Protein misfolding cyclic amplification

Fabio Moda; Sandra Pritzkow; Claudio Soto

doi:10.1007/978-1-4614-5305-5

Protein misfolding cyclic amplification

Fabio Moda, Sandra Pritzkow, Claudio Soto

Fondazione IRCCS Istituto Neurologico "C. Besta"

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Prion diseases are caused by a conformational conversion of the cellular prion protein (PrP^C) to a pathological conformer (PrP^Sc). The “prion-only” hypothesis suggests that PrP^Sc is the infectious agent that propagates the disease acting as a template for theconversion of PrP^C. In 2001, we developed a novel in vitro technique, called Protein misfolding cyclic ampli fi cation (PMCA), which mimics this pathological process in an accelerated way. Thereby, minimal amount of PrP^Sc can be ampli fi ed to several millions fold, providing an important tool for diagnosis and investigation of prion biology, and the molecular mechanism of prion conversion. PMCA also offers a great platform for the study and ampli fi cation of the protein misfolding process associated with other neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases.

Original language	English
Title of host publication	Prions and Diseases: Volume 1, Physiology and Pathophysiology
Publisher	Springer New York
Pages	83-92
Number of pages	10
ISBN (Print)	9781461453055, 9781461453048
DOIs	https://doi.org/10.1007/978-1-4614-5305-5
Publication status	Published - Jan 1 2013

Keywords

PMCA
Prion decontamination procedures
Prion diseases
Prion transmission
Protein misfolding cyclic amplification
Transmissible spongiform encephalopathies

ASJC Scopus subject areas

Medicine(all)
Neuroscience(all)

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10.1007/978-1-4614-5305-5

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title = "Protein misfolding cyclic amplification",

abstract = "Prion diseases are caused by a conformational conversion of the cellular prion protein (PrPC) to a pathological conformer (PrPSc). The “prion-only” hypothesis suggests that PrPSc is the infectious agent that propagates the disease acting as a template for theconversion of PrPC. In 2001, we developed a novel in vitro technique, called Protein misfolding cyclic ampli fi cation (PMCA), which mimics this pathological process in an accelerated way. Thereby, minimal amount of PrPSc can be ampli fi ed to several millions fold, providing an important tool for diagnosis and investigation of prion biology, and the molecular mechanism of prion conversion. PMCA also offers a great platform for the study and ampli fi cation of the protein misfolding process associated with other neurodegenerative disorders, such as Alzheimer{\textquoteright}s and Parkinson{\textquoteright}s diseases.",

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