The cellular prion protein and its derived fragments in human prion diseases and their role as potential biomarkers

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The cellular prion protein and its derived fragments in human prion diseases and their role as potential biomarkers. / Thüne, Katrin; Schmitz, Matthias; Villar-Piqué, Anna; Altmeppen, Hermann Clemens; Schlomm, Markus; Zafar, Saima; Glatzel, Markus; Llorens, Franc; Zerr, Inga.

In: EXPERT REV MOL DIAGN, Vol. 19, No. 11, 11.2019, p. 1007-1018.

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@article{2b9b033d89d54a5ba730bd71a69f4775,
title = "The cellular prion protein and its derived fragments in human prion diseases and their role as potential biomarkers",
abstract = "Introduction: Human prion diseases are a heterogeneous group of incurable and debilitating conditions characterized by a progressive degeneration of the central nervous system. The conformational changes of the cellular prion protein and its formation into an abnormal isoform, spongiform degeneration, neuronal loss, and neuroinflammation are central to prion disease pathogenesis. It has been postulated that truncated variants of aggregation-prone proteins are implicated in neurodegenerative mechanisms. An increasing body of evidence indicates that proteolytic fragments and truncated variants of the prion protein are formed and accumulated in the brain of prion disease patients. These prion protein variants provide a high degree of relevance to disease pathology and diagnosis. Areas covered: In the present review, we summarize the current knowledge on the occurrence of truncated prion protein species and their potential roles in pathophysiological states during prion diseases progression. In addition, we discuss their usability as a diagnostic biomarker in prion diseases. Expert opinion: Either as a primary factor in the formation of prion diseases or as a consequence from neuropathological affection, abnormal prion protein variants and fragments may provide independent information about mechanisms of prion conversion, pathological states, or disease progression.",
author = "Katrin Th{\"u}ne and Matthias Schmitz and Anna Villar-Piqu{\'e} and Altmeppen, {Hermann Clemens} and Markus Schlomm and Saima Zafar and Markus Glatzel and Franc Llorens and Inga Zerr",
year = "2019",
month = nov,
doi = "10.1080/14737159.2019.1667231",
language = "English",
volume = "19",
pages = "1007--1018",
journal = "EXPERT REV MOL DIAGN",
issn = "1473-7159",
publisher = "Expert Reviews Ltd.",
number = "11",

}

RIS

TY - JOUR

T1 - The cellular prion protein and its derived fragments in human prion diseases and their role as potential biomarkers

AU - Thüne, Katrin

AU - Schmitz, Matthias

AU - Villar-Piqué, Anna

AU - Altmeppen, Hermann Clemens

AU - Schlomm, Markus

AU - Zafar, Saima

AU - Glatzel, Markus

AU - Llorens, Franc

AU - Zerr, Inga

PY - 2019/11

Y1 - 2019/11

N2 - Introduction: Human prion diseases are a heterogeneous group of incurable and debilitating conditions characterized by a progressive degeneration of the central nervous system. The conformational changes of the cellular prion protein and its formation into an abnormal isoform, spongiform degeneration, neuronal loss, and neuroinflammation are central to prion disease pathogenesis. It has been postulated that truncated variants of aggregation-prone proteins are implicated in neurodegenerative mechanisms. An increasing body of evidence indicates that proteolytic fragments and truncated variants of the prion protein are formed and accumulated in the brain of prion disease patients. These prion protein variants provide a high degree of relevance to disease pathology and diagnosis. Areas covered: In the present review, we summarize the current knowledge on the occurrence of truncated prion protein species and their potential roles in pathophysiological states during prion diseases progression. In addition, we discuss their usability as a diagnostic biomarker in prion diseases. Expert opinion: Either as a primary factor in the formation of prion diseases or as a consequence from neuropathological affection, abnormal prion protein variants and fragments may provide independent information about mechanisms of prion conversion, pathological states, or disease progression.

AB - Introduction: Human prion diseases are a heterogeneous group of incurable and debilitating conditions characterized by a progressive degeneration of the central nervous system. The conformational changes of the cellular prion protein and its formation into an abnormal isoform, spongiform degeneration, neuronal loss, and neuroinflammation are central to prion disease pathogenesis. It has been postulated that truncated variants of aggregation-prone proteins are implicated in neurodegenerative mechanisms. An increasing body of evidence indicates that proteolytic fragments and truncated variants of the prion protein are formed and accumulated in the brain of prion disease patients. These prion protein variants provide a high degree of relevance to disease pathology and diagnosis. Areas covered: In the present review, we summarize the current knowledge on the occurrence of truncated prion protein species and their potential roles in pathophysiological states during prion diseases progression. In addition, we discuss their usability as a diagnostic biomarker in prion diseases. Expert opinion: Either as a primary factor in the formation of prion diseases or as a consequence from neuropathological affection, abnormal prion protein variants and fragments may provide independent information about mechanisms of prion conversion, pathological states, or disease progression.

U2 - 10.1080/14737159.2019.1667231

DO - 10.1080/14737159.2019.1667231

M3 - SCORING: Journal article

C2 - 31512940

VL - 19

SP - 1007

EP - 1018

JO - EXPERT REV MOL DIAGN

JF - EXPERT REV MOL DIAGN

SN - 1473-7159

IS - 11

ER -