Both Types Of Diabetes Are Caused By The Same Mechanism


Mar 18, 2013
USA / Europe
Ray has written on the similarities between type I and type II diabetes and how they are really the same disease, but of different severity. Modern medicine claimed for years that the two types are fundamentally different, and type I is an auto-immune condition. This article claims scientists in New Zealand have finally managed to get evidence that Ray is right. ... /?id=12649 ... 4.abstract

The study above claims that both types of diabetes are caused by over-accumulation of amylin, which also happens to be a defining feature of hypothyroidism. In fact, chronically elevated amylin is thought to cause thyroid cancer.


Jul 24, 2013
It seems like there are vistas about amylin's action in the factors of decline, under the generative perspective of Dr. Peat.
Mol Neurodegener. 2014 Aug 22;9(1):30. [Epub ahead of print]
Neuroinflammation and neurologic deficits in diabetes linked to brain accumulation of amylin.
Srodulski S, Sharma S, Bachstetter AB, Brelsfoard JM, Pascual C, Xie XS, Saatman KE, Van Eldik LJ, Despa F.

"CONCLUSIONS: Hyperamylinemia promotes accumulation of oligomerized amylin in the brain leading to neurological deficits through an oligomerized amylin-mediated inflammatory response. Additional studies are needed to determine whether brain amylin accumulation may predispose to diabetic brain injury and cognitive decline."
Mol Cell Endocrinol. 2013 Jan 30;365(2):309-15. doi: 10.1016/j.mce.2012.11.013.
Amylin exerts osteogenic actions with different efficacy depending on the diabetic status.
Gutiérrez-Rojas I1, Lozano D, Nuche-Berenguer B, Moreno P, Acitores A, Ramos-Álvarez I, Rovira A, Novials A, Martín-Crespo E, Villanueva-Peñacarrillo ML, Esbrit P.


Apr 15, 2013
Thats interesting. Im still trying to understand a lot of Peats articles.
I dont know what amylin is and basically what I understood from Peats articles is that
unsaturated fats cause diabetes.
What causes over production of amylin and how do you prevent it or reverse it?


Jan 25, 2014
Fatty acids induce amylin expression and secretion by pancreatic beta-cells.
These data demonstrate that FAs differently regulate amylin and insulin expression and induce both amylin and insulin release. Ca(2+) and PKC signaling pathways and de novo-synthesized protein(s) were involved in FA-induced amylin expression. Induction of amylin production and release by FA may contribute to its biological functions under physiological conditions.

MCP-1 upregulates amylin expression in murine pancreatic β cells through ERK/JNK-AP1 and NF-κB related signaling pathways independent of CCR2.
Amylin is the most abundant component of islet amyloid implicated in the development of type 2 diabetes. Plasma amylin levels are elevated in individuals with obesity and insulin resistance. Monocyte chemoattractant protein-1 (MCP-1, CCL2) is involved in insulin resistance of obesity and type 2 diabetes. We investigated the effect of MCP-1 on amylin expression and the underlying mechanisms with murine pancreatic β-cell line MIN6 and pancreatic islets.
MCP-1 induces amylin expression through ERK1/2/JNK-AP1 and NF-κB related signaling pathways independent of CCR2. Amylin upregulation by MCP-1 may contribute to elevation of plasma amylin in obesity and insulin resistance.

Monocyte chemoattractant protein-1 (MCP-1): an overview.
Chemokines constitute a family of chemoattractant cytokines and are subdivided into four families on the basis of the number and spacing of the conserved cysteine residues in the N-terminus of the protein. Chemokines play a major role in selectively recruiting monocytes, neutrophils, and lymphocytes, as well as in inducing chemotaxis through the activation of G-protein-coupled receptors. Monocyte chemoattractant protein-1 (MCP-1/CCL2) is one of the key chemokines that regulate migration and infiltration of monocytes/macrophages. Both CCL2 and its receptor CCR2 have been demonstrated to be induced and involved in various diseases. Migration of monocytes from the blood stream across the vascular endothelium is required for routine immunological surveillance of tissues, as well as in response to inflammation. This review will discuss these biological processes and the structure and function of CCL2.

Antimicrobial activity of human islet amyloid polypeptides: an insight into amyloid peptides' connection with antimicrobial peptides.
Human islet amyloid polypeptide (hIAPP) shows an antimicrobial activity towards two types of clinically relevant bacteria. The potency of hIAPP varies with its aggregation states. Circular dichroism was employed to determine the interaction between hIAPP and bacteria lipid membrane mimic. The antimicrobial activity of each aggregate species is associated with their ability to induce membrane disruption. Our findings provide new evidence revealing the antimicrobial activity of amyloid peptide, which suggest a possible connection between amyloid peptides and antimicrobial peptides.

Common mechanism unites membrane poration by amyloid and antimicrobial peptides.
Poration of bacterial membranes by antimicrobial peptides such as magainin 2 is a significant activity performed by innate immune systems. Pore formation by soluble forms of amyloid proteins such as islet amyloid polypeptide (IAPP) is implicated in cell death in amyloidoses. Similarities in structure and poration activity of these two systems suggest a commonality of mechanism. Here, we investigate and compare the mechanisms by which these peptides induce membrane leakage and bacterial cell death through the measurement of liposome leakage kinetics and bacterial growth inhibition. For both systems, leakage occurs through the nucleation-dependent formation of stable membrane pores. Remarkably, we observe IAPP and magainin 2 to be fully cross-cooperative in the induction of leakage and inhibition of bacterial growth. The effects are dramatic, with mixtures of these peptides showing activities >100-fold greater than simple sums of the activities of individual peptides. Direct protein-protein interactions cannot be the origin of cooperativity, as IAPP and its enantiomer D-IAPP are equally cross-cooperative. We conclude that IAPP and magainin 2 induce membrane leakage and cytotoxicity through a shared, cross-cooperative, tension-induced poration mechanism.
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