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Myositis facilitates preclinical accumulation of pathological prion protein in muscle

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Myositis facilitates preclinical accumulation of pathological prion protein in muscle. / Neumann, Melanie; Krasemann, Susanne; Schröck, Katharina; Steinbach, Karin; Glatzel, Markus.

in: ACTA NEUROPATHOL COM, Jahrgang 1, Nr. 1, 01.01.2013, S. 78.

Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung

Harvard

Neumann, M, Krasemann, S, Schröck, K, Steinbach, K & Glatzel, M 2013, 'Myositis facilitates preclinical accumulation of pathological prion protein in muscle', ACTA NEUROPATHOL COM, Jg. 1, Nr. 1, S. 78. https://doi.org/10.1186/2051-5960-1-78

APA

Neumann, M., Krasemann, S., Schröck, K., Steinbach, K., & Glatzel, M. (2013). Myositis facilitates preclinical accumulation of pathological prion protein in muscle. ACTA NEUROPATHOL COM, 1(1), 78. https://doi.org/10.1186/2051-5960-1-78

Vancouver

Neumann M, Krasemann S, Schröck K, Steinbach K, Glatzel M. Myositis facilitates preclinical accumulation of pathological prion protein in muscle. ACTA NEUROPATHOL COM. 2013 Jan 1;1(1):78. https://doi.org/10.1186/2051-5960-1-78

Bibtex

@article{9f2fdc4d0b2c42e7a7e595994961dfc0,
title = "Myositis facilitates preclinical accumulation of pathological prion protein in muscle",
abstract = "BACKGROUND: In human and animal prion diseases, pathological prion protein, PrPSc, as well as prion infectivity is mainly found in the central nervous system, but also in lymphoid organs and muscle. Pathophysiology of prion colonization of lymphoid organs has been studied intensively, yet how myositis influences prion accumulation in muscle is unknown.RESULT: We have investigated the influence of myositis on PrPSc accumulation and prion infectivity in two distinct mouse models of experimental autoimmune myositis. Furthermore, we have addressed the relevance of PrPC expression in the lymphoreticular system in myositis by generating bone marrow chimeras.Here we show that myositis positively influences muscular PrPSc accumulation at preclinical time points and that PrPC-expression in the lymphoid system is critical for this. In muscle, PrPSc and prion infectivity are uncoupled with detectable PrPSc but no prion infectivity at preclinical time points. Muscle has an intrinsically high ability to clear PrPSc once myositis has ceased, possibly involving autophagy.CONCLUSION: Our findings provide new insights into the pathophysiology of prion colonization in muscle pointing out that myositis leads to enhanced prion colonization of muscle in subclinical prion disease.",
author = "Melanie Neumann and Susanne Krasemann and Katharina Schr{\"o}ck and Karin Steinbach and Markus Glatzel",
year = "2013",
month = jan,
day = "1",
doi = "10.1186/2051-5960-1-78",
language = "English",
volume = "1",
pages = "78",
journal = "ACTA NEUROPATHOL COM",
issn = "2051-5960",
publisher = "BioMed Central Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Myositis facilitates preclinical accumulation of pathological prion protein in muscle

AU - Neumann, Melanie

AU - Krasemann, Susanne

AU - Schröck, Katharina

AU - Steinbach, Karin

AU - Glatzel, Markus

PY - 2013/1/1

Y1 - 2013/1/1

N2 - BACKGROUND: In human and animal prion diseases, pathological prion protein, PrPSc, as well as prion infectivity is mainly found in the central nervous system, but also in lymphoid organs and muscle. Pathophysiology of prion colonization of lymphoid organs has been studied intensively, yet how myositis influences prion accumulation in muscle is unknown.RESULT: We have investigated the influence of myositis on PrPSc accumulation and prion infectivity in two distinct mouse models of experimental autoimmune myositis. Furthermore, we have addressed the relevance of PrPC expression in the lymphoreticular system in myositis by generating bone marrow chimeras.Here we show that myositis positively influences muscular PrPSc accumulation at preclinical time points and that PrPC-expression in the lymphoid system is critical for this. In muscle, PrPSc and prion infectivity are uncoupled with detectable PrPSc but no prion infectivity at preclinical time points. Muscle has an intrinsically high ability to clear PrPSc once myositis has ceased, possibly involving autophagy.CONCLUSION: Our findings provide new insights into the pathophysiology of prion colonization in muscle pointing out that myositis leads to enhanced prion colonization of muscle in subclinical prion disease.

AB - BACKGROUND: In human and animal prion diseases, pathological prion protein, PrPSc, as well as prion infectivity is mainly found in the central nervous system, but also in lymphoid organs and muscle. Pathophysiology of prion colonization of lymphoid organs has been studied intensively, yet how myositis influences prion accumulation in muscle is unknown.RESULT: We have investigated the influence of myositis on PrPSc accumulation and prion infectivity in two distinct mouse models of experimental autoimmune myositis. Furthermore, we have addressed the relevance of PrPC expression in the lymphoreticular system in myositis by generating bone marrow chimeras.Here we show that myositis positively influences muscular PrPSc accumulation at preclinical time points and that PrPC-expression in the lymphoid system is critical for this. In muscle, PrPSc and prion infectivity are uncoupled with detectable PrPSc but no prion infectivity at preclinical time points. Muscle has an intrinsically high ability to clear PrPSc once myositis has ceased, possibly involving autophagy.CONCLUSION: Our findings provide new insights into the pathophysiology of prion colonization in muscle pointing out that myositis leads to enhanced prion colonization of muscle in subclinical prion disease.

U2 - 10.1186/2051-5960-1-78

DO - 10.1186/2051-5960-1-78

M3 - SCORING: Journal article

C2 - 24299111

VL - 1

SP - 78

JO - ACTA NEUROPATHOL COM

JF - ACTA NEUROPATHOL COM

SN - 2051-5960

IS - 1

ER -