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Article ; Online: Tissue-based diagnosis of systemic amyloidosis: Experience of the informal diagnostic center at Uppsala University Hospital.

Damjanovic Vesterlund, Justina / Ihse, Elisabet / Thelander, Ulrika / Zancanaro, Alice / Westermark, Gunilla T / Westermark, Per

Upsala journal of medical sciences

2022 Volume 127

Abstract: Diagnosis of systemic amyloidosis is a clinical challenge and usually relies on a tissue biopsy. We have developed diagnostic methods based on the presence of amyloid deposits in abdominal subcutaneous fat tissue. This tissue is also used to determine ... ...

Abstract	Diagnosis of systemic amyloidosis is a clinical challenge and usually relies on a tissue biopsy. We have developed diagnostic methods based on the presence of amyloid deposits in abdominal subcutaneous fat tissue. This tissue is also used to determine the biochemical type of amyloidosis, performed by western blot and immunohistochemical analyses with the aid of in-house developed rabbit antisera and mouse monoclonal antibodies. Mass spectrometric methods are under development for selected cases. The diagnostic outcome for 2018-2020 was studied. During this period, we obtained 1,562 biopsies, of which 1,397 were unfixed subcutaneous fat tissue with varying degrees of suspicion of systemic amyloidosis. Of these, 440 contained amyloid deposits. The biochemical nature of the amyloid was determined by western blot analysis in 319 specimens and by immunohistochemistry in further 51 cases.
MeSH term(s)	Animals ; Mice ; Rabbits ; Plaque, Amyloid ; Amyloidosis/diagnosis ; Amyloidosis/pathology ; Amyloid ; Biopsy ; Hospitals
Chemical Substances	Amyloid
Language	English
Publishing date	2022-09-27
Publishing country	Sweden
Document type	Journal Article
ZDB-ID	183949-4
ISSN	2000-1967 ; 0300-9734
ISSN (online)	2000-1967
ISSN	0300-9734
DOI	10.48101/ujms.v127.8913
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Article ; Online: Development of Mouse Monoclonal Antibodies Against Human Amyloid Fibril Proteins for Diagnostic and Research Purposes.

Westermark, Gunilla T / Ihse, Elisabet / Westermark, Per

Methods in molecular biology (Clifton, N.J.)

2018 Volume 1779, Page(s) 401–414

Abstract: Commercial antibodies against varying proteins are often not optimal for identification of proteins in their amyloid fibril forms. Reasons can be the different conformation but also a variety of modifications like N- or C-terminal truncation. Therefore, ... ...

Abstract	Commercial antibodies against varying proteins are often not optimal for identification of proteins in their amyloid fibril forms. Reasons can be the different conformation but also a variety of modifications like N- or C-terminal truncation. Therefore, development of own monoclonal antibodies against amyloid fibril proteins may be advantageous. This chapter gives suggestions of how to be successful in such approaches.
MeSH term(s)	Amyloidosis/diagnosis ; Amyloidosis/genetics ; Amyloidosis/metabolism ; Animals ; Antibodies, Monoclonal, Murine-Derived/metabolism ; Epitopes/metabolism ; Humans ; Hybridomas/cytology ; Hybridomas/metabolism ; Mice ; Prealbumin/chemistry ; Prealbumin/genetics ; Prealbumin/immunology ; Rabbits
Chemical Substances	Antibodies, Monoclonal, Murine-Derived ; Epitopes ; Prealbumin ; TTR protein, human
Language	English
Publishing date	2018-05-28
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1940-6029
ISSN (online)	1940-6029
DOI	10.1007/978-1-4939-7816-8_24
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Article ; Online: Amyloid fibril composition type is consistent over time in patients with Val30Met (p.Val50Met) transthyretin amyloidosis.

Anan, Intissar / Suhr, Ole B / Liszewska, Katarzyna / Mejia Baranda, Jorge / Pilebro, Björn / Wixner, Jonas / Ihse, Elisabet

PloS one

2022 Volume 17, Issue 3, Page(s) e0266092

Abstract: 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 ... ...

Abstract	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.
MeSH term(s)	Abdominal Fat/metabolism ; Aged ; Aging/pathology ; Amyloid/metabolism ; Amyloid Neuropathies, Familial/metabolism ; Humans ; Prealbumin/metabolism
Chemical Substances	Amyloid ; Prealbumin
Language	English
Publishing date	2022-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0266092
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Article ; Online: Cardiac microcalcifications in transthyretin (ATTR) amyloidosis.

Thelander, Ulrika / Westermark, Gunilla T / Antoni, Gunnar / Estrada, Sergio / Zancanaro, Alice / Ihse, Elisabet / Westermark, Per

International journal of cardiology

2022 Volume 352, Page(s) 84–91

Abstract: Background: Bone tracers bind to amyloid-containing heart of most patients with ATTR amyloidosis. Amyloid deposits outside the heart are often scarce and bone scintigraphy is increasingly often used to diagnose cardiac involvement. However, the nature ... ...

Abstract	Background: Bone tracers bind to amyloid-containing heart of most patients with ATTR amyloidosis. Amyloid deposits outside the heart are often scarce and bone scintigraphy is increasingly often used to diagnose cardiac involvement. However, the nature of the binding of bone tracers to the heart is not clear. Objective: To identify possible calcium deposits in hearts with amyloid, explaining bone tracer binding. Methods and results: Formalin-fixed and paraffin embedded cardiac specimens from three patients with ATTR and one with AL amyloidosis, all with cardiac deposits, were studied. The specimens covered large parts of the heart. Sections were stained immunohistochemically for ATTR deposits and according to von Kóssa for calcifications. The study identified in all hearts, but particularly in the ATTR materials, focal, tight swarms of tiny calcifications. These were sometimes associated with amyloid but found as frequent in areas without such deposits. Autoradiography with [ Conclusions: Our study indicates that binding of skeletal probes to amyloid-containing hearts depends on an irregular presence of clouds of very tiny calcifications, which seem not to be directly associated with amyloid fibrils. Therefore, [
MeSH term(s)	Amyloid Neuropathies, Familial/complications ; Amyloid Neuropathies, Familial/diagnostic imaging ; Calcinosis/complications ; Calcinosis/diagnostic imaging ; Heart ; Humans ; Prealbumin ; Tomography, X-Ray Computed
Chemical Substances	Prealbumin
Language	English
Publishing date	2022-01-22
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	779519-1
ISSN	1874-1754 ; 0167-5273
ISSN (online)	1874-1754
ISSN	0167-5273
DOI	10.1016/j.ijcard.2022.01.036
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Article ; Online: The Swedish open-label diflunisal trial (DFNS01) on hereditary transthyretin amyloidosis and the impact of amyloid fibril composition.

Wixner, Jonas / Westermark, Per / Ihse, Elisabet / Pilebro, Björn / Lundgren, Hans-Erik / Anan, Intissar

Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis

2019 Volume 26, Issue sup1, Page(s) 39–40

MeSH term(s)	Adult ; Aged ; Aged, 80 and over ; Amyloid/drug effects ; Amyloid Neuropathies, Familial/drug therapy ; Amyloid Neuropathies, Familial/genetics ; Amyloid Neuropathies, Familial/pathology ; Diflunisal/administration & dosage ; Diflunisal/adverse effects ; Drug-Related Side Effects and Adverse Reactions/classification ; Drug-Related Side Effects and Adverse Reactions/pathology ; Female ; Humans ; Male ; Middle Aged ; Mutation ; Prealbumin/genetics ; Sweden/epidemiology
Chemical Substances	Amyloid ; Prealbumin ; Diflunisal (7C546U4DEN)
Language	English
Publishing date	2019-07-25
Publishing country	England
Document type	Journal Article ; Randomized Controlled Trial
ZDB-ID	1205246-2
ISSN	1744-2818 ; 1350-6129
ISSN (online)	1744-2818
ISSN	1350-6129
DOI	10.1080/13506129.2019.1593133
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Article ; Online: Abdominal fat pad biopsies exhibit good diagnostic accuracy in patients with suspected transthyretin amyloidosis.

Paulsson Rokke, Hedvig / Sadat Gousheh, Nima / Westermark, Per / Suhr, Ole B / Anan, Intissar / Ihse, Elisabet / Pilebro, Björn / Wixner, Jonas

Orphanet journal of rare diseases

2020 Volume 15, Issue 1, Page(s) 278

Abstract: Background: The diagnostic accuracy of histopathological detection of transthyretin amyloid (ATTR) by Congo red staining of abdominal fat samples has been questioned since low sensitivity has been reported, especially for patients with ATTR ... ...

Abstract	Background: The diagnostic accuracy of histopathological detection of transthyretin amyloid (ATTR) by Congo red staining of abdominal fat samples has been questioned since low sensitivity has been reported, especially for patients with ATTR cardiomyopathy. However, the outcome of surgically obtained fat pad biopsies has not yet been evaluated. The aim was to evaluate the diagnostic accuracy of skin punch biopsies from abdominal fat in patients with suspected ATTR amyloidosis. Material and methods: Data were evaluated from patients who had undergone abdominal fat pad biopsies using a skin punch due to suspected amyloidosis from 2006 to 2015. The biopsies had been analysed using Congo red staining to determine the presence of amyloid, and immunohistochemistry or Western blot to determine the type of amyloidosis. The final diagnosis was based on the clinical picture, biopsy results and DNA sequencing. Minimum follow-up after the initial biopsy was 3 years. Results: Two hundred seventy-four patients (61% males) were identified, and in 132 (48%), a final diagnosis of amyloidosis had been settled. The majority (93%) had been diagnosed with hereditary transthyretin (ATTRv) amyloidosis, and therefore subsequent analyses were focused on these patients. Overall, our data showed a test specificity of 99% and a sensitivity of 91%. Ninety-eight (94%) of the patients had neuropathic symptoms at diagnosis, whereas 57 (55%) had signs of amyloid cardiomyopathy. Subgroup analyses showed that patients with merely neuropathic symptoms displayed the highest test sensitivity of 91%, whereas patients with pure cardiomyopathy displayed the lowest sensitivity of 83%. However, no significant differences in sensitivity were found between patients with or without cardiomyopathy or between the sexes. Conclusions: Abdominal fat pad biopsies exhibit good diagnostic accuracy in patients with suspect ATTRv amyloidosis, including patients presenting with cardiomyopathy. In addition, the method enables typing not only of the precursor protein but also of the amyloid fibril type, which is related to the phenotype and to the outcome of the disease.
MeSH term(s)	Abdominal Fat ; Adipose Tissue ; Amyloid Neuropathies, Familial/diagnosis ; Amyloid Neuropathies, Familial/genetics ; Biopsy ; Female ; Humans ; Male ; Prealbumin/genetics
Chemical Substances	Prealbumin
Language	English
Publishing date	2020-10-08
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1750-1172
ISSN (online)	1750-1172
DOI	10.1186/s13023-020-01565-8
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Article ; Online: Amyloid fibril composition within hereditary Val30Met (p. Val50Met) transthyretin amyloidosis families.

Suhr, Ole Bernt / Wixner, Jonas / Anan, Intissar / Lundgren, Hans-Erik / Wijayatunga, Priyantha / Westermark, Per / Ihse, Elisabet

PloS one

2019 Volume 14, Issue 2, Page(s) e0211983

Abstract: 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 ... ...

Abstract	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.
MeSH term(s)	Adult ; Age of Onset ; Aged ; Amino Acid Substitution ; Amyloid/genetics ; Amyloid/metabolism ; Amyloid Neuropathies, Familial/genetics ; Amyloid Neuropathies, Familial/metabolism ; Female ; Genetic Predisposition to Disease ; Humans ; Male ; Middle Aged ; Pedigree ; Prealbumin/genetics ; Prealbumin/metabolism
Chemical Substances	Amyloid ; Prealbumin ; TTR protein, human
Language	English
Publishing date	2019-02-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0211983
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Article ; Online: Cellular internalization of alpha-synuclein aggregates by cell surface heparan sulfate depends on aggregate conformation and cell type.

Ihse, Elisabet / Yamakado, Hodaka / van Wijk, Xander M / Lawrence, Roger / Esko, Jeffrey D / Masliah, Eliezer

Scientific reports

2017 Volume 7, Issue 1, Page(s) 9008

Abstract: Amyloid aggregates found in the brain of patients with neurodegenerative diseases, including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger areas of the brain through a prion-like seeding mechanism. Not much is known ... ...

Abstract	Amyloid aggregates found in the brain of patients with neurodegenerative diseases, including Alzheimer's and Parkinson's disease, are thought to spread to increasingly larger areas of the brain through a prion-like seeding mechanism. Not much is known about which cell surface receptors may be involved in the cell-to-cell transfer, but proteoglycans are of interest due to their well-known propensity to interact with amyloid aggregates. In this study, we investigated the involvement of plasma membrane-bound heparan and chondroitin sulfate proteoglycans in cellular uptake of aggregates consisting of α-synuclein, a protein forming amyloid aggregates in Parkinson's disease. We show, using a pH-sensitive probe, that internalization of α-synuclein amyloid fibrils in neuroblastoma cells is dependent on heparan sulfate, whereas internalization of smaller non-amyloid oligomers is not. We also show that α-synuclein fibril uptake in an oligodendrocyte-like cell line is equally dependent on heparan sulfate, while astrocyte- and microglia-like cell lines have other means to internalize the fibrils. In addition, we analyzed the interaction between the α-synuclein amyloid fibrils and heparan sulfate and show that overall sulfation of the heparan sulfate chains is more important than sulfation at particular sites along the chains.
MeSH term(s)	Animals ; Astrocytes/metabolism ; Cell Line ; Endocytosis ; Heparitin Sulfate/metabolism ; Humans ; Microglia/metabolism ; Neurons/metabolism ; Oligodendroglia/metabolism ; Protein Aggregates ; Rats ; alpha-Synuclein/metabolism
Chemical Substances	Protein Aggregates ; alpha-Synuclein ; Heparitin Sulfate (9050-30-0)
Language	English
Publishing date	2017-08-21
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-017-08720-5
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Article ; Online: Transthyretin Glu54Leu - an unknown mutation within the Swedish population associated with amyloid cardiomyopathy and a unique fibril type.

Hellman, Urban / Lång, Kenneth / Ihse, Elisabet / Jonasson, Jenni / Olsson, Malin / Lundgren, Hans-Erik / Pilebro, Björn / Westermark, Per / Wixner, Jonas / Anan, Intissar

Scandinavian journal of clinical and laboratory investigation

2019 Volume 79, Issue 6, Page(s) 372–376

Abstract: For the first time, we report of a Swedish family of five individuals with ... ...

Abstract	For the first time, we report of a Swedish family of five individuals with a
MeSH term(s)	Amino Acid Substitution ; Amyloid/chemistry ; Amyloid/genetics ; Amyloid Neuropathies, Familial/complications ; Amyloid Neuropathies, Familial/diagnosis ; Amyloid Neuropathies, Familial/genetics ; Cardiomyopathies/complications ; Cardiomyopathies/diagnosis ; Cardiomyopathies/genetics ; Humans ; Mutation ; Pedigree ; Phenotype ; Prealbumin/genetics ; Sweden
Chemical Substances	Amyloid ; Prealbumin ; TTR protein, human
Language	English
Publishing date	2019-06-06
Publishing country	England
Document type	Case Reports ; Journal Article
ZDB-ID	3150-1
ISSN	1502-7686 ; 0036-5513
ISSN (online)	1502-7686
ISSN	0036-5513
DOI	10.1080/00365513.2019.1624977
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Article ; Online: Variation in amount of wild-type transthyretin in different fibril and tissue types in ATTR amyloidosis.

Ihse, Elisabet / Suhr, Ole B / Hellman, Ulf / Westermark, Per

Journal of molecular medicine (Berlin, Germany)

2010 Volume 89, Issue 2, Page(s) 171–180

Abstract: Familial transthyretin (TTR) amyloidosis is caused by a mutation in the TTR gene, although wild-type (wt) TTR is also incorporated into the amyloid fibrils. Liver transplantation (LT) is the prevailing treatment of the disease and is performed in order ... ...

Abstract	Familial transthyretin (TTR) amyloidosis is caused by a mutation in the TTR gene, although wild-type (wt) TTR is also incorporated into the amyloid fibrils. Liver transplantation (LT) is the prevailing treatment of the disease and is performed in order to eliminate the mutant TTR from plasma. The outcome of the procedure is varied; especially problematic is a progressive cardiomyopathy seen in some patients, presumably caused by continued incorporation of wtTTR. What determines the discrepancy in outcome is not clear. We have previously shown that two structurally distinct amyloid fibrils (with or without fragmented ATTR) are found among ATTRV30M patients. In this study, we investigated the proportion of wtATTR in cardiac and adipose amyloid from patients having either fibril type. It was found that cardiac amyloid more easily incorporates wtTTR than adipose amyloid, offering a potential explanation for the vulnerability of cardiac tissue for continued amyloidosis after LT. In cardiac tissue, fibrils with fragmented ATTR contained a higher wt proportion than fibrils without, suggesting that continued incorporation of wtTTR after LT, perhaps, can take place more easily in these patients. In adipose tissue, a rapid increase in wt proportion after LT indicates that a rather fast turnover of the deposits must occur. A difference in wt proportion between the fibril types was seen post-LT but not pre-LT, possibly caused by differences in turnover rate. Conclusively, this study further establishes the basic dissimilarities between the two fibril types and demonstrates that their role in LT outcome needs to be further investigated.
MeSH term(s)	Adipose Tissue/metabolism ; Adult ; Aged ; Aged, 80 and over ; Amyloid/metabolism ; Amyloidosis/physiopathology ; Female ; Heterozygote ; Humans ; Liver Transplantation ; Male ; Middle Aged ; Mutation ; Myocardium/metabolism ; Prealbumin/genetics ; Prealbumin/metabolism
Chemical Substances	Amyloid ; Prealbumin
Language	English
Publishing date	2010-11-25
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1223802-8
ISSN	1432-1440 ; 0946-2716
ISSN (online)	1432-1440
ISSN	0946-2716
DOI	10.1007/s00109-010-0695-1
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