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BETA
Lundgren, Hans-Erik
Alternative names
Publications (10 of 12) 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
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
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
Hellman, U., Lundgren, H.-E., Westermark, P., Stafberg, C., Nahi, H., Tachlinski, S., . . . Suhr, O. B. (2015). A genealogical and clinical study of the phenotypical variation within the Swedish transthyretin His88Arg (p. His108Arg) amyloidosis family. European Journal of Medical Genetics, 58(4), 211-215
Open this publication in new window or tab >>A genealogical and clinical study of the phenotypical variation within the Swedish transthyretin His88Arg (p. His108Arg) amyloidosis family
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2015 (English)In: European Journal of Medical Genetics, ISSN 1769-7212, E-ISSN 1878-0849, Vol. 58, no 4, p. 211-215Article in journal (Refereed) Published
Abstract [en]

In 2005 we reported the first case of transthyretin His88Arg (p. His108Arg) amyloidosis, a mutation characterised by cardiomyopathy. Six additional gene carriers of whom five have clinical symptoms of disease have now been identified in Sweden, and we have been able to identify a possible founder and to characterise the Swedish phenotype of the transthyretin (TTR) His88Arg mutation. Genealogical studies of church records were used to identify the individuals with the disease and their families. Routine clinical investigations of neurological and heart manifestation of the disease were utilised. We found that genealogically all seven individuals were related and originated from the same region in Sweden. Amyloid deposits were demonstrated in biopsies and the TTR His88Arg mutation was identified in all patients. Patients had a late onset disease (similar to 50 years of age) and all exhibited a severe amyloid cardiomyopathy. A pronounced peripheral axonal neuropathy was with certainty demonstrated in one patient only, who also was operated for a magnetic resonance confirmed spinal stenosis, however, without any effect on his neurological symptoms. Five of the patients had carpal tunnel syndrome. The first reported case is now deceased from cardiac failure. One patient has had a sequential heart and liver transplantation. One gene carrier had no symptoms or findings of disease on latest evaluation at the age of 44. In conclusion: the Swedish TTRHis88Arg patients all have a common Swedish founder. Cardiomyopathy with heart failure, as well as carpal tunnel syndrome and spinal stenosis were early signs of disease; but peripheral neuropathy was present in one patient before symptoms of cardiomyopathy so the phenotypical presentation of this mutation is variable.

Keywords
Amyloidosis-hereditary, Cardiomyopathy, Genealogy, Neuropathy, Transthyretin
National Category
Medical Genetics
Identifiers
urn:nbn:se:umu:diva-106370 (URN)10.1016/j.ejmg.2015.02.005 (DOI)000353995500003 ()25721874 (PubMedID)
Available from: 2015-07-15 Created: 2015-07-14 Last updated: 2018-06-07Bibliographically approved
Suhr, O. B., Andersen, O., Aronsson, T., Jonasson, J., Kalimo, H., Lundahl, C., . . . Westermark, P. (2009). Report of five rare or previously unknown amyloidogenic transthyretin mutations disclosed in Sweden.. Amyloid: Journal of Protein Folding Disorders, 16(4), 208-214
Open this publication in new window or tab >>Report of five rare or previously unknown amyloidogenic transthyretin mutations disclosed in Sweden.
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2009 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 16, no 4, p. 208-214Article in journal (Refereed) Published
Abstract [en]

The number of amyloidogenic transthyretin (TTR) mutations described in the literature is more than 100. However, for several mutations, the phenotype has been described in a few individuals only; thus, the knowledge of the clinical course and the outcome after therapeutical interventions such as liver transplantation is limited. We describe the phenotype associated with five rare amyloidogenic TTR mutations that lately were discovered in Sweden: ATTR Val30Leu, Ala45Ser, Leu55Gln, Gly57Arg and Tyr69His of which ATTR Gly57Arg is previously unknown. The symptoms at onset differed, but cardiomyopathy and peripheral neuropathy were observed in all except the ATTR Tyr69His mutation. Likewise, carpal tunnel syndrome was found or had been present in all cases except the case with the ATTR Val30Leu mutation. The phenotype of the ATTR Tyr69His mutation was characterised by oculo-meningeal symptoms with seizures and a steadily progressing dementia, symptoms rarely found in ATTR amyloidosis, but similar to those previously described for this mutation, where all cases appear to originate from one Swedish family. Two patients with the ATTR Leu55Gln and Ala45Ser mutations have been subjected to liver transplantation, but echocardiographic examination has revealed an increasing cardiomyopathy after transplantation in both cases, the ATTR Leu55Gln patient succumbed 2 years after transplantation from progressive disease.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:umu:diva-32414 (URN)10.3109/13506120903421587 (DOI)19922332 (PubMedID)
Available from: 2010-03-11 Created: 2010-03-11 Last updated: 2018-06-08Bibliographically approved
Hellman, U., Alarcon, F., Lundgren, H.-E., Suhr, O. B., Bonaiti-Pellié, C. & Planté-Bordeneuve, V. (2008). Heterogeneity of penetrance in familial amyloid polyneuropathy, ATTR Val30Met, in the Swedish population.. Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, 15(3), 181-6
Open this publication in new window or tab >>Heterogeneity of penetrance in familial amyloid polyneuropathy, ATTR Val30Met, in the Swedish population.
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2008 (English)In: Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis, ISSN 1744-2818, Vol. 15, no 3, p. 181-6Article in journal (Refereed) Published
Abstract [en]

Transthyretin (TTR) familial amyloid polyneuropathies (FAP) are autosomal dominant devastating afflictions. They were first described in Portugal, later in Japan and Sweden and are now recognized worldwide. The TTR Val30Met mutation is the most common, and depending on the geographic origin, a wide variation in age at onset of the disease is observed. In Europe, northern Sweden is the second most prevalent area of the disease, and a late age of onset of 56 years has been reported. The present study aims to estimate the penetrance in TTR Val30Met Swedish families. Genealogical investigations, clinical data and genotyping were obtained in 77 TTR-Val30Met Swedish families. The penetrance in Val30Met carriers and variation within the endemic area, according to gender and transmitting parents were calculated by a newly developed bias-free method. The penetrance estimates were low, i.e. 1.7% and 22% at age 30 and 60 years, respectively, and far from complete (69%) by age 90 years. Differences between Piteå and Skellefteå regions were observed. Moreover, penetrance was significantly higher when the mutation was inherited from the mother than from the father. The low penetrance observed in TTR FAP kindreds and its variations is important information for the genetic counseling and treatment of Swedish FAP patients and their families.

Identifiers
urn:nbn:se:umu:diva-19462 (URN)10.1080/13506120802193720 (DOI)18925456 (PubMedID)
Available from: 2009-03-05 Created: 2009-03-05 Last updated: 2018-06-09
Holmgren, G., Hellman, U., Anan, I., Lundgren, H.-E., Jonasson, J., Stafberg, C., . . . Suhr, O. B. (2005). Cardiomyopathy in Swedish patients with the Gly53Glu and His88Arg transthyretin variants.. Amyloid, 12(3), 184-8
Open this publication in new window or tab >>Cardiomyopathy in Swedish patients with the Gly53Glu and His88Arg transthyretin variants.
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2005 (English)In: Amyloid, ISSN 1350-6129, Vol. 12, no 3, p. 184-8Article in journal (Refereed) Published
Identifiers
urn:nbn:se:umu:diva-14698 (URN)10.1080/13506120500223126 (DOI)16194874 (PubMedID)
Available from: 2007-09-14 Created: 2007-09-14 Last updated: 2018-06-09Bibliographically approved
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