I am re-publishing a prior post regrading amyolids because we have received such widespread feed back on this week’s post on EBV.  Amyloids or  truncated proteins, which your body cannot breakdown, are like a super food for the virus so they will be keeping you sick but keeping your virus strong and well  feed.    So if you have been exposed to EBV you should be gluten free 2.0  (see another post), low sugar ( that means fruit and grains) and only eating wild game animal protein and fish.

We have made observations in certain clients regarding the inability to properly digest protein and a wide variety of ailments; from multiple sclerosis (MS), cancer,  Lyme’s Disease,  EBV, POTS, dementia, parkinsons,  to even inexplicable symptoms such as seizures, tremors, migraines, and debilitating fatigue. In researching the background of these diseases, there was always a common denominator – amyloids, protein-like substances. There are now approximately 50 disorders which are associated with amyloids (Knowles et al 2014). These disorders include but are not limited to HIV, cancer, MS, Parkinson’s, Alzheimer’s, Lyme’s Disease, Postural Orthostatic Tachycardia Syndrome (POTS), and type 2 diabetes (Agarwal et al 2007, Cozzi et al 1992, Knowles et al 2014). Researchers at the University of Cambridge state there has been explosion of interest in amyloid research because many of the disorders associated with amyloids are no longer rare and they are rapidly becoming among the most common and debilitating medical conditions in the modern world (Knowles et al 2014). These disorders can either be strongly associated with aging, (Alzheimer’s), lifestyle, (type 2 diabetes) (Knowles et al 2014), or environmental factors (Lyme’s Disease) (Mattsson et al 2010).

The formation of amyloids starts when normal proteins in our body become truncated and/or misfolded. These proteins lose their normal function and begin to form thread like structures called fibrils which can attach to nerves, tissues and organs and eventually lead to the build up of plaque-like amyloids. Not only do amyloids have debilitating consequences on our health, the truncated and/or misfolded proteins themselves can wreck havoc on our bodies (Knowles et al 2014).

Diseases associated with amyloids can be grouped into three types: (1) neurodegenerative, in which aggregations occur in the brain (e.g. MS, Alzheimer’s, Parkinson’s, and Amyotrophic Lateral Sclerosis (ALS)); (2) localized amyloidosis, in which amyloids occurs in a single type of tissue other than the brain (e.g. the pancreas in type 2 diabetes), and (3) systemic amyloidosis, in which amyloids occur in multiple tissues other than the brain (e.g. Amyloid A (AA) amyloidosis, which is a complication of a number of diseases, infections, and cancer) (Chiti and Dobson 2006).

Recent research suggest that a variety of factors accelerate the amyloid formation process. These factors include pre-amyloid fragments from: yeast, bacteria and even animal meat. When these fragments are injected or orally ingested, they accelerate AA amyloidosis in mice which had been subjected to these inflammatory stimuli (Lundmark et al 2005). Lundmark et al (2005) suggest this may be of great importance for understanding the cause of human amyloid disease. Exposure (by ingestion or inhalation) to these naturally occurring fibrils may bring seeds that increase amyloid formation leading to disease in predisposed individuals.

Additional research on the onset of amyloidosis was done by Murakami et al (2014). They showed pre-amyloid fibrils from animal meat of cow or chicken can stimulate the formation of AA amyloidosis, suggesting ingesting this type of meat may prove to be a public health hazard. This research supports observations Teri has made while working with her clients. She has found excess sugar in our bodies enhance yeast and bacteria growth. Yeast, bacteria, and animal protein contribute to the formation of amyloids which can lead to a variety of aliments and diseases.

We have also discovered through many clients, that copper toxicity may be associated with the inability to digest protein; thereby contributing to the formation of amyloids. Metal ions, such as copper, have important functions throughout the body. However, with increasing age and/or oxidative stress, the body can be become comprised, decreasing the ability to transport these elements through the body where they are most needed. As a result, they become harmful to the human body. For example, copper has been linked to amyloid formation (Alexandrescru 2005 and DeToma et al 2012). Alzheimer research has shown that copper inhibits clearance of toxic amyloid proteins so they can not be excreted by the body’s natural mechanisms through the blood brain barrier which results in the formation of amyloid plaques (Singh et al 2013).

In our practice, we have seen hundreds of cases were protein malabsorption and copper were linked to MS, ALS, autism, Lyme’s Disease, cancer, Parkinson’s, type 2 diabetes, kidney disease, and endocrine and pituitary dysfunction. Symptoms indicating a person may be affected by protein malabsorption and copper include neuropathy, tingling in hands and feet, digestive dysfunction, fatigue, benign cysts, fibroids, neuromas (calcifications), tinnitus, low muscle tone, numbness, endometriosis, migraines, and anemia. Pathogenic yeast and bacterial infections which contribute to the amyloids may present the following symptoms: warts, flatulence, bloating, and diarrhea.

Through adopting a nutritional approach, eliminating yeast and pathogenic bacteria, reducing intestinal permeability , only eating wild animal protein and fish, only goat or sheep dairy,  and using proteolytic enzymes to destroy amyloids, the natural pathways of metabolism are supported and these conditions resolve. Proteolytic enzymes have been shown to be involved in the battle against cancer. Balashova and Lokhov (2010) found the proteolytic enzyme, trypsin, is effective at reducing cancer tumors. Also, Yamashita et al (2003) discovered trypsin is involved in tumor suppression. The proteolytic enzyme supplement we use in our treatments contains trypsin.
Agarwal AK, Garg R, Ritch A, and Sarkar P. Postural orthostatic tachycardia syndrome. Postgrad Med J. 2007. 83(981): 478–480.

Alexandrescu AT. Amyloid accomplices and enforcers. Protein Sci. 2005. 14(1):1-12.

Balashova EE, Lokhov PG. Proteolytically-cleaved Fragments of Cell-surface Proteins from Live Tumor Cells Stimulate Anti-tumor Immune Response In vitro. J Carcinogene Mutagene. 2010. 1:103.

Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem. 2006. 75:333-66.

Cozzi PJ, Abu-Jawdeh GM, Green RM, Green D. Amyloidosis in association with human immunodeficiency virus infection. Clin Infect Dis. 1992. 14(1):189-91.

DeToma AS, Salamekh S, Ramamoorthy A, Lim MH. Misfolded proteins in Alzheimer’s disease and type 2 diabetes. Chem. Soc. Rev. 2012. 41:608–621.

Knowles TP, Vendruscolo M, Dobson CM. The amyloid state and its association with protein misfolding diseases. Nat Rev Mol Cell Biol. 2014. 15(6):384-96.

Lundmark K,Westermark GT, Olsen A,Westermark P. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism. Proc. Natl. Acad. Sci. USA. 2005. 102:6098–102.

Mattsson N, Bremell D, Anckarsäter R, Blennow K, Anckarsäter H, Zetterberg H, Hagberg L. Neuroinflammation in Lyme neuroborreliosis affects amyloid metabolism. BMC Neurol. 2010. 10:51-56.

Murakami T, Ishiguro N, Higuchi K. Transmission of Systemic AA Amyloidosis in Animals. Vet Path. 2014. 51(2): 363-371.

Singh I, Sagare AP, Coma M, Perlmutter D, Gelein R, Bell RD, Deane RJ, Zhong E, Parisi M, Ciszewski J, Kasper RT, Deane R. Low levels of copper disrupt brain amyloid-β homeostasis by altering its production and clearance. Proc Natl Acad Sci USA. 2013. 110(36):14771-6.

Yamashita K, Mimori K, Inoue H, Mori M, Sidransky D. A tumor-suppressive role for trypsin in human cancer progression. Cancer Res. 2003. 63:6575–6578.


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