil), ATTR amyloidosis with PN should be suspected in any patient who has length-dependent small-fiber PN with autonomic dysfunction and a family history of ATTR amyloidosis, unexplained weight loss, heart rhythm disorders, vitreous opacities, or renal abnormalities. In nonendemic countries, the disease may present as idiopathic rapidly progressive sensory motor axonal neuropathy or atypical CIDP with any of the above symptoms or with bilateral carpal tunnel syndrome, gait disorders, or cardiac hypertrophy. Diagnosis should include DNA testing, biopsy, and amyloid typing. Patients should be followed up every 6-12 months, depending on the severity of the disease and response to therapy. This review outlines detailed recommendations to improve the diagnosis of ATTR amyloidosis with PN.

Place, publisher, year, edition, pages
Springer Berlin/Heidelberg, 2021
Keywords
ATTR amyloidosis, ATTRv, Diagnosis, hATTR, Peripheral neuropathy, Transthyretin amyloidosis
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-176103 (URN)10.1007/s00415-019-09688-0 (DOI)000574072100001 ()31907599 (PubMedID)2-s2.0-85077555379 (Scopus ID)
Note

First published online: 06 January 2020

Available from: 2020-11-11 Created: 2020-11-11 Last updated: 2022-05-05Bibliographically approved
Nakov, R., Suhr, O. B., Ianiro, G., Kupcinskas, J., Segal, J. P., Dumitrascu, D. L., . . . Wixner, J. (2021). Recommendations for the diagnosis and management of transthyretin amyloidosis with gastrointestinal manifestations. European Journal of Gastroenterology and Hepathology, 33(5), 613-622
Open this publication in new window or tab >>Recommendations for the diagnosis and management of transthyretin amyloidosis with gastrointestinal manifestations
Show others...
2021 (English)In: European Journal of Gastroenterology and Hepathology, ISSN 0954-691X, E-ISSN 1473-5687, Vol. 33, no 5, p. 613-622Article, review/survey (Refereed) Published
Abstract [en]

Transthyretin amyloid (ATTR) amyloidosis is an adult-onset, rare systemic disorder characterized by the accumulation of misfolded fibrils in the body, including the peripheral nerves, the heart and the gastrointestinal tract. Gastrointestinal manifestations are common in hereditary (ATTRv) amyloidosis and are present even before the onset of the polyneuropathy in some cases. Delays in diagnosis of ATTRv amyloidosis with gastrointestinal manifestations commonly occur because of fragmented knowledge among gastroenterologists and general practitioners, as well as a shortage of centers of excellence and specialists dedicated to disease management. Although the disease is becoming well-recognized in the societies of Neurology and Cardiology, it is still unknown for most gastroenterologists. This review presents the recommendations for ATTRv amyloidosis with gastrointestinal manifestations elaborated by a working group of European gastroenterologists and neurologists, and aims to provide digestive health specialists with an overview of crucial aspects of ATTRv amyloidosis diagnosis to help facilitate rapid and accurate identification of the disease by focusing on disease presentation, misdiagnosis and management of gastrointestinal symptoms.

Place, publisher, year, edition, pages
Lippincott Williams & Wilkins, 2021
National Category
Gastroenterology and Hepatology
Identifiers
urn:nbn:se:umu:diva-182383 (URN)10.1097/MEG.0000000000002030 (DOI)000639305200003 ()33394808 (PubMedID)2-s2.0-85103682985 (Scopus ID)
Available from: 2021-04-26 Created: 2021-04-26 Last updated: 2023-09-05Bibliographically approved
Eldhagen, P., Berg, S., Lund, L. H., Sörensson, P., Suhr, O. B. & Westermark, P. (2021). Transthyretin amyloid deposits in lumbar spinal stenosis and assessment of signs of systemic amyloidosis. Journal of Internal Medicine, 289(6), 895-905
Open this publication in new window or tab >>Transthyretin amyloid deposits in lumbar spinal stenosis and assessment of signs of systemic amyloidosis
Show others...
2021 (English)In: Journal of Internal Medicine, ISSN 0954-6820, E-ISSN 1365-2796, Vol. 289, no 6, p. 895-905Article in journal (Refereed) Published
Abstract [en]

Background: Wild‐type transthyretin (ATTRwt) amyloidosis is the most common systemic amyloidosis in Western countries and manifests mainly as progressive restrictive cardiomyopathy.

Objective: To study the prevalence of ATTR deposits in ligament tissue in patients undergoing surgery for lumbar spinal stenosis and to assess whether these deposits are associated with cardiac amyloidosis.

Materials and methods: A total of 250 patients, aged 50–89 (57% women), none with known cardiovascular disease, were included. Ligaments were investigated microscopically for amyloid. ATTR type was determined by immunohistochemistry and fibril type by Western blot. The amount of amyloid was graded 0‐4. All patients with grade 3‐4 ATTR deposits were offered cardiac investigation including ECG, cardiac ultrasound, plasma NT‐proBNP and cardiac magnetic resonance (CMR), including modern tissue characterization.

Results: Amyloid was identified in 221 of the samples (88.4%). ATTR appeared in 93 samples (37%) of whom 42 (17 women and 25 men) were graded 3‐4; all had fibril type A (mixture of full‐length TTR and fragmented TTR). Twenty‐nine of 42 patients with grade 3‐4 ATTR deposits accepted cardiovascular investigations; none of them had definite signs of cardiac amyloidosis, but five men had a history of carpal tunnel syndrome.

Conclusions: The prevalence of ATTR deposits in ligamentum flavum in patients with lumbar spinal stenosis was high but not associated with manifest ATTR cardiac amyloidosis. However, the findings of fibril type A, the prevalence of previous carpal tunnel syndrome and ATTR amyloid in surrounding adipose and vascular tissue indicate that amyloid deposits in ligamentum flavum may be an early manifestation of systemic ATTR disease.

Place, publisher, year, edition, pages
John Wiley & Sons, 2021
Keywords
ATTR amyloidosis, cardiac amyloidosis, Lumbar spinal stenosis, magnetic resonance imaging, systemic amyloidosis
National Category
Other Clinical Medicine
Identifiers
urn:nbn:se:umu:diva-178957 (URN)10.1111/joim.13222 (DOI)000605447800001 ()33274477 (PubMedID)2-s2.0-85099097460 (Scopus ID)
Funder
Pfizer AB
Available from: 2021-02-12 Created: 2021-02-12 Last updated: 2022-05-05Bibliographically approved
Coelho, T., Adams, D., Conceicao, I., Waddington-Cruz, M., Schmidt, H. H., Buades, J., . . . Suhr, O. B. (2020). A phase II, open-label, extension study of long-term patisiran treatment in patients with hereditary transthyretin-mediated (hATTR) amyloidosis. Orphanet Journal of Rare Diseases, 15(1), Article ID 179.
Open this publication in new window or tab >>A phase II, open-label, extension study of long-term patisiran treatment in patients with hereditary transthyretin-mediated (hATTR) amyloidosis
Show others...
2020 (English)In: Orphanet Journal of Rare Diseases, E-ISSN 1750-1172, Vol. 15, no 1, article id 179Article in journal (Refereed) Published
Abstract [en]

Background: Patisiran, an RNA interference therapeutic, has demonstrated robust reduction of wild-type and mutant transthyretin protein and was able to improve polyneuropathy and quality of life following 18 months of treatment in patients with hereditary transthyretin-mediated (hATTR) amyloidosis.In this 24-month Phase II open-label extension study, we evaluated the effects of patisiran treatment (0.3 mg/kg intravenously every 3 weeks) on safety, serum transthyretin levels, and clinical parameters. Efficacy assessments included modified Neuropathy Impairment Score +7 (mNIS+7) and multiple disease-relevant measures. Cardiac assessments were performed in a pre-specified cardiac subgroup.

Results: Twenty-seven patients entered this study, including 12 (44%) with ambulation difficulties due to their neuropathy and 11 (41%) who met criteria for the cardiac subgroup. During treatment, the majority of adverse events were mild/moderate in severity; there were no drug-related adverse events leading to treatment discontinuation. The most common drug-related adverse events were flushing and infusion-related reactions (22% each). Patisiran resulted in rapid, robust (similar to 82%), and sustained reduction of mean transthyretin levels over 24 months. A mean 6.95-point decrease (improvement) in mNIS+7 from baseline was observed at 24 months. Patisiran's impact on mNIS+7 was irrespective of concomitant tafamidis or diflunisal use, sex, or age. Clinical assessments of motor function, autonomic symptoms, disease stage, and quality of life remained stable over 24 months. No significant changes were observed for echocardiographic measures or cardiac biomarkers in the cardiac subgroup. Exploratory analyses demonstrated improvements in nerve-fiber density with corresponding reductions in amyloid burden observed in skin biopsies over 24 months.

Conclusions: Long-term treatment with patisiran had an acceptable safety profile and was associated with halting/improvement of polyneuropathy progression in patients with hATTR amyloidosis.

Place, publisher, year, edition, pages
BioMed Central (BMC), 2020
Keywords
ATTR amyloidosis, Cardiomyopathy, Patisiran, Polyneuropathy, RNA interference
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-174053 (URN)10.1186/s13023-020-01399-4 (DOI)000551966000001 ()32641071 (PubMedID)2-s2.0-85087693350 (Scopus ID)
Available from: 2020-08-13 Created: 2020-08-13 Last updated: 2024-03-14Bibliographically approved
Projects
Human Monoclonal Antibodies for the Therapy of Transthyretin Amyloidosis Diseases [2014-04162_Vinnova]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-1175-2369

Search in DiVA

Show all publications