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Lundmark, Katarzyna
Alternative names
Publications (10 of 15) Show all publications
Shariatpanahi, A., Hultman, P., Öllinger, K., Westermark, G. T. & Lundmark, K. (2019). Lipid membranes accelerate amyloid formation in the mouse model of AA amyloidosis. Amyloid: Journal of Protein Folding Disorders, 26(1), 34-44
Open this publication in new window or tab >>Lipid membranes accelerate amyloid formation in the mouse model of AA amyloidosis
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2019 (English)In: Amyloid: Journal of Protein Folding Disorders, ISSN 1350-6129, E-ISSN 1744-2818, Vol. 26, no 1, p. 34-44Article in journal (Refereed) Published
Abstract [en]

Introduction: AA amyloidosis develops as a result of prolonged inflammation and is characterized by deposits of N-terminal proteolytic fragments of the acute phase reactant serum amyloid A (SAA). Macrophages are usually found adjacent to amyloid, suggesting their involvement in the formation and/or degradation of the amyloid fibrils. Furthermore, accumulating evidence suggests that lipid membranes accelerate the fibrillation of different amyloid proteins.

Methods: Using an experimental mouse model of AA amyloidosis, we compared the amyloidogenic effect of liposomes and/or amyloid-enhancing factor (AEF). Inflammation was induced by subcutaneous injection of silver nitrate followed by intravenous injection of liposomes and/or AEF to accelerate amyloid formation.

Results: We showed that liposomes accelerate amyloid formation in inflamed mice, but the amyloidogenic effect of liposomes was weaker compared with AEF. Regardless of the induction method, amyloid deposits were mainly found in the marginal zones of the spleen and coincided with the depletion of marginal zone macrophages, while red pulp macrophages and metallophilic marginal zone macrophages proved insensitive to amyloid deposition.

Conclusions: We conclude that increased intracellular lipid content facilitates AA amyloid fibril formation and show that the mouse model of AA amyloidosis is a suitable system for further mechanistic studies.

Place, publisher, year, edition, pages
Taylor & Francis, 2019
Keywords
Amyloid; liposomes; lipid membrane; macrophages; AA amyloidosis
National Category
Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
Identifiers
urn:nbn:se:liu:diva-157278 (URN)10.1080/13506129.2019.1576606 (DOI)000466218300001 ()30929476 (PubMedID)2-s2.0-85063746690 (Scopus ID)
Note

Funding Agencies|County Council of Ostergotland; Magnus Bergvalls Research Foundation; Broderna Karlssons Research Foundation; K. Molins Minnesfond and Hildur Pettersons Research Foundation

Available from: 2019-06-12 Created: 2019-06-12 Last updated: 2019-10-29Bibliographically approved
Hashem, R., Tynngård, N., Lundmark, K. & Falk, L. (2019). Microcystic adnexal carcinoma originating in a nevus sebaceous: a case report of a 16-year-old boy. Acta Dermato-Venereologica, 99(12), 1182-1183
Open this publication in new window or tab >>Microcystic adnexal carcinoma originating in a nevus sebaceous: a case report of a 16-year-old boy
2019 (English)In: Acta Dermato-Venereologica, ISSN 0001-5555, E-ISSN 1651-2057, Vol. 99, no 12, p. 1182-1183Article in journal (Refereed) Published
Place, publisher, year, edition, pages
Uppsala, Sweden: Society for the Publication of Acta Dermato - Venereologica, 2019
National Category
Dermatology and Venereal Diseases
Identifiers
urn:nbn:se:liu:diva-160353 (URN)10.2340/00015555-3272 (DOI)000496991600025 ()31386165 (PubMedID)
Available from: 2019-09-19 Created: 2019-09-19 Last updated: 2020-02-20Bibliographically approved
Orfanidis, K., Wäster, P., Lundmark, K., Rosdahl, I. & Öllinger, K. (2017). Evaluation of tubulin β-3 as a novel senescence-associated gene in melanocytic malignant transformation.. Pigment Cell & Melanoma Research, 30(2), 243-254
Open this publication in new window or tab >>Evaluation of tubulin β-3 as a novel senescence-associated gene in melanocytic malignant transformation.
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2017 (English)In: Pigment Cell & Melanoma Research, ISSN 1755-1471, E-ISSN 1755-148X, Vol. 30, no 2, p. 243-254Article in journal (Refereed) Published
Abstract [en]

Malignant melanoma might develop from melanocytic nevi in which the growth-arrested state has been broken. We analyzed the gene expression of young and senescent human melanocytes in culture and compared the gene expression data with a dataset from nevi and melanomas. A concordant altered gene expression was identified in 84 genes when comparing the growth-arrested samples with proliferating samples. TUBB3, which encodes the microtubule protein tubulin β-3, showed a decreased expression in senescent melanocytes and nevi and was selected for further studies. Depletion of tubulin β-3 caused accumulation of cells in the G2/M phase and decreased proliferation and migration. Immunohistochemical assessment of tubulin β-3 in benign lesions revealed strong staining in the superficial part of the intradermal components, which faded with depth. In contrast, primary melanomas exhibited staining without gradient in a disordered pattern and strong staining of the invasive front. Our results describe an approach to find clinically useful diagnostic biomarkers to more precisely identify cutaneous malignant melanoma and present tubulin β-3 as a candidate marker. This article is protected by copyright. All rights reserved.

Place, publisher, year, edition, pages
Blackwell Munksgaard, 2017
Keywords
senescence, nevus, melanoma, microarray, tubulin β-3
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:liu:diva-134870 (URN)10.1111/pcmr.12572 (DOI)000397412300010 ()28024114 (PubMedID)2-s2.0-85014598335 (Scopus ID)
Note

Funding agencies: Swedish Research Council; Welander-Finsen Foundation; Ostgotaregionens Cancer Foundation; Swedish Cancer Society; County Council of Ostergotland; Olle Engkvist Foundation

Available from: 2017-02-28 Created: 2017-02-28 Last updated: 2019-12-19Bibliographically approved
Bergfors, E., Lundmark, K. & Nyström Kronander, U. (2013). A child with a long-standing, intensely itching subcutaneous nodule on a thigh: an uncommon (?) reaction to commonly used vaccines. BMJ Case Reports
Open this publication in new window or tab >>A child with a long-standing, intensely itching subcutaneous nodule on a thigh: an uncommon (?) reaction to commonly used vaccines
2013 (English)In: BMJ Case Reports, ISSN 1757-790XArticle in journal (Refereed) Published
Abstract [en]

A 2-year-old girl presented with an intensely itching subcutaneous nodule on the front of a thigh. The nodule persisted for 10 months until it was excised. Subsequent investigation for malignancy and systemic disease showed no pathological findings. The diagnosis, persistent itching vaccination granuloma, was revealed by hazard almost 2 years after the onset of symptoms. Persistent itching subcutaneous nodules at the injection site for aluminium containing vaccines (mostly diphtheria-tetanus-pertussis combination vaccines for primary immunisation of infants) may appear with a long delay after the vaccination (months), cause prolonged itching (years) and are often associated with contact allergy to aluminium. The condition is poorly recognised in Health Care which may lead to prolonged symptoms and unnecessary investigations.

Place, publisher, year, edition, pages
BMJ Publishing Group, 2013
Keywords
itching, subcutaneous, nodule, vaccine
National Category
Pediatrics Dermatology and Venereal Diseases General Practice
Identifiers
urn:nbn:se:liu:diva-91041 (URN)10.1136/bcr-2012-007779 (DOI)23354861 (PubMedID)
Available from: 2013-04-12 Created: 2013-04-12 Last updated: 2018-01-11
Lundmark, K., Vahdat Shariatpanahi, A. & Westermark, G. T. (2013). Depletion of Spleen Macrophages Delays AA Amyloid Development: A Study Performed in the Rapid Mouse Model of AA Amyloidosis. PLoS ONE, 8(11), e79104
Open this publication in new window or tab >>Depletion of Spleen Macrophages Delays AA Amyloid Development: A Study Performed in the Rapid Mouse Model of AA Amyloidosis
2013 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 8, no 11, p. e79104-Article in journal (Refereed) Published
Abstract [en]

AA amyloidosis is a systemic disease that develops secondary to chronic inflammatory diseases Macrophages are often found in the vicinity of amyloid deposits and considered to play a role in both formation and degradation of amyloid fibrils. In spleen reside at least three types of macrophages, red pulp macrophages (RPM), marginal zone macrophages (MZM), metallophilic marginal zone macrophages (MMZM). MMZM and MZM are located in the marginal zone and express a unique collection of scavenger receptors that are involved in the uptake of blood-born particles. The murine AA amyloid model that resembles the human form of the disease has been used to study amyloid effects on different macrophage populations. Amyloid was induced by intravenous injection of amyloid enhancing factor and subcutaneous injections of silver nitrate and macrophages were identified with specific antibodies. We show that MZMs are highly sensitive to amyloid and decrease in number progressively with increasing amyloid load. Total area of MMZMs is unaffected by amyloid but cells are activated and migrate into the white pulp. In a group of mice spleen macrophages were depleted by an intravenous injection of clodronate filled liposomes. Subsequent injections of AEF and silver nitrate showed a sustained amyloid development. RPMs that constitute the majority of macrophages in spleen, appear insensitive to amyloid and do not participate in amyloid formation.

Place, publisher, year, edition, pages
Public Library of Science, 2013
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-102982 (URN)10.1371/journal.pone.0079104 (DOI)000327254700092 ()
Note

Funding Agencies|Swedish Research Council|GTW5343|County Council of Ostergotland Magnus Bergvalls research foundation||Ingrid Svenssons research foundation||Broderna Karlssons research foundation||Hildur Pettersons research foundation||

Available from: 2014-01-09 Created: 2014-01-09 Last updated: 2019-08-15
Lundmark, K., Vahdat Shariatpanahi, A., Westermark, P. & Westermark, G. T. (2010). Depletion of macrophages influences amyloid deposition in spleen in AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, vol 17, issue , pp 115-115. In: AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS (pp. 115-115). Informa Healthcare, 17
Open this publication in new window or tab >>Depletion of macrophages influences amyloid deposition in spleen in AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, vol 17, issue , pp 115-115
2010 (English)In: AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, Informa Healthcare , 2010, Vol. 17, p. 115-115Conference paper, Published paper (Refereed)
Abstract [en]

n/a

Place, publisher, year, edition, pages
Informa Healthcare, 2010
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-60258 (URN)000279801500149 ()
Available from: 2010-10-08 Created: 2010-10-08 Last updated: 2010-10-12
Vahdat Shariatpanahi, A., Lundmark, K. & Westermark, G. T. (2010). Distribution of macrophages in spleen with amyloid in AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, vol 17, issue , pp 99-100. In: AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS (pp. 99-100). Informa Healthcare, 17
Open this publication in new window or tab >>Distribution of macrophages in spleen with amyloid in AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, vol 17, issue , pp 99-100
2010 (English)In: AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS, Informa Healthcare , 2010, Vol. 17, p. 99-100Conference paper, Published paper (Refereed)
Abstract [en]

n/a

Place, publisher, year, edition, pages
Informa Healthcare, 2010
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-60257 (URN)000279801500117 ()
Available from: 2010-10-08 Created: 2010-10-08 Last updated: 2010-10-12
Westermark, P., Lundmark, K. & Westermark, G. (2009). Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model. PLoS ONE, 4(6), e6041
Open this publication in new window or tab >>Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model
2009 (English)In: PLoS ONE, ISSN 1932-6203, Vol. 4, no 6, p. e6041-Article in journal (Refereed) Published
Abstract [en]

Background: Mouse AA-amyloidosis is a transmissible disease by a prion-like mechanism where amyloid fibrils act by seeding. Synthetic peptides with no amyloid relationship can assemble into amyloid-like fibrils and these may have seeding capacity for amyloid proteins. Principal Findings: Several synthetic peptides, designed for nanotechnology, have been examined for their ability to produce fibrils with Congo red affinity and concomitant green birefringence, affinity for thioflavin S and to accelerate AA-amyloidosis in mice. It is shown that some amphiphilic fibril-forming peptides not only produced Congo red birefringence and showed affinity for thioflavin S, but they also shortened the lag phase for systemic AA-amyloidosis in mice when they were given intravenously at the time of inflammatory induction with silver nitride. Peptides, not forming amyloid-like fibrils, did not have such properties. Conclusions: These observations should caution researchers and those who work with synthetic peptides and their derivatives to be aware of the potential health concerns. © 2009 Westermark et al.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-21313 (URN)10.1371/journal.pone.0006041 (DOI)
Note
Original Publication: P. Westermark, Katarzyna Lundmark and Gunilla Westermark, Fibrils from designed non-amyloid-related synthetic peptides induce AA-amyloidosis during inflammation in an animal model, 2009, PLoS ONE, (4), 6, e6041. http://dx.doi.org/10.1371/journal.pone.0006041 Available from: 2009-09-30 Created: 2009-09-30 Last updated: 2009-10-03
Lundmark, K., Westermark, G., Olsén, A. & Westermark, P. (2005). Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism. Proceedings of the National Academy of Sciences of the United States of America, 102(17), 6098-6102
Open this publication in new window or tab >>Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism
2005 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 102, no 17, p. 6098-6102Article in journal (Refereed) Published
Abstract [en]

Secondary, or amyloid protein A (AA), amyloidosis is a complication of chronic inflammatory diseases, both infectious and noninfectious. AA constitutes the insoluble fibrils, which are deposited in different organs, and is a major N-terminal part of the acute phase protein serum AA. It is not known why only some patients with chronic inflammation develop AA amyloidosis. Nucleation is a widely accepted mechanism in amyloidogenesis. Preformed amyloid-like fibrils act as nuclei in amyloid fibril formation in vitro, and AA amyloid fibrils and synthetic amyloid-like fibrils also may serve as seed for fibril formation in vivo. In addition to amyloid fibrils, there is a variety of similar nonmammalian protein fibrils with β-pleated structure in nature. We studied three such naturally occurring protein fibrils: silk from Bombyx mori, Sup35 from Saccharomyces cerevisiae, and curli from Escherichia coli. Our results show that these protein fibrils exert amyloid-accelerating properties in the murine experimental AA amyloidosis, suggesting that such environment factors may be important risk factors in amyloidogenesis.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-30441 (URN)10.1073/pnas.0501814102 (DOI)16004 (Local ID)16004 (Archive number)16004 (OAI)
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2018-10-08Bibliographically approved
Lundmark, K., Westermark, G. T., Nyström, S., Murphy, C. L., Solomon, A. & Westermark, P. (2002). Transmissibility of systemic amyloidosis by a prion-like mechanism. Proceedings of the National Academy of Sciences of the United States of America, 99(10), 6979-6984
Open this publication in new window or tab >>Transmissibility of systemic amyloidosis by a prion-like mechanism
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2002 (English)In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 99, no 10, p. 6979-6984Article in journal (Refereed) Published
Abstract [en]

The generation of amyloid fibrils from an amyloidogenic polypeptide occurs by a nucleation-dependent process initiated in vitro by seeding the protein solution with preformed fibrils. This phenomenon is evidenced in vivo by the fact that amyloid protein A (AA) amyloidosis in mice is markedly accelerated when the animals are given, in addition to an inflammatory stimulus, an i.v. injection of protein extracted from AA amyloid-laden mouse tissue. Heretofore, the chemical nature of this “amyloid enhancing factor” (AEF) has not been definitively identified. Here we report that the active principle of AEF extracted from the spleen of mice with silver nitrate-induced AA amyloidosis was identified unequivocally as the AA fibril itself. Further, we demonstrated that this material was extremely potent, being active in doses <1 ng, and that it retained its biologic activity over a considerable length of time. Notably, the AEF was also effective when administered orally. Our studies have provided evidence that AA and perhaps other forms of amyloidosis are transmissible diseases, akin to the prion-associated disorders.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-20805 (URN)10.1073/pnas.092205999 (DOI)12011456 (PubMedID)
Available from: 2009-09-21 Created: 2009-09-21 Last updated: 2017-12-13Bibliographically approved
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