Difference Between Amyloid and Prion

Amyloids and prions are both synonymous with neurodegenerative disorders, disorders that cause degeneration inside the brain. Amyloids are not brain specific, every bit they can cause disorders in whatever organs in the torso. In terms of neurology, the human being neurodegenerative disorders for which amyloids and prions are directly or indirectly responsible, are those such every bit Alzheimer’southward affliction, Parkinson’southward disease, and Creutzfeldt-Jakob disease. Understanding the workings inside amyloids forms an important aspect of understanding prions and neurodegeneration.

Difference between Amyloid and Prion

Definition and Pathophysiology

Amyloids are aggregates (a formation made from many parts compiled together) of a rod-like structure which contains repetitions of a sure type of protein. When abnormal plasma cells stemming from the bone marrow form aberrant light concatenation proteins, they enter the bloodstream and form amyloid deposits. These deposits can cause a build up in any vital organ in the body (such as the encephalon, center or intestines), resulting in various serious medical conditions.

Prions are an abnormal grade or folding of the specific proteins of amyloids deposited in the brain, making them infectious and able to renew indefinitely. In other words, prions are divers as a subclass of amyloids where protein assemblage has come infectious and changed the state of self-production. The prions have the power to transmit their misfolded poly peptide shape into the same proteins occurring in a normal state.

Prions are responsible for the neurodegenerative disorders that can occur in humans and animals. This is due to the misshaped protein existence more difficult to break down past enzymes and end up accumulating in the neurons instead, resulting in destruction. When this neuron devastation progresses, it gradually causes tissue of the encephalon to take a sponge-like pattern filled with holes.

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Potential causes

Amyloids occur when bone marrow produces abnormal blood plasma cells. These abnormal plasma cells then form abnormal types of light chain proteins. When the abnormal light chain proteins enter the circulation system (blood stream), they deposit into vital organs throughout the torso. This tin can be due to:

  • Genetic or hereditary components (which impact the eyes, heart, kidneys and the brain)
  • Chronic diseases and types of cancers
  • Cell mutations
  • Rare infections

Prions are the misshaped proteins causing amyloids deposited in the brain. Genetically, the PRNP factor is responsible for directing the body to product prion poly peptide. When this gene mutates it tin can crusade aberrant protein production, resulting in specific prion diseases of the brain. Prion disease can also occur sporadically, resulting in other specific diseases of the encephalon.


Symptoms of abnormal amyloid protein deposits vary and depend on which tissue or organ has been affected past the deposits.

Prion disease, caused by misshaped prion proteins resulting in amyloids in the brain, often presents the post-obit symptoms:

  • Memory difficulties and changes in judgment
  • Personality changes
  • Confusion, difficulty with speech, and/or disorientation
  • Changes in coordination and involuntary muscle spasms
  • Decreased quality of vision or blindness


Diagnosing the occurrence of amyloids in the affected organs specifically can be done through biomarker tests. These include measuring the changes in the size of the organ and its functions, measuring levels of specific proteins in the blood, in cerebrospinal fluid, and on scans (MRI, CT, PET).

Diagnosing prion proteins in the brain causing prion disease can be washed through scans of the encephalon to mensurate role and size, cerebrospinal fluid testing for specific prion disease markers and neurodegeneration markers, and EEG to tape electrical activity changes in the brain.

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Treating amyloids depends on where they occur. The only fashion to completely abolish amyloids from existence produced is to undergo intensive chemotherapy to destroy abnormal blood cells in the bone marrow responsible for amyloid production. In that location is no other style to treat amyloids and the disorders caused by the occurrence of them are treated on a specific footing.

Prions causing prion illness can be treated with medications, assisted living associated with neurodegeneration, upholding hydration and food intake. This does not cure the production of prions or neurodegeneration simply provides a way for improving quality of life and treating associated symptoms.

Table of comparison between amyloid and prion

Summary of Amyloid vs Prion

Amyloids and prions are both associated with protein misshaping and sure neurodegenerative disorders. In the case of amyloids, misshaped proteins can cause disorders in whatever organ where they are deposited. Prions, nevertheless, are the misshaped proteins that can cause amyloids in the brain and take associated disorders limited to the brain. In terms of neurodegenerative disorders, amyloids are responsible for Alzheimer’s disease and Parkinson’s disease, where prions are responsible for Creutzfeldt-Jakob illness.


Are prions a blazon of amyloid?

Amyloids are aggregates with a fibrillar structure that is constituted by repetitions of a specific protein. Prions are defined as a sub grade of amyloids. With prions, the protein aggregation becomes cocky-perpetuating and so becomes infectious – this is the cause of many fatal neurodegenerative diseases such equally Creutzfeldt-Jacob disease.

How are amyloid plaques related to prions?

Amyloid plaques have been found in the brains of people with Creutzfeldt-Jacob disease. Creutzfeldt-Jacob affliction is an affliction caused by prions. Scrapie is some other prion disease, this fourth dimension institute in animals, with amyloid plaques that are composed of prion proteins

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What is the difference betwixt a prion and a poly peptide?

The main departure between a protein and a prion is in the structure – prions are misfolded causing them to exist able to change the shape of other similar proteins, thus becoming infectious.

Is amyloid beta a prion?

Due to its power to self-propagate as well as the being of several singled-out ‘strains’, amyloid beta shares a lot of indistinguishable properties with prions. These backdrop are what is probable making it possible to become a prion during diseases.

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