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Publications (10 of 17) Show all publications
Anan, I., Bång, J., Lundgren, H.-E., Wixner, J. & Westermark, P. (2019). A case report of osteoarthritis associated with hereditary transthyretin amyloidosis ATTRV30M. Paper presented at 16th International Symposium on Amyloidosis (ISA), Kumamoto, JAPAN, March 26-29, 2018.. Amyloid: Journal of Protein Folding Disorders, 26, 29-30
Open this publication in new window or tab >>A case report of osteoarthritis associated with hereditary transthyretin amyloidosis ATTRV30M
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2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, p. 29-30Article in journal (Refereed) Published
Place, publisher, year, edition, pages
Taylor & Francis, 2019
National Category
Rheumatology and Autoimmunity
Identifiers
urn:nbn:se:umu:diva-162352 (URN)10.1080/13506129.2019.1593132 (DOI)000477775700017 ()31343355 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), Kumamoto, JAPAN, March 26-29, 2018.
Note

Special Issue. Supplement 1.

Available from: 2019-08-16 Created: 2019-08-16 Last updated: 2019-08-27Bibliographically approved
Suhr, O. B., Wixner, J., Anan, I., Lundgren, H.-E., Wijayatunga, P., Westermark, P. & Ihse, E. (2019). Amyloid fibril composition within hereditary Val30Met (p. Val50Met) transthyretin amyloidosis families. PLoS ONE, 14(2), Article ID e0211983.
Open this publication in new window or tab >>Amyloid fibril composition within hereditary Val30Met (p. Val50Met) transthyretin amyloidosis families
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2019 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 14, no 2, article id e0211983Article in journal (Refereed) Published
Abstract [en]

Background: The amyloid fibril in hereditary transthyretin (TTR) Val30Met (pVal50Met) amyloid (ATTR Val30Met) amyloidosis is composed of either a mixture of full-length and TTR fragments (Type A) or of only full-length TTR (Type B). The type of amyloid fibril exerts an impact on the phenotype of the disease, and on the outcome of diagnostic procedures and therapy. The aim of the present study was to investigate if the type of amyloid fibril remains the same within ATTR Val30Met amyloidosis families. Methods: Fifteen families were identified in whom at least two first-degree relatives had their amyloid fibril composition determined. The type of ATTR was determined by Western blot in all but two patients. For these two patients a positive 99mTc-3,3-diphosphono-1,2-propanodicarboxylic acid scintigraphy indicated ATTR Type A. Results: In 14 of the 15 families, the same amyloid fibril composition was noted irrespective of differences in age at onset. In the one family, different ATTR fibril types was found in two brothers with similar ages at onset. Conclusions: Family predisposition appears to have an impact on amyloid fibril composition in members of the family irrespective of their age at onset of disease, but if genetically determined, the gene/genes are likely to be situated at another location than the TTR gene in the genome.

Place, publisher, year, edition, pages
Public Library Science, 2019
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-157583 (URN)10.1371/journal.pone.0211983 (DOI)000459806400043 ()30811423 (PubMedID)
Available from: 2019-04-01 Created: 2019-04-01 Last updated: 2019-04-01Bibliographically approved
Marberg, T., Karling, P., Söderberg, K., Anan, I. & Wixner, J. (2019). Self-reported gastrointestinal symptoms are more common in liver transplanted transthyretin amyloidosis patients than in healthy controls and in patients transplanted for end-stage liver disease. Paper presented at 16th International Symposium on Amyloidosis (ISA), Kumamoto, Japan, March 26-29, 2018. Amyloid: Journal of Protein Folding Disorders, 26, 47-48
Open this publication in new window or tab >>Self-reported gastrointestinal symptoms are more common in liver transplanted transthyretin amyloidosis patients than in healthy controls and in patients transplanted for end-stage liver disease
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2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, p. 47-48Article in journal (Refereed) Published
Place, publisher, year, edition, pages
Taylor & Francis, 2019
National Category
Gastroenterology and Hepatology
Identifiers
urn:nbn:se:umu:diva-162351 (URN)10.1080/13506129.2019.1582514 (DOI)000477775700026 ()31343318 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), Kumamoto, Japan, March 26-29, 2018
Note

Special issue, Supplement 1

Available from: 2019-08-16 Created: 2019-08-16 Last updated: 2019-08-27Bibliographically approved
Wixner, J., Westermark, P., Ihse, E., Pilebro, B., Lundgren, H.-E. & Anan, I. (2019). The Swedish open-label diflunisal trial (DFNS01) on hereditary transthyretin amyloidosis and the impact of amyloid fibril composition [Letter to the editor]. Paper presented at 16th International Symposium on Amyloidosis (ISA), Kumamoto, Japan, March 26-29, 2018.. Amyloid: Journal of Protein Folding Disorders, 26, 39-40
Open this publication in new window or tab >>The Swedish open-label diflunisal trial (DFNS01) on hereditary transthyretin amyloidosis and the impact of amyloid fibril composition
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2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, p. 39-40Article in journal, Letter (Refereed) Published
Place, publisher, year, edition, pages
Taylor & Francis Group, 2019
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-162491 (URN)10.1080/13506129.2019.1593133 (DOI)000477775700022 ()31343354 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), Kumamoto, Japan, March 26-29, 2018.
Note

Special Issue, Supplement 1.

Available from: 2019-08-26 Created: 2019-08-26 Last updated: 2019-08-27Bibliographically approved
Unéus, E., Wilhelmsson, C., Suhr, O., Anan, I., Wixner, J., Pilebro, B., . . . Sundström, T. (2019). Visualisation of amyloid deposition within the brain of long-term hereditary transthyretin amyloidosis survivors by 18F-flutemetamol positron emission tomography. Paper presented at 5th Congress of the European Academy of Neurology (EAN), June 29 – July 2, 2019, Oslo, Norway. European Journal of Neurology, 26(S1), 287-287, Article ID EPR3027.
Open this publication in new window or tab >>Visualisation of amyloid deposition within the brain of long-term hereditary transthyretin amyloidosis survivors by 18F-flutemetamol positron emission tomography
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2019 (English)In: European Journal of Neurology, ISSN 1351-5101, E-ISSN 1468-1331, Vol. 26, no S1, p. 287-287, article id EPR3027Article in journal, Meeting abstract (Other academic) Published
Abstract [en]

Background and aims: Hereditary transthyretin amyloid (ATTRv) amyloidosis caused by the transthyretin (TTR) Val30Met (p.V50M) mutation is characterised by peripheral neuropathy, and central nervous (CNS) complications has rarely been reported. However, liver transplantation has prolonged the patients’ survival, and CNS complications attributed to amyloid angiopathy caused by CNS synthesis of variant TTR have been reported. The aim of the study was to ascertain CNS amyloid deposition in long-term ATTRv survivors.

Methods: 20 ATTR Val30Met patients with symptoms from the CNS and a median disease duration of 16 years (9-25 years) together with five Alzheimer (AD) patients, who served as positive controls were included in the study. Amyloid CNS deposits were assessed by 18F- flutemetamol PET/CT examination utilising relative z scores with pons as reference.

Results: Expectedly, all Alzheimer patients had an clearly increased global composite z score above 2.0 compared with 55% of the ATTRv patients. There was an increased local uptake corresponding to cerebellum in 12 ATTRv patients compared to only one in the AD group (fig 1). Four of these ATTRv patients had a global composite z score within the normal range. No correlation between duration after 9 years and amyloid CNS deposition was noted.

Conclusion: Amyloid deposition within the brain after long-standing ATTRv amyloidosis is increased and is often noted in the cerebellum. However, not all patient display amyloid CNS deposition, thus, additional causes for CNS complications should always be considered.

Place, publisher, year, edition, pages
John Wiley & Sons, 2019
National Category
Neurology
Identifiers
urn:nbn:se:umu:diva-161913 (URN)10.1111/ene.14018 (DOI)000474481001092 ()
Conference
5th Congress of the European Academy of Neurology (EAN), June 29 – July 2, 2019, Oslo, Norway
Available from: 2019-08-12 Created: 2019-08-12 Last updated: 2019-08-12Bibliographically approved
Wixner, J., Törnblom, H., Karling, P., Anan, I. & Lindberg, G. (2018). Abnormal small bowel motility in patients with hereditary transthyretin amyloidosis. Neurogastroenterology and Motility, 30(9), Article ID e13354.
Open this publication in new window or tab >>Abnormal small bowel motility in patients with hereditary transthyretin amyloidosis
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2018 (English)In: Neurogastroenterology and Motility, ISSN 1350-1925, E-ISSN 1365-2982, Vol. 30, no 9, article id e13354Article in journal (Refereed) Published
Abstract [en]

Background: Gastrointestinal complications are common in hereditary transthyretin amyloid (ATTRm) amyloidosis. The underlying mechanisms have not been fully elucidated, and the patients' small bowel function remains largely unexplored. The aim of the present study was to compare the small bowel motility in ATTRm amyloidosis patients with that in non-amyloidosis patient controls.

Methods: ATTRm amyloidosis patients undergoing evaluation for liver transplantation were consecutively investigated with 24-hour duodenojejunal manometry (n=19). The somatostatin analogue octreotide was used to induce fasting motility. Patients with age at onset of 50years were defined as late-onset cases. For each patient, three age- and sex-matched patient controls (n=57) were selected from the total pool of investigated patients.

Key Results: Manometry was judged as abnormal in 58% of the patients and in 26% of the patient controls (P=.01). Patients displayed significantly more daytime phase III migrating motor complexes than patient controls (median 4 vs 2, P<.01), and had a higher frequency of low-amplitude complexes (16% vs 4%; however, this difference did not reach statistical significance, P=.10). Furthermore, late-onset patients showed a delay in octreotide response (5.4 vs 3.8minutes, P<.01), but this was not observed for early-onset patients or within the control group.

Conclusions and Inferences: Patients with ATTRm amyloidosis displayed abnormalities in their small bowel motility more frequently than non-amyloidosis patient controls, and the manometric pattern was probably best consistent with a combined neuromyopathic disorder. The delayed octreotide response in late-onset patients warrants further investigation.

Place, publisher, year, edition, pages
Wiley-Blackwell, 2018
Keywords
familial amyloid neuropathy, functional gastrointestinal disorders, intestinal motility, manometry, octreotide acetate, transthyretin amyloidosis
National Category
Gastroenterology and Hepatology
Identifiers
urn:nbn:se:umu:diva-152414 (URN)10.1111/nmo.13354 (DOI)000445193400010 ()29655299 (PubMedID)
Available from: 2018-10-05 Created: 2018-10-05 Last updated: 2019-05-16Bibliographically approved
Wange, N., Anan, I., Ericzon, B.-G., Pennlert, J., Pilebro, B., Suhr, O. B. & Wixner, J. (2018). Atrial Fibrillation and Central Nervous Complications in Liver Transplanted Hereditary Transthyretin Amyloidosis Patients. Transplantation, 102(2), e59-e66
Open this publication in new window or tab >>Atrial Fibrillation and Central Nervous Complications in Liver Transplanted Hereditary Transthyretin Amyloidosis Patients
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2018 (English)In: Transplantation, ISSN 0041-1337, E-ISSN 1534-6080, Vol. 102, no 2, p. e59-e66Article in journal (Refereed) Published
Abstract [en]

Background. Central nervous system (CNS) complications are increasingly noted in liver transplanted (LTx) hereditary transthyretin amyloid (ATTRm) amyloidosis patients; this suggests that the increased survival allows for intracranial ATTRm formation from brain synthesized mutant TTR. However, atrial fibrillation (AF), a recognised risk factor for ischemic CNS complications, is also observed after LTx. The aim of the study was to investigate the occurrence of CNS complications and AF in LTx ATTRm amyloidosis patients. Methods. The medical records of all LTx ATTRm amyloidosis patients in the county of Vasterbotten, Sweden, were investigated for information on CNS complications, AF, anticoagulation (AC) therapy, hypertension, cardiac ischemic disease, hypertrophy, and neurological status. Results. Sixty-three patients that had survived for 3 years or longer after LTx were included in the analysis. Twenty-five patients had developed 1 or more CNS complications at a median of 21 years after onset of disease. AF was noted in 21 patients (median time to diagnosis 24 years). Cerebrovascular events (CVE) developed in 17 (median time to event 21 years). CVEs occurred significantly more often in patients with AF (P < 0.002). AC therapy significantly reduced CVEs, including bleeding in patients with AF (P = 0.04). Multivariate analysis identified AF as the only remaining regressor with a significant impact on CVE (hazard ratio, 3.8; 95% confidence interval 1.1-9.5; P = 0.029). Conclusions. AF is an important risk factor for CVE in LTx ATTRm amyloidosis patients, and AC therapy should be considered. However, the increased bleeding risk with AC therapy in patients with intracranial amyloidosis should be acknowledged.

Place, publisher, year, edition, pages
LIPPINCOTT WILLIAMS & WILKINS, 2018
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:umu:diva-144941 (URN)10.1097/TP.0000000000001975 (DOI)000424093400004 ()29019809 (PubMedID)
Available from: 2018-02-23 Created: 2018-02-23 Last updated: 2019-05-21Bibliographically approved
Wixner, J., Suhr, O. B. & Anan, I. (2018). Management of gastrointestinal complications in hereditary transthyretin amyloidosis: a single-center experience over 40 years. Expert Review of Gastroenterology & Hepatology, 12(1), 73-81
Open this publication in new window or tab >>Management of gastrointestinal complications in hereditary transthyretin amyloidosis: a single-center experience over 40 years
2018 (English)In: Expert Review of Gastroenterology & Hepatology, ISSN 1747-4124, E-ISSN 1747-4132, Vol. 12, no 1, p. 73-81Article, review/survey (Refereed) Published
Abstract [en]

Introduction: Hereditary transthyretin amyloidosis (ATTRm amyloidosis) is a rare disease caused by the deposition and accumulation of insoluble non-native transthyretin fibrils in the body. The disease inevitably results in widespread organ disruption, and poor life expectancy. The GI tract is one organ system vulnerable to disruption and, although the clinical presentation of the disease varies, GI involvement affects most patients with ATTRm amyloidosis.

Areas covered: This article presents our experience with diagnosing and treating the GI symptoms of ATTRm amyloidosis patients at our center over the last 40 years, in the Swedish clustering area of the disease. Our aim is to help other physicians to better manage GI complications in patients with this rare but widespread condition.

Expert commentary: GI symptoms are debilitating complications for ATTRm amyloidosis patients to experience, yet with the appropriate questioning and diagnosis methods, symptomatic treatments of these symptoms can be implemented to provide relief. Further, patients with fewer GI complications and a good nutritional status are also better candidates for liver transplantation which, in selected cases, is the best disease-modifying treatment of ATTRm amyloidosis to date.

Place, publisher, year, edition, pages
Taylor & Francis, 2018
Keywords
amyloidosis, familial amyloid neuropathy, gastric emptying, gastrointestinal tract, liver, therapeutics, ansthyretin
National Category
Gastroenterology and Hepatology
Identifiers
urn:nbn:se:umu:diva-146467 (URN)10.1080/17474124.2018.1397511 (DOI)000427553900008 ()29073801 (PubMedID)
Available from: 2018-04-10 Created: 2018-04-10 Last updated: 2019-05-16Bibliographically approved
Wixner, J., Pilebro, B., Lundgren, H.-E., Olsson, M. & Anan, I. (2017). Effect of doxycycline and ursodeoxycholic acid on transthyretin amyloidosis. Amyloid: Journal of Protein Folding Disorders, 24(1), 78-79
Open this publication in new window or tab >>Effect of doxycycline and ursodeoxycholic acid on transthyretin amyloidosis
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2017 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 24, no 1, p. 78-79Article in journal, Meeting abstract (Refereed) Published
Abstract [en]

Doxycycline has been shown to disrupt transthyretin amyloid (ATTR) fibrils [1] and tauro-ursodeoxycholic acid (TUDCA) has been shown to reduce TTR toxic aggregates in mice [2]. Further, in 2010 Cardoso et al. showed that a combined doxycycline/TUDCA treatment had a synergistic effect, decreasing ATTR deposition. Ursodeoxycholic acid (UDCA) is a bile acid used for the treatment of certain cholestatic syndromes with an efficacy similar to that of TUDCA. Based on this knowledge, we wanted to explore if treatment with doxycycline and UDCA (Dox/Urso) would prevent disease progression in ATTR amyloidosis. UDCA was selected since TUDCA is not available in Sweden.

National Category
Rheumatology and Autoimmunity
Identifiers
urn:nbn:se:umu:diva-134748 (URN)10.1080/13506129.2016.1269739 (DOI)000399943700041 ()28042702 (PubMedID)
Available from: 2017-05-11 Created: 2017-05-11 Last updated: 2019-05-21Bibliographically approved
Suhr, O. B., Wixner, J., Pilebro, B., Lundgren, H.-E. & Anan, I. (2017). The Swedish landscape of hereditary ATTR amyloidosis. Amyloid: Journal of Protein Folding Disorders, 24(1), 93-94
Open this publication in new window or tab >>The Swedish landscape of hereditary ATTR amyloidosis
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2017 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 24, no 1, p. 93-94Article in journal, Meeting abstract (Refereed) Published
Abstract [en]

Northern Sweden is a well-known clustering area for hereditary transthyretin (TTR) amyloid (ATTR) amyloidosis caused by the Val30Met mutation. However, several additional mutations have been found in the Swedish population, of which many, such as the Ala45Ser, Gly57Arg and His88Arg mutations, have not been reported outside of Sweden to the best of our knowledge. We aim to give an overview of the various mutations found in the Swedish population.

National Category
Medical Genetics
Identifiers
urn:nbn:se:umu:diva-134749 (URN)10.1080/13506129.2017.1286580 (DOI)000399943700049 ()28434364 (PubMedID)
Available from: 2017-05-11 Created: 2017-05-11 Last updated: 2019-05-21Bibliographically approved
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ORCID iD: ORCID iD iconorcid.org/0000-0002-1536-1277

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