AZ EMBERI PRIONBETEGSEGEK

Translated title of the contribution: Human prion diseases

G. G. Kovacs, L. László

Research output: Contribution to journalArticle

Abstract

Prion diseases are caused by slow infections. The abnormal protease resistant isoform of the physiologic prion protein plays a crucial role in the pathogenesis. Prion diseases are transmissible, though no exogenous nucleic acid was found. Etiologically human prion diseases may be exogenous (kuru, iatrogenic Creutzfeldt-Jakob disease 'variant' Creutzfeldt-]akob disease), sporadic (classical Creutzfeldt-Jakob disease) and familial (familial Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker disease, fatal familiar insomnia). The diagnostic procedure starts with observing clinically a progressive dementia course, myoclonus with symptoms of various nervous system functions. EEG, cranial MR scan and examination of the cerebrospinal fluid may support the clinical diagnosis. Neuropathologically prion diseases are characterized by spongiform changes, loss of neurons, astrocytosis, and rarely plaque-formation. Definitively prion disease can be confirmed with post mortem investigations(observation of the abnormal prion protein biochemically or using immunodytochemistry) and with genetic analysis of a mutant prion gene in familial forms. Certain precautions are advised when dealing with prion disease patients, especially during surgical and pathological procedures.

Original languageHungarian
Pages (from-to)476-484
Number of pages9
JournalLege Artis Medicinae
Volume8
Issue number7-8
Publication statusPublished - 1998

Fingerprint

Prion Diseases
Creutzfeldt-Jakob Syndrome
Gerstmann-Straussler-Scheinker Disease
Kuru
Myoclonus
Gliosis
Prions
Sleep Initiation and Maintenance Disorders
Nucleic Acids
Nervous System
Cerebrospinal Fluid
Dementia
Electroencephalography
Protein Isoforms
Peptide Hydrolases
Observation
Neurons
Infection
Genes

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Kovacs, G. G., & László, L. (1998). AZ EMBERI PRIONBETEGSEGEK. Lege Artis Medicinae, 8(7-8), 476-484.

AZ EMBERI PRIONBETEGSEGEK. / Kovacs, G. G.; László, L.

In: Lege Artis Medicinae, Vol. 8, No. 7-8, 1998, p. 476-484.

Research output: Contribution to journalArticle

Kovacs, GG & László, L 1998, 'AZ EMBERI PRIONBETEGSEGEK', Lege Artis Medicinae, vol. 8, no. 7-8, pp. 476-484.
Kovacs, G. G. ; László, L. / AZ EMBERI PRIONBETEGSEGEK. In: Lege Artis Medicinae. 1998 ; Vol. 8, No. 7-8. pp. 476-484.
@article{d34383cce66e4bdabc305d9d584896a9,
title = "AZ EMBERI PRIONBETEGSEGEK",
abstract = "Prion diseases are caused by slow infections. The abnormal protease resistant isoform of the physiologic prion protein plays a crucial role in the pathogenesis. Prion diseases are transmissible, though no exogenous nucleic acid was found. Etiologically human prion diseases may be exogenous (kuru, iatrogenic Creutzfeldt-Jakob disease 'variant' Creutzfeldt-]akob disease), sporadic (classical Creutzfeldt-Jakob disease) and familial (familial Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker disease, fatal familiar insomnia). The diagnostic procedure starts with observing clinically a progressive dementia course, myoclonus with symptoms of various nervous system functions. EEG, cranial MR scan and examination of the cerebrospinal fluid may support the clinical diagnosis. Neuropathologically prion diseases are characterized by spongiform changes, loss of neurons, astrocytosis, and rarely plaque-formation. Definitively prion disease can be confirmed with post mortem investigations(observation of the abnormal prion protein biochemically or using immunodytochemistry) and with genetic analysis of a mutant prion gene in familial forms. Certain precautions are advised when dealing with prion disease patients, especially during surgical and pathological procedures.",
keywords = "Creutzfeldt-Jakob disease, Prion, Spongiform encephalopathy",
author = "Kovacs, {G. G.} and L. L{\'a}szl{\'o}",
year = "1998",
language = "Hungarian",
volume = "8",
pages = "476--484",
journal = "Lege Artis Medicinae",
issn = "0866-4811",
publisher = "Literatura Medica Publishing House",
number = "7-8",

}

TY - JOUR

T1 - AZ EMBERI PRIONBETEGSEGEK

AU - Kovacs, G. G.

AU - László, L.

PY - 1998

Y1 - 1998

N2 - Prion diseases are caused by slow infections. The abnormal protease resistant isoform of the physiologic prion protein plays a crucial role in the pathogenesis. Prion diseases are transmissible, though no exogenous nucleic acid was found. Etiologically human prion diseases may be exogenous (kuru, iatrogenic Creutzfeldt-Jakob disease 'variant' Creutzfeldt-]akob disease), sporadic (classical Creutzfeldt-Jakob disease) and familial (familial Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker disease, fatal familiar insomnia). The diagnostic procedure starts with observing clinically a progressive dementia course, myoclonus with symptoms of various nervous system functions. EEG, cranial MR scan and examination of the cerebrospinal fluid may support the clinical diagnosis. Neuropathologically prion diseases are characterized by spongiform changes, loss of neurons, astrocytosis, and rarely plaque-formation. Definitively prion disease can be confirmed with post mortem investigations(observation of the abnormal prion protein biochemically or using immunodytochemistry) and with genetic analysis of a mutant prion gene in familial forms. Certain precautions are advised when dealing with prion disease patients, especially during surgical and pathological procedures.

AB - Prion diseases are caused by slow infections. The abnormal protease resistant isoform of the physiologic prion protein plays a crucial role in the pathogenesis. Prion diseases are transmissible, though no exogenous nucleic acid was found. Etiologically human prion diseases may be exogenous (kuru, iatrogenic Creutzfeldt-Jakob disease 'variant' Creutzfeldt-]akob disease), sporadic (classical Creutzfeldt-Jakob disease) and familial (familial Creutzfeldt-Jakob disease, Gerstmann-Straussler-Scheinker disease, fatal familiar insomnia). The diagnostic procedure starts with observing clinically a progressive dementia course, myoclonus with symptoms of various nervous system functions. EEG, cranial MR scan and examination of the cerebrospinal fluid may support the clinical diagnosis. Neuropathologically prion diseases are characterized by spongiform changes, loss of neurons, astrocytosis, and rarely plaque-formation. Definitively prion disease can be confirmed with post mortem investigations(observation of the abnormal prion protein biochemically or using immunodytochemistry) and with genetic analysis of a mutant prion gene in familial forms. Certain precautions are advised when dealing with prion disease patients, especially during surgical and pathological procedures.

KW - Creutzfeldt-Jakob disease

KW - Prion

KW - Spongiform encephalopathy

UR - http://www.scopus.com/inward/record.url?scp=0031665768&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031665768&partnerID=8YFLogxK

M3 - Article

VL - 8

SP - 476

EP - 484

JO - Lege Artis Medicinae

JF - Lege Artis Medicinae

SN - 0866-4811

IS - 7-8

ER -