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Westermark, Per
Alternative names
Publications (10 of 110) 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), MAR 26-29, 2018, Kumamoto, JAPAN. Amyloid: Journal of Protein Folding Disorders, 26(Suppl. 1), 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, no Suppl. 1, p. 29-30Article in journal (Refereed) Published
Place, publisher, year, edition, pages
TAYLOR & FRANCIS LTD, 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:uu:diva-392892 (URN)10.1080/13506129.2019.1593132 (DOI)000477775700017 ()31343355 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN
Available from: 2019-09-24 Created: 2019-09-24 Last updated: 2019-09-24Bibliographically 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.

National Category
Clinical Laboratory Medicine
Research subject
Pathology
Identifiers
urn:nbn:se:uu:diva-380618 (URN)10.1371/journal.pone.0211983 (DOI)000459806400043 ()30811423 (PubMedID)
Available from: 2019-03-29 Created: 2019-03-29 Last updated: 2019-04-12Bibliographically approved
Bellotti, V., Merlini, G. & Westermark, P. (2019). Biographical item "Robert Kisilevsky, Md, Phd, 1937-2019 In Memoriam", in Amyloid: The Journal of Protein Folding Disorders Volume 26, 2019, Issue 4, p 179.. , 26(4)
Open this publication in new window or tab >>Biographical item "Robert Kisilevsky, Md, Phd, 1937-2019 In Memoriam", in Amyloid: The Journal of Protein Folding Disorders Volume 26, 2019, Issue 4, p 179.
2019 (English)Other (Other (popular science, discussion, etc.))
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:uu:diva-398529 (URN)10.1080/13506129.2019.1660158 (DOI)000484996900001 ()31482745 (PubMedID)
Available from: 2019-12-06 Created: 2019-12-06 Last updated: 2019-12-06Bibliographically approved
Liberta, F., Loerch, S., Rennegarbege, M., Schierhorn, A., Westermark, P., Westermark, G., . . . Schmidt, M. (2019). Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids. Nature Communications, 10, Article ID 1104.
Open this publication in new window or tab >>Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids
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2019 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 1104Article in journal (Refereed) Published
Abstract [en]

Systemic AA amyloidosis is a worldwide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from the acute phase protein serum amyloid A. Here, we report the purification and electron cryo-microscopy analysis of amyloid fibrils from a mouse and a human patient with systemic AA amyloidosis. The obtained resolutions are 3.0 angstrom and 2.7 angstrom for the murine and human fibril, respectively. The two fibrils differ in fundamental properties, such as presence of right-hand or left-hand twisted cross-beta sheets and overall fold of the fibril proteins. Yet, both proteins adopt highly similar beta-arch conformations within the N-terminal similar to 21 residues. Our data demonstrate the importance of the fibril protein N-terminus for the stability of the analyzed amyloid fibril morphologies and suggest strategies of combating this disease by interfering with specific fibril polymorphs.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP, 2019
National Category
Cell and Molecular Biology Clinical Laboratory Medicine
Research subject
Pathology
Identifiers
urn:nbn:se:uu:diva-379892 (URN)10.1038/s41467-019-09033-z (DOI)000460510000001 ()30846696 (PubMedID)
Funder
EU, Horizon 2020German Research Foundation (DFG), FA 456/15-1German Research Foundation (DFG), SCHM 3276/1
Available from: 2019-03-25 Created: 2019-03-25 Last updated: 2019-03-29Bibliographically approved
Schmidt, M., Wiese, S., Adak, V., Engler, J., Agarwal, S., Fritz, G., . . . Fändrich, M. (2019). Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis. Nature Communications, 10, Article ID 5008.
Open this publication in new window or tab >>Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis
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2019 (English)In: Nature Communications, ISSN 2041-1723, E-ISSN 2041-1723, Vol. 10, article id 5008Article in journal (Refereed) Published
Abstract [en]

ATTR amyloidosis is one of the worldwide most abundant forms of systemic amyloidosis. The disease is caused by the misfolding of transthyretin protein and the formation of amyloid deposits at different sites within the body. Here, we present a 2.97 angstrom cryo electron microscopy structure of a fibril purified from the tissue of a patient with hereditary Val30Met ATTR amyloidosis. The fibril consists of a single protofilament that is formed from an N-terminal and a C-terminal fragment of transthyretin. Our structure provides insights into the mechanism of misfolding and implies the formation of an early fibril state from unfolded transthyretin molecules, which upon proteolysis converts into mature ATTR amyloid fibrils.

Place, publisher, year, edition, pages
NATURE PUBLISHING 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:uu:diva-397799 (URN)10.1038/s41467-019-13038-z (DOI)000493712700001 ()31676763 (PubMedID)
Funder
German Research Foundation (DFG), SCHM 3276/1Erik, Karin och Gösta Selanders Foundation
Available from: 2019-11-27 Created: 2019-11-27 Last updated: 2019-11-27Bibliographically approved
Posautz, A. & Westermark, P. (2019). Experimental transmission of AA amyloidosis in the European brown hare (Lepus europaeus) - first results. Paper presented at 16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN. Amyloid: Journal of Protein Folding Disorders, 26(Suppl. 1), 121-122
Open this publication in new window or tab >>Experimental transmission of AA amyloidosis in the European brown hare (Lepus europaeus) - first results
2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, no Suppl. 1, p. 121-122Article in journal (Refereed) Published
Place, publisher, year, edition, pages
TAYLOR & FRANCIS LTD, 2019
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:uu:diva-392845 (URN)10.1080/13506129.2019.1593131 (DOI)000477775700065 ()31343351 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN
Available from: 2019-09-10 Created: 2019-09-10 Last updated: 2019-09-10Bibliographically approved
Posautz, A., Loncaric, I. & Westermark, P. (2019). Is there a connection between the microbiome and AA amyloidosis?: First hints from the European brown hare (Lepus europaeus). Paper presented at 16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN. Amyloid: Journal of Protein Folding Disorders, 26(Suppl. 1), 119-120
Open this publication in new window or tab >>Is there a connection between the microbiome and AA amyloidosis?: First hints from the European brown hare (Lepus europaeus)
2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, no Suppl. 1, p. 119-120Article in journal (Refereed) Published
Place, publisher, year, edition, pages
TAYLOR & FRANCIS LTD, 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:uu:diva-392844 (URN)10.1080/13506129.2019.1593130 (DOI)000477775700064 ()31343352 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN
Available from: 2019-09-10 Created: 2019-09-10 Last updated: 2019-09-10Bibliographically 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. Paper presented at 16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN. Amyloid: Journal of Protein Folding Disorders, 26(Suppl. 1), 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, no Suppl. 1, p. 39-40Article in journal (Refereed) Published
Place, publisher, year, edition, pages
TAYLOR & FRANCIS LTD, 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:uu:diva-392843 (URN)10.1080/13506129.2019.1593133 (DOI)000477775700022 ()31343354 (PubMedID)
Conference
16th International Symposium on Amyloidosis (ISA), MAR 26-29, 2018, Kumamoto, JAPAN
Available from: 2019-09-10 Created: 2019-09-10 Last updated: 2019-09-10Bibliographically approved
Hellman, U., Lang, 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, 79(6), 372-376
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, Vol. 79, no 6, p. 372-376Article in journal (Refereed) Published
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 LTD, 2019
Keywords
Amyloidosis, transthyretin, neuropathy, cardiomyopathy, amyloid fibril
National Category
Cardiac and Cardiovascular Systems
Identifiers
urn:nbn:se:uu:diva-396073 (URN)10.1080/00365513.2019.1624977 (DOI)000474016000001 ()31169435 (PubMedID)
Funder
Knut and Alice Wallenberg FoundationKnut and Alice Wallenberg FoundationVästerbotten County Council
Available from: 2019-10-30 Created: 2019-10-30 Last updated: 2019-10-30Bibliographically approved
Skinner, M. & Westermark, P. (2018). Alan S. Cohen 1926-2018 Obituary. Amyloid: Journal of Protein Folding Disorders, 25(2), 73-74
Open this publication in new window or tab >>Alan S. Cohen 1926-2018 Obituary
2018 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 25, no 2, p. 73-74Article in journal (Other academic) Published
Place, publisher, year, edition, pages
Taylor & Francis, 2018
National Category
Neurology
Identifiers
urn:nbn:se:uu:diva-369065 (URN)10.1080/13506129.2018.1481621 (DOI)000446965400001 ()30032648 (PubMedID)
Available from: 2018-12-13 Created: 2018-12-13 Last updated: 2019-06-27Bibliographically approved
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