[Prion diseases]

Maite Martínez1, Elena Merino, Clara Ibeas

  • 1Unidad de Hospitalización de Neurología, Hospital Universitario Marqués de Valdecilla, Santander.

Revista De Enfermeria (Barcelona, Spain)
|September 25, 2003
PubMed

Insights

This review examines 17 years of prion disease cases to develop improved patient care guidelines. It aims to enhance understanding and effectiveness in managing these rare neurological disorders for healthcare teams.

Area of Science:

  • Neurology
  • Infectious Diseases
  • Patient Care

Context:

  • Retrospective review of prion disease cases over 17 years.
  • Identified need for updated treatment guidelines and nursing protocols.
  • Lack of nursing-specific publications on prion disease management.

Purpose:

  • Establish specific guidelines for prion disease treatment, norms, and attitudes.
  • Improve understanding and effectiveness of care for prion disease patients.
  • Provide counsel to healthcare teams involved in patient care.

Summary:

  • Analyzed 17 years of hospital data on prion diseases.
  • Developed evidence-based guidelines for comprehensive patient management.
  • Focused on enhancing multidisciplinary team collaboration and patient support.

Impact:

  • Aims to elevate the quality of care for prion disease patients.
  • Provides a foundational document for nursing practice in prion disease management.
  • Contributes to better-prepared healthcare professionals in managing rare neurological conditions.

Related Concept Videos

Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid Fibrils03:03

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins.  Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils. 
Amyloid deposits were observed as early as 1639 in the liver and the spleen.   In 1854, Rudolph Virchow performed iodine staining, normally used to...
Subviral Agents01:29

Subviral Agents

Subviral agents are infectious entities that resemble viruses but lack one or more viral components, such as a capsid or essential replication machinery. These agents include viroids, prions, and satellites, each possessing distinct structural and functional characteristics that influence their mode of infection and replication.Viroids are the simplest subviral agents, consisting of circular, single-stranded RNA molecules without a protein coat. They exclusively infect plants, relying entirely...
Rabies01:28

Rabies

Rabies is a lethal zoonotic disease caused by a single-stranded, negative-sense RNA virus of the Lyssavirus genus, within the family Rhabdoviridae. Its primary mode of transmission to humans is through bites or saliva-contaminated scratches from infected mammals such as dogs, bats, raccoons, or foxes. Transmission can also occur if infectious saliva contacts abraded skin or intact mucous membranes, including the conjunctiva.Viral Entry and Early ReplicationOnce introduced at the bite or scratch...
Parkinson Disease ll: Pathophysiology01:24

Parkinson Disease ll: Pathophysiology

Parkinson disease (PD) is a progressive neurodegenerative disorder primarily affecting movement, with additional non-motor features. Its pathophysiology involves complex interactions among genetic susceptibility, environmental exposures, and cellular dysfunction, including dopaminergic neuron loss, protein aggregation, and mitochondrial impairment.Selective NeurodegenerationA key feature is the degeneration of dopaminergic neurons in the substantia nigra pars compacta, leading to reduced...
Huntington Disease l: Introduction01:21

Huntington Disease l: Introduction

Huntington disease or HD is a progressive, fatal neurodegenerative disorder inherited in an autosomal dominant pattern.PathophysiologyIt is caused by expansion of the CAG trinucleotide repeat in the HTT gene on chromosome 4 (4p16.3), producing an abnormal huntingtin protein with an expanded polyglutamine tract. This misfolded protein disrupts cellular function, leading to neuronal death. Normal alleles have ≤26 repeats, 27–35 are intermediate (risk of expansion), 36–39 show reduced penetrance,...