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Publications (10 of 49) Show all publications
Planté-Bordeneuve, V., Gorram, F., Olsson, M., Anan, I., Mazzeo, A., Gentile, L., . . . Nuel, G. (2023). A multicentric study of the disease risks and first manifestations in Hereditary transthyretin amyloidosis (ATTRv): insights for an earlier diagnosis. Amyloid: Journal of Protein Folding Disorders, 30(3), 313-320
Open this publication in new window or tab >>A multicentric study of the disease risks and first manifestations in Hereditary transthyretin amyloidosis (ATTRv): insights for an earlier diagnosis
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2023 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 30, no 3, p. 313-320Article in journal (Refereed) Published
Abstract [en]

Background: In hereditary transthyretin amyloidosis (ATTRv), early manifestation and age at onset (AO) may vary strikingly. We assessed the disease’risk (penetrance), AO and initial features in ATTRv families to gain insights on the early disease presentation. Methods: Genealogical information, AO and first disease manifestations were collected in ATTRv families, from Sweden, Italy (Sicily), Spain (Mallorca), France, Turkey, Brazil. Penetrance was computed using a non-parametric survival method. Results: We analysed 258 TTRV30M kindreds and 84 carrying six other variants (TTRT49A, F64L, S77Y, S77F, E89Q, I107V). In ATTRV30M families, the earliest disease risk was found at age 20 years in the Portuguese and Mallorcan families and at age 30-35 years, in the French and Swedish groups. The risks were higher in men and in carriers of maternal descent. In families carrying TTR-nonV30M variants, the earliest disease risk ranged from 30 y-o in TTRT49A to 55 y-o in TTRI107V families. Peripheral neuropathy symptoms were the most frequent initial manifestations. Among patients carrying TTRnonV30M variants, about 25% had an initial cardiac phenotype, one third a mixed phenotype. Conclusion: Our work provided solid data on the risks and early features of ATTRv in a spectrum of families to enhance an early diagnosis and treatment.

Place, publisher, year, edition, pages
Taylor & Francis, 2023
Keywords
amyloid polyneuropathy, Genetics, penetrance, peripheral neuropathy, transthyretin
National Category
Medical Genetics Neurology
Identifiers
urn:nbn:se:umu:diva-205361 (URN)10.1080/13506129.2023.2178891 (DOI)000935256100001 ()2-s2.0-85148588708 (Scopus ID)
Available from: 2023-03-29 Created: 2023-03-29 Last updated: 2023-09-22Bibliographically approved
Arvidsson, S., Eriksson, R., Anan, I. & Heldestad, V. (2023). Enlarged cross-sectional area in peripheral nerves in Swedish patients with hereditary V30M transthyretin amyloidosis. Annals of Medicine, 55(2), Article ID 2239269.
Open this publication in new window or tab >>Enlarged cross-sectional area in peripheral nerves in Swedish patients with hereditary V30M transthyretin amyloidosis
2023 (English)In: Annals of Medicine, ISSN 0785-3890, E-ISSN 1365-2060, Vol. 55, no 2, article id 2239269Article in journal (Refereed) Published
Abstract [en]

Introduction: In hereditary transthyretin amyloidosis (ATTRv), two different fibrillar forms causing the amyloid deposition, have been identified, displaying substantially cardiac or neuropathic symptoms. Neuropathic symptoms are more frequent in early-onset patients, whereas late-onset patients, besides cardiac symptoms, seem to develop carpal tunnel syndrome, more often. With ultrasonography (US) of peripheral nerves, it is possible to distinguish structural changes, and enlarged cross-sectional area (CSA). The main purpose of this study was, for the first time, to elucidate US of peripheral nerves in Swedish ATTRv patients at an early stage of the disease, and to evaluate possible early enlarged CSA.

Material and methods: This prospective study included first visit data of 13 patients, aged 30–88 years, of which 11 with late-onset age. All had a positive V30M mutation. Eight men and six women (aged 28–74 years) served as controls.

Results: Significantly enlarged CSA was seen in ATTRv patients for the tibial nerve at the ankle (p =.001), the sural nerve (p <.001), the peroneal nerve at the popliteal fossa (p =.003), and the ulnar nerve at the middle upper arm (p =.007).

Conclusion: US of peripheral nerves could be a valuable tool in disease evaluation and could facilitate monitoring of disease progression.

Place, publisher, year, edition, pages
Taylor & Francis Group, 2023
Keywords
Hereditary transthyretin amyloidosis, nerve cross-sectional area, nerve entrapments, peripheral nerves, ultrasonography
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-214062 (URN)10.1080/07853890.2023.2239269 (DOI)37619249 (PubMedID)2-s2.0-85168627277 (Scopus ID)
Funder
Umeå University, 2022-06-10Knut and Alice Wallenberg Foundation, RV-762081
Available from: 2023-09-05 Created: 2023-09-05 Last updated: 2024-03-19Bibliographically approved
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
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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
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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
Gharibyan, A., Jayaweera, S. W., Lehmann, M., Anan, I. & Olofsson, A. (2022). Endogenous Human Proteins Interfering with Amyloid Formation. Biomolecules, 12(3), Article ID 446.
Open this publication in new window or tab >>Endogenous Human Proteins Interfering with Amyloid Formation
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2022 (English)In: Biomolecules, E-ISSN 2218-273X, Vol. 12, no 3, article id 446Article, review/survey (Refereed) Published
Abstract [en]

Amyloid formation is a pathological process associated with a wide range of degenerative disorders, including Alzheimer’s disease, Parkinson’s disease, and diabetes mellitus type 2. During disease progression, abnormal accumulation and deposition of proteinaceous material are accompanied by tissue degradation, inflammation, and dysfunction. Agents that can interfere with the process of amyloid formation or target already formed amyloid assemblies are consequently of therapeutic interest. In this context, a few endogenous proteins have been associated with an anti-amyloidogenic activity. Here, we review the properties of transthyretin, apolipoprotein E, clusterin, and BRICHOS protein domain which all effectively interfere with amyloid in vitro, as well as displaying a clinical impact in humans or animal models. Their involvement in the amyloid formation process is discussed, which may aid and inspire new strategies for therapeutic interventions.

Place, publisher, year, edition, pages
MDPI, 2022
Keywords
Alpha-synuclein, Amyloid inhibition, Amyloid-beta, Apolipoprotein E, BRICHOS, Clusterin, Endogenous proteins, IAPP, Transthyretin
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:umu:diva-193407 (URN)10.3390/biom12030446 (DOI)000775848600001 ()2-s2.0-85126704016 (Scopus ID)
Available from: 2022-03-31 Created: 2022-03-31 Last updated: 2023-09-05Bibliographically approved
Mejia Baranda, J., Ljungberg, J., Wixner, J., Anan, I. & Oskarsson, V. (2022). Epidemiology of hereditary transthyretin amyloidosis in the northernmost region of Sweden: a retrospective cohort study. Amyloid: Journal of Protein Folding Disorders, 29(2), 120-127
Open this publication in new window or tab >>Epidemiology of hereditary transthyretin amyloidosis in the northernmost region of Sweden: a retrospective cohort study
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2022 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 29, no 2, p. 120-127Article in journal (Refereed) Published
Abstract [en]

Introduction: Epidemiological data on hereditary transthyretin (ATTRv) amyloidosis from the northernmost region of Sweden (Norrbotten) are sparse.

Methods: We reviewed the medical records of all incident cases of ATTRv amyloidosis in Norrbotten between 2006 and 2018. Official population and mortality statistics were used to estimate incidence rates and standardised mortality ratios (SMRs).

Results: Ninety-three patients were diagnosed with ATTRv amyloidosis between 2006 and 2018 (median age, 72.8 years; 68.8% men; 95.7% Val30Met [p.Val50Met] mutation). The incidence rate per 100,000 persons and year increased from 1.50 (95% confidence interval [CI], 0.84–2.47) cases in 2006–2009 to 4.92 (95%CI, 3.46–6.78) cases in 2016–2018. The SMR in the ATTRv amyloidosis cohort was 2.64 times higher than in the general population in 2006–2018 (95%CI, 1.78–3.77). However, there were indications of lower SMRs over time (2006–2012, 2.96 [95%CI, 1.73–4.74]; 2013–2018, 2.32 [95%CI, 1.23–3.96]) and by use of disease-modifying drugs (no, 3.21 [95%CI, 1.87–5.13]; yes, 2.09 [95%CI, 1.08–3.64]).

Conclusion: The incidence of ATTRv amyloidosis increased 3-fold in Norrbotten between 2006 and 2018, most likely due to a previous underdiagnosis–with suggestions of lowered mortality during later years, possibly due to the introduction of disease-modifying drugs.

Place, publisher, year, edition, pages
Taylor & Francis, 2022
Keywords
Amyloid, amyloidosis, epidemiology, hereditary, Sweden, transthyretin
National Category
Public Health, Global Health, Social Medicine and Epidemiology
Identifiers
urn:nbn:se:umu:diva-191741 (URN)10.1080/13506129.2022.2026323 (DOI)000742289900001 ()35023433 (PubMedID)2-s2.0-85122894118 (Scopus ID)
Funder
Norrbotten County Council
Available from: 2022-01-24 Created: 2022-01-24 Last updated: 2023-05-22Bibliographically approved
Samuelsson, K., Jovanovic, A., Egervall, K., Anan, I., Wixner, J. & Press, R. (2022). Hereditary transthyretin amyloidosis in Sweden: Comparisons between a non-endemic and an endemic region. Amyloid: Journal of Protein Folding Disorders, 29(4), 220-227
Open this publication in new window or tab >>Hereditary transthyretin amyloidosis in Sweden: Comparisons between a non-endemic and an endemic region
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2022 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 29, no 4, p. 220-227Article in journal (Refereed) Published
Abstract [en]

Introduction: Hereditary transthyretin amyloidosis (ATTRv) is endemic in northern Sweden (Västerbotten). The awareness of ATTRv amyloidosis is lower in Stockholm, a non-endemic region in Sweden. The aim of this study was to compare the possible differences in diagnostic delay, disease phenotypes, treatment and survival between a non-endemic and an endemic region in Sweden.

Methods: The in- and outpatient diagnosis registry at the Department of Neurology at Karolinska University Hospital and the Amyloidosis Centre at University Hospital of Umeå were used to identify patients between January 2006 and November 2017.

Results: In total, 21 patients in Stockholm and 134 patients in Västerbotten were included. The time between symptom onset to time-point of diagnosis was significantly longer in Stockholm vs Västerbotten. This corresponded to a longer median time between first visit at amyloidosis centre to time-point of diagnosis in Stockholm vs in Västerbotten. The most common reason for a diagnostic delay was negative tissue biopsies.

Conclusion: There was a diagnostic-, but no patient-delay in non-endemic Stockholm vs endemic Västerbotten. Despite a more severe neuropathic phenotype in Stockholm at the onset, the systemic affection over the course of disease and of survival seems not to be influenced by the diagnosis delay in Stockholm.

Place, publisher, year, edition, pages
Taylor & Francis, 2022
Keywords
amyloid polyneuropathy, Amyloidosis, diagnosis delay, endemic, transthyretin
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-194889 (URN)10.1080/13506129.2022.2065191 (DOI)000786511100001 ()35438016 (PubMedID)2-s2.0-85129232924 (Scopus ID)
Funder
Pfizer AB
Available from: 2022-06-07 Created: 2022-06-07 Last updated: 2023-05-22Bibliographically approved
Schmidt, H. H., Wixner, J., Planté-Bordeneuve, V., Muñoz-Beamud, F., Lladó, L., Gillmore, J. D., . . . Adams, D. (2022). Patisiran treatment in patients with hereditary transthyretin-mediated amyloidosis with polyneuropathy after liver transplantation. American Journal of Transplantation, 22(6), 1646-1657
Open this publication in new window or tab >>Patisiran treatment in patients with hereditary transthyretin-mediated amyloidosis with polyneuropathy after liver transplantation
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2022 (English)In: American Journal of Transplantation, ISSN 1600-6135, E-ISSN 1600-6143, Vol. 22, no 6, p. 1646-1657Article in journal (Refereed) Published
Abstract [en]

Hereditary transthyretin-mediated (hATTR) amyloidosis, or ATTRv amyloidosis, is a progressive disease, for which liver transplantation (LT) has been a long-standing treatment. However, disease progression continues post-LT. This Phase 3b, open-label trial evaluated efficacy and safety of patisiran in patients with ATTRv amyloidosis with polyneuropathy progression post-LT. Primary endpoint was median transthyretin (TTR) reduction from baseline. Twenty-three patients received patisiran for 12 months alongside immunosuppression regimens. Patisiran elicited a rapid, sustained TTR reduction (median reduction [Months 6 and 12 average], 91.0%; 95% CI: 86.1%–92.3%); improved neuropathy, quality of life, and autonomic symptoms from baseline to Month 12 (mean change [SEM], Neuropathy Impairment Score, −3.7 [2.7]; Norfolk Quality of Life-Diabetic Neuropathy questionnaire, −6.5 [4.9]; least-squares mean [SEM], Composite Autonomic Symptom Score-31, −5.0 [2.6]); and stabilized disability (Rasch-built Overall Disability Scale) and nutritional status (modified body mass index). Adverse events were mild or moderate; five patients experienced ≥1 serious adverse event. Most patients had normal liver function tests. One patient experienced transplant rejection consistent with inadequate immunosuppression, remained on patisiran, and completed the study. In conclusion, patisiran reduced serum TTR, was well tolerated, and improved or stabilized key disease impairment measures in patients with ATTRv amyloidosis with polyneuropathy progression post-LT (www.clinicaltrials.gov NCT03862807).

Place, publisher, year, edition, pages
John Wiley & Sons, 2022
Keywords
clinical research/practice, clinical trial, liver allograft function/dysfunction, liver transplantation/hepatology, molecular biology: small interfering RNA, neurology, patient survival, pharmacology
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-193692 (URN)10.1111/ajt.17009 (DOI)000780378600001 ()35213769 (PubMedID)2-s2.0-85127222590 (Scopus ID)
Available from: 2022-05-02 Created: 2022-05-02 Last updated: 2023-05-29Bibliographically 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
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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
Jayaweera, S. W., Surano, S., Pettersson, N., Oskarsson, E., Lettius, L., Gharibyan, A. L., . . . Olofsson, A. (2021). Mechanisms of Transthyretin Inhibition of IAPP Amyloid Formation. Biomolecules, 11(3), Article ID 411.
Open this publication in new window or tab >>Mechanisms of Transthyretin Inhibition of IAPP Amyloid Formation
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2021 (English)In: Biomolecules, E-ISSN 2218-273X, Vol. 11, no 3, article id 411Article in journal, Editorial material (Refereed) Published
Abstract [en]

Amyloid-formation by the islet amyloid polypeptide (IAPP), produced by the β-cells in the human pancreas, has been associated with the development of type II diabetes mellitus (T2DM). The human plasma-protein transthyretin (TTR), a well-known amyloid-inhibiting protein, is interestingly also expressed within the IAPP producing β-cells. In the present study, we have characterized the ability of TTR to interfere with IAPP amyloid-formation, both in terms of its intrinsic stability as well as with regard to the effect of TTR-stabilizing drugs. The results show that TTR can prolong the lag-phase as well as impair elongation in the course of IAPP-amyloid formation. We also show that the interfering ability correlates inversely with the thermodynamic stability of TTR, while no such correlation was observed as a function of kinetic stability. Furthermore, we demonstrate that the ability of TTR to interfere is maintained also at the low pH environment within the IAPP-containing granules of the pancreatic β-cells. However, at both neutral and low pH, the addition of TTR-stabilizing drugs partly impaired its efficacy. Taken together, these results expose mechanisms of TTR-mediated inhibition of IAPP amyloid-formation and highlights a potential therapeutic target to prevent the onset of T2DM.

Place, publisher, year, edition, pages
MDPI, 2021
Keywords
IAPP, TTR, amylin, amyloid, diabetes, islet amyloid polypeptide, thioflavin T, transthyretin
National Category
Basic Medicine
Identifiers
urn:nbn:se:umu:diva-182798 (URN)10.3390/biom11030411 (DOI)000633423800001 ()33802170 (PubMedID)2-s2.0-85103862637 (Scopus ID)
Funder
The Swedish Brain Foundation, FO2018-0334Stiftelsen Olle Engkvist Byggmästare, 199-0469Stiftelsen Gamla Tjänarinnor, 2018-00718
Available from: 2021-05-05 Created: 2021-05-05 Last updated: 2023-09-05Bibliographically approved
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0003-2874-7643

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