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Pilebro, Björn
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Publications (10 of 14) Show all publications
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
Hellman, U., Lång, K., Ihse, E., Jonasson, J., Olsson, M., Lundgren, H.-E., . . . Anan, I. (2019). Transthyretin Glu54Leu - an unknown mutation within the Swedish population associated with amyloid cardiomyopathy and a unique fibril type. Scandinavian Journal of Clinical and Laboratory Investigation, 1-5
Open this publication in new window or tab >>Transthyretin Glu54Leu - an unknown mutation within the Swedish population associated with amyloid cardiomyopathy and a unique fibril type
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2019 (English)In: Scandinavian Journal of Clinical and Laboratory Investigation, ISSN 0036-5513, E-ISSN 1502-7686, p. 1-5Article in journal (Refereed) Epub ahead of print
Abstract [en]

For the first time, we report of a Swedish family of five individuals with a TTR Glu54Leu (p. Glu74Leu) mutation in the transthyretin gene. This mutation has been previously described a few times in the literature, but no phenotypic or clinical description has been done before. The most common mutation in the Swedish population is TTRVal30Met and is mostly found in the Northern part of Sweden. Interestingly, the TTRGlu54Leu mutation was found in the same endemic area. The main phenotype of the TTR Glu54Leu patients is severe cardiomyopathy, which resulted in heart transplantation for the index person. As previously seen for ATTR amyloidosis patients with mainly cardiomyopathy, the amyloid fibrils consisted of a mixture of full-length and fragmented TTR species. However, western blot analyses detected a previously unrecognized band, indicating that these patients may have a third, so far unrecognized, fibril composition type that is distinct from the usual type A band pattern.

Place, publisher, year, edition, pages
Taylor & Francis, 2019
Keywords
Amyloidosis, amyloid fibril, cardiomyopathy, neuropathy, transthyretin
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:umu:diva-160383 (URN)10.1080/00365513.2019.1624977 (DOI)000474016000001 ()31169435 (PubMedID)
Funder
Knut and Alice Wallenberg FoundationVästerbotten County Council
Available from: 2019-06-18 Created: 2019-06-18 Last updated: 2019-07-26
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
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
Pilebro, B., Arvidsson, S., Lindqvist, P., Sundström, T., Westermark, P., Antoni, G., . . . Sörensen, J. (2018). Positron emission tomography (PET) utilizing Pittsburgh compound B (PIB) for detection of amyloid heart deposits in hereditary transthyretin amyloidosis (ATTR). Journal of Nuclear Cardiology, 25(1), 240-248
Open this publication in new window or tab >>Positron emission tomography (PET) utilizing Pittsburgh compound B (PIB) for detection of amyloid heart deposits in hereditary transthyretin amyloidosis (ATTR)
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2018 (English)In: Journal of Nuclear Cardiology, ISSN 1071-3581, E-ISSN 1532-6551, Vol. 25, no 1, p. 240-248Article in journal (Refereed) Published
Abstract [en]

Background: DPD scintigraphy has been advocated for imaging cardiac amyloid in ATTR amyloidosis. PET utilizing 11C-Pittsburgh compound B (PIB) is the gold standard for imaging brain amyloid in Alzheimer’s disease. PIB was recently shown to identify cardiac amyloidosis in both AL and ATTR amyloidosis. In the ATTR population, two types of amyloid fibrils exist, one containing fragmented and full-length TTR (type A) and the other only full-length TTR (type B). The aim of this study was to further evaluate PIB-PET in patients with hereditary ATTR amyloidosis.

Methods: Ten patients with biopsy-proven V30M ATTR amyloidosis and discrete or no signs of cardiac involvement were included. Patients were grouped according to TTR-fragmentation. All underwent DPD scintigraphy, echocardiography, and PIB-PET. A left ventricular PIB-retention index (PIB-RI) was established and compared to five normal volunteers.

Results: PIB-RI was increased in all patients (P < 0.001), but was significantly higher in type B than in type A (0.129 ± 0.041 vs 0.040 ± 0.006 min−1, P = 0.009). Cardiac DPD uptake was elevated in group A and absent in group B.

Conclusion: PIB-PET, in contrast to DPD scintigraphy, has the potential to specifically identify cardiac amyloid depositions irrespective of amyloid fibril composition. The heart appears to be a target organ for amyloid deposition in ATTR amyloidosis.

Place, publisher, year, edition, pages
Springer, 2018
Keywords
Cardiomyopathy, amyloidosis, Pittsburgh compound B
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:umu:diva-127300 (URN)10.1007/s12350-016-0638-5 (DOI)000423585200038 ()27645889 (PubMedID)2-s2.0-84988421982 (Scopus ID)
Available from: 2016-11-07 Created: 2016-11-07 Last updated: 2019-05-21Bibliographically approved
Henein, M. Y., Suhr, O. B., Arvidsson, S., Pilebro, B., Westermark, P., Hörnsten, R. & Lindqvist, P. (2018). Reduced left atrial myocardial deformation irrespective of cavity size: a potential cause for atrial arrhythmia in hereditary transthyretin amyloidosis. Amyloid: Journal of Protein Folding Disorders, 25(1), 46-53
Open this publication in new window or tab >>Reduced left atrial myocardial deformation irrespective of cavity size: a potential cause for atrial arrhythmia in hereditary transthyretin amyloidosis
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2018 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 25, no 1, p. 46-53Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: Cardiac amyloidosis (CA) is a myocardial disease and commonly under-diagnosed condition. In CA patients, atrial fibrillation might occur in the absence of left atrial (LA) enlargement.

OBJECTIVES: The aim of this study is to assess LA size and function, and its relationship with atrial arrhythmia in patients with hereditary transthyretin amyloidosis (ATTR).

METHODS: Forty-six patients with confirmed ATTR amyloidosis on abdominal biopsy were studied. Assessment with 2D echocardiography and 2D strain showed 31 patients had increased LV wall thickness (LVWT) (septal thickness >12 mm), and 15 had normal LVWT. In addition to conventional measurements, LV and LA global longitudinal strain (GLS%) and strain rate (SR) were obtained. Western blot analysis was done to assess fibril type. ATTR patients with increased LVWT were compared with 23 patients with hypertrophic cardiomyopathy (HCM) and 31 healthy controls. ATTR amyloidosis patients also underwent 24 hour Holter monitoring to determine the presence of atrial arrhythmia.

RESULTS: Atrial deformation during atrial systole was reduced in ATTR amyloidosis patients with increased LVWT independent of LA size and in contrast to HCM. Twenty of the ATTR amyloidosis patients (54%) had ECG evidence of significant atrial arrhythmic events. LA strain rate, during atrial systole, was the only independent predictor of atrial arrhythmia (β = 3.28, p = .012).

CONCLUSION: In ATTR cardiomyopathy with increased LVWT, LA myocardial function is abnormal, irrespective of atrial cavity size. Reduced LA myocardial SR during atrial systole, irrespective of cavity volume, E/e' and LV deformation, is also a strong predictor for atrial arrhythmic events.

Place, publisher, year, edition, pages
Taylor & Francis, 2018
Keywords
Arrhythmia, Holter ECG, deformation echocardiography, left atrial function
National Category
Other Clinical Medicine
Identifiers
urn:nbn:se:umu:diva-145431 (URN)10.1080/13506129.2018.1430027 (DOI)000428570300007 ()29369708 (PubMedID)
Available from: 2018-03-05 Created: 2018-03-05 Last updated: 2019-05-17Bibliographically 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
Pilebro, B. (2017). The heart in hereditary transthyretin amyloidosis: clinical studies on the impact of amyloid fibril composition. (Doctoral dissertation). Umeå: Umeå University
Open this publication in new window or tab >>The heart in hereditary transthyretin amyloidosis: clinical studies on the impact of amyloid fibril composition
2017 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Background Hereditary transthyretin amyloid (ATTRm) amyloidosis is a systemic disease mainly affecting the peripheral nervous system and the heart. The disease is inherited in an autosomal dominant manner with a varying penetrance. It is caused by mutations in the transthyretin (TTR) gene. Today more than 100 disease causing mutations are known. The V30M mutation that is endemic in northern Sweden is the best studied and comprises the majority of the reported disease cases in the world. In ATTRm amyloidosis caused by the V30M mutation two distinct sub populations are seen, one with disease onset early in life and a mainly neuropathic disease and the other with late onset disease and both neuropathic disease and a progressive cardiomyopathy. These phenotypical findings have in Swedish patients been tied to differences in amyloid fibril composition. Generally, patients with early onset disease have amyloid fibrils containing only full length transthyretin (type B) whereas patients with late onset disease have amyloid containing both full length and fragmented transthyretin (type A). Until recently, the only available treatment for the disease has been liver transplantation. Patients with type A fibrils, especially males, have significantly worse survival after liver transplant due to progressive amyloid cardiomyopathy. Furthermore, it appears that type A fibrils may be the most common finding in other mutations.

This thesis work aims to in depth investigate the impact amyloid fibril composition has on cardiac manifestations of the disease and on the outcome of available and novel modalities for cardiac amyloid imaging.

Methods The four studies included in the thesis were done as part of the on going clinical research at the Swedish centre for transthyretin amyloidosis in Umeå.  Patients in whom amyloid fibril composition had been determined were included. Available echocardiographic data were analysed to find predictors for left ventricular hypertrophy and systolic function as measured by strain analysis in a large cohort of 105 patients (paper I). Serial 12-lead electrocardiograms from 98 patients were gathered and retrospectively interpreted and analysed to investigate the impact of amyloid fibril composition and disease progression on frequency and development of ECG abnormalities (paper IV).  DPD scintigraphy, cardiac biomarkers, clinical data and echocardiograms were analysed in a cohort of 53 consecutive patients. to assess the impact of amyloid fibril composition on the outcome of DPD scintigraphy and its relationship with cardiac hypertrophy. (paper II). To evaluate the usefulness of positron emission tomography (PET) using the amyloid specific tracer PIB, 10 patients, five with each fibril type, were selected and examined. The patients selected had a similar age of onset and similar echocardiographic findings (paper III).

Results Paper I: Type A fibrils, male gender and age were independent factors associated with increased LV thickness. The distribution of amyloid fibril composition did not differ between the sexes, but in patients with type A fibrils, females had lower median cardiac wall thickness (p<0.01and better left ventricular septal strain (p=0.04).The gender differences were not apparent in patients with type B fibrils.

Paper II: Ninety-seven per cent of patients with type A fibrils had pathological cardiac DPD uptake compared to none of the patients with type B fibrils. Among patients with normal septal thickness, none of 15 patients with type B fibrils had positive scintigraphy compared with 2 out of 2 with type A fibrils (P<0.01) Cardiac biomarkers, demographic data and cardiac biomarkers were significantly different, but could not differentiate between type A and type B fibrils in individual patients.

Paper III: All patients had pathological cardiac PIB retention. In patients with type B fibrils the retention was significantly higher (p<0.01) than in patients with type A fibrils. Based on the selection criteria, no significant differences were seen in various echocardiographic measurements.

Paper IV: All patients had a high prevalence of AV-blocks, LAH and anterior infarction pattern. Patients with type A fibrils had significantly more electrocardiographic abnormalities compared to those with type B fibrils, both at an early stage of diseases and at later follow up.

Conclusion Type A fibrils are associated with more pronounced cardiac involvement, which appear to be more severe in males than in females. In study II we showed that DPD scintigraphy appears to be a very good tool for non-invasive determination of amyloid fibril composition. Papers III and IV show that patients with type B amyloid have cardiac involvement even without echocardiographic or DPD-scintigraphic evidence of amyloid cardiomyopathy and that ECG abnormalities are common irrespectively of amyloid fibril composition, and increase with time for both groups. 

Place, publisher, year, edition, pages
Umeå: Umeå University, 2017. p. 55
Series
Umeå University medical dissertations, ISSN 0346-6612 ; 1904
Keywords
Amyloidosis, Transthyretin, Cardiomyopathy, Echocardiography, Scintigraphy, Positron emission tomography
National Category
Cardiac and Cardiovascular Systems
Research subject
Medicine, cardiovascular disease; Cardiology; Clinical Physiology
Identifiers
urn:nbn:se:umu:diva-139495 (URN)978-91-7601-745-6 (ISBN)
Public defence
2017-10-06, Sal D, 9 tr, Norrlands universitetssjukhus, Umeå, 17:00 (Swedish)
Opponent
Supervisors
Funder
Swedish Heart Lung Foundation
Available from: 2017-09-15 Created: 2017-09-14 Last updated: 2018-06-09Bibliographically 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
Pilebro, B., Suhr, O. B., Näslund, U., Westermark, P., Lindqvist, P. & Sundström, T. (2016). 99mTC-DPD uptake reflects amyloid fibril composition in hereditary transthyretin amyloidosis. Upsala Journal of Medical Sciences, 121(1), 17-24
Open this publication in new window or tab >>99mTC-DPD uptake reflects amyloid fibril composition in hereditary transthyretin amyloidosis
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2016 (English)In: Upsala Journal of Medical Sciences, ISSN 0300-9734, E-ISSN 2000-1967, Vol. 121, no 1, p. 17-24Article in journal (Refereed) Published
Abstract [en]

Aims In transthyretin amyloid (ATTR) amyloidosis various principal phenotypes have been described: cardiac, neuropathic, or a mixed cardiac and neuropathic. In addition, two different types of amyloid fibrils have been identified (type A and type B). Type B fibrils have thus far only been found in predominantly early-onset V30M and in patients carrying the Y114C mutation, whereas type A is noted in all other mutations currently examined as well as in wild-type ATTR amyloidosis. The fibril type is a determinant of the ATTR V30M disease phenotype. Tc-99m-DPD scintigraphy is a highly sensitive method for diagnosing heart involvement in ATTR amyloidosis. The objective of this study was to determine the relationship between ATTR fibril composition and Tc-99m-DPD scintigraphy outcome in patients with biopsy-proven ATTR amyloidosis. Methods Altogether 55 patients with biopsy-proven diagnosis of ATTR amyloidosis and amyloid fibril composition determined were examined by Tc-99m-DPD scintigraphy. The patients were grouped and compared according to their type of amyloid fibrils. Cardiovascular evaluation included ECG, echocardiography, and cardiac biomarkers. The medical records were scrutinized to identify subjects with hypertension or other diseases that have an impact on cardiac dimensions. Results A total of 97% with type A and none of the patients with type B fibrils displayed Tc-99m-DPD uptake at scintigraphy (p < 0.001). Findings from analyses of cardiac biomarkers, ECG, and echocardiography, though significantly different, could not differentiate between type A and B fibrils in individual patients. Conclusion In ATTR amyloidosis, the outcome of Tc-99m-DPD scintigraphy is strongly related to the patients' transthyretin amyloid fibril composition.

Place, publisher, year, edition, pages
Taylor & Francis, 2016
Keywords
transthyretin, Amyloidosis hereditary, echocardiography, scintigraphy, amyloid cardiomyopathy
National Category
Clinical Medicine
Identifiers
urn:nbn:se:umu:diva-119085 (URN)10.3109/03009734.2015.1122687 (DOI)000372123700003 ()26849806 (PubMedID)
Available from: 2016-04-19 Created: 2016-04-11 Last updated: 2018-06-07Bibliographically approved
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