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.Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review
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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 -