Nattokinase Degrades Amyloids and Prions

This article discusses the research that showed that nattokinase could dissolve amyloids and prion proteins.

What are Amyloids and Prions?

Both are abnormal proteins because they are misfolded. Proteins in the different parts of the body serve many functions. Proteins can be structural (bone), related to movement (muscles), and protection (skin).

Proteins are also found in hormones like insulin, digestive enzymes, cytokines, and blood cells responsible for the immune response.

Proteins have to be in a proper shape to be functional. If not, they could cause diseases.

Amyloids

Amyloids can be found in the brains of people with neurodegenerative conditions like Alzheimer’s, Parkinson’s, and Huntington’s disease.

Amyloid-beta (Aβ) fibril accumulation in the brain is associated with Alzheimer’s disease. The alpha-synuclein protein is found in Lewy Body Dementia and Parkinson’s Disease.

Amyloids are also seen in type 2 diabetes and spongiform encephalopathies, where the holes in the brain make it look like a sponge.

The list below shows some amyloid proteins and their respective precursors and the diseases they produce.[2] The precursor proteins are the normally occurring functional proteins. Once misfolded, they become amyloids and cause illness.

Disease	Precursor protein	Amyloid protein
Alzheimer’s disease	Amyloid precursor protein	Aβ peptides
Atrial amyloidosis	Atrial natriuretic factor (ANF)	Amyloid ANF
Spongiform encephalopathies	Prion protein (PrPc)	PrPsc
Primary systemic amyloidosis	Immunoglobulin light and heavy chains	AL and AH
Senile systemic amyloidosis	Wild-type transthyretin	ATTR
Hemodialysis-related amyloidosis	β2-microglobulin	Aβ2M
Hereditary nonneuropathic systemic amyloidosis	Lysozyme	ALys
Type II diabetes	Pro-IAPP	IAPP or “amylin”
Injection-localized amyloidosis	Insulin	AIns
Secondary systemic amyloidosis	(Apo) serum amyloid A	Serum amyloid A
Hereditary cerebral amyloid angiopathy	Cystatin C	ACys
Finnish hereditary systemic amyloidosis	Gelsolin	AGel
Familial amyloid polyneuropathy I	Transthyretin variants	ATTR
Familial amyloid polyneuropathy II	Apolipoprotein A1	AApoA1
Aging pituitary, prolactinomas	Prolactin	APro
Familial amyloidosis	Fibrinogen αA-chain	AFib
British familial dementia	Amyloid Bri Precursor Protein	ABri

Prions

A prion is a misfolded protein that can spread to others. They are found in animals and humans. Examples are scrapie in sheep, chronic wasting disease in deer, and bovine spongiform encephalopathy (BSE) in cattle (commonly known as “mad cow disease”).

In humans, prions cause Jacob-Creutzfeldt Disease (CJD), the human version of mad cow disease. It is believed that CJD is from ingesting beef with prions from a “mad cow.”

The image below is a microscopic view of a brain with spongiform degeneration in a patient who died of Creutzfeldt-Jakob disease (CJD).

Source: By Tulemo – Own work, CC BY-SA 4.0, https://commons.wikimedia.org/w/index.php?curid=119745241

CJD after the COVID shots

In a preprint study that included the late Nobel Prize virologist Luc Montagnier as one of the authors, they reported 26 cases of new-onset CJD after their COVID jabs.

Twenty-three out of the 26 cases developed symptoms within 15 days of their second injection of an mRNA vaccine. The other three cases were associated with AstraZeneca, a DNA vector vaccine, and symptoms appeared within the first month. The time to death was under five months after the injection.

Twenty-three out of the 26 cases developed symptoms within 15 days of their second injection of an mRNA vaccine. Three

Prions are considered a subclass of amyloid. Research in amyloid and prions are ongoing, and the more we know, the more the lines are blurred between amyloids and prions.

Endogenous prions. Not all people with CJD got it from a “mad cow.” Prions can also form inside the body from human proteins. A review article listed 37 peptides or proteins that can form extracellular amyloid deposits in human diseases.[3]

There are other ways to get infected with prion diseases: blood transfusion [4] and contaminated surgical instruments. In 2016, Maine Medical center postponed all their elective surgery as a precaution when one patient was diagnosed with a possible prion disease.

In summary, prions and amyloid-related diseases are not that rare and may be more common than we know. It can spread by blood transfusion, contaminated surgical instruments, or form spontaneously inside the body.

Is there a solution?

Nattokinase can degrade amyloid and prions

One study might provide an answer. The study Amyloid-Degrading Ability of Nattokinase from Bacillus subtilis Natto was published in the Journal of Agricultural and Food Chemistry.[1]

The study compared the ability of nattokinase and other serine proteases to digest amyloid-beta (Aβ) fibrils, insulin amyloid fibrils, and human prion proteins.

Nattokinase is an enzyme produced by the Bacillus subtilis bacteria. It is commonly found in natto, a fermented soybean food. It is also available over the counter.

Best Naturals Nattokinase 2,000 FU (100 mg)

Amyloid-beta fibrils are one of the major components of amyloid plaques in Alzheimer’s disease.

Insulin fibrils resulting from repeated insulin injections in diabetes patients can cause injection-localized amyloidosis. Insulin fibrils can block insulin pumps.

They found that nattokinase can effectively degrade the three abnormal proteins in a condition mimicking the human body. (physiologic pH of 7 and temperature of 37°C). Additionally, nattokinase was more efficient than plasmin in cleaving amyloid under the same conditions.[1]

Plasmin is a substance typically formed in the human body that dissolves blood clots. The ability of nattokinase to dissolve blood clots makes it an excellent thrombolytic.

I discussed that in The Outstanding Vascular Effects and Dose of Nattokinase.

The research also found that nattokinase is more efficient in degrading amyloids and prions than other protease enzymes. And nattokinase is the only enzyme that can be taken by mouth and retain its effectiveness.[1]

The ability to degrade amyloids outside the brain is notable because recent studies found that amyloid-beta clearance outside the brain substantially lowers amyloid accumulation in the brain and potentially lower the risk of Alzheimer’s disease.[5]

To conclude, amyloid and prion diseases could be more common than initially thought. Nattokinase could break up amyloid and prion proteins and potentially solve those problems.

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References:

Hsu RL, Lee KT, Wang JH, Lee LY, Chen RP. Amyloid-degrading ability of nattokinase from Bacillus subtilis natto. J Agric Food Chem. 2009 Jan 28;57(2):503-8. PMID: 19117402 Doi: 10.1021/jf803072r.
Rambaran RN, Serpell LC. Amyloid fibrils: abnormal protein assembly. Prion. 2008 Jul-Sep;2(3):112-7. doi: 10.4161/pri.2.3.7488. Epub 2008 Jul 20. PMID: 19158505; PMCID: PMC2634529.
Chiti, F.; Dobson, C. M. Protein misfolding, functional amyloid, and human disease. Annu. ReV. Biochem. 2006, 75, 333–366.
Hunter, N.; Foster, J.; Chong, A.; McCutcheon, S.; Parnham, D.; Eaton, S.; MacKenzie, C.; Houston, F. Transmission of prion diseases by blood transfusion. J. Gen. Virol. 2002, 83, 2897–2905.
Cheng, Y., Tian, DY. & Wang, YJ. Peripheral clearance of brain-derived Aβ in Alzheimer’s disease: pathophysiology and therapeutic perspectives. Transl Neurodegener 9, 16 (2020). https://doi.org/10.1186/s40035-020-00195-1

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