Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby resulting in loss of pancreatic β-cells. Although type II diabetes is on the increase each year, possibly due to bad eating habits of modern society, research on the culprit for this disease is still in its early days. In addition, unlike the culprit for Alzheimer's disease, amyloid β-peptide, amylin has failed to receive attention worthy of being featured in an abundance of review articles. Thus, the aim of this paper is to shine the spotlight on amylin in an attempt to put it onto the top of researchers' to-do list since the secondary complications of type II diabetes have far-reaching and severe consequences on public health both in developing and fully developed countries alike. This paper will cover characteristics of the amylin aggregates, mechanisms of toxicity, and a particular focus on inhibitors of toxicity and techniques used to assess these inhibitors.

Bi-directional interactions between the endocrine and immune systems have been well described, particularly in relation to the growth hormone and adrenal axes. The possible effects of the thyroid gland on the immune system have not been clearly elucidated. This report describes a patient with congenital hypothyroidism and immune deficiency characterized by severe and persistent lymphopenia. The clinical course was punctuated by recurrent episodes of respiratory symptoms (in association with bronchiectasis) and diarrhea. The child ultimately died from overwhelming respiratory infection. It is proposed that the prolonged deficiency of thyroid hormone may be directly related to the impairment of the cellular immune system.

Amylin has been implicated in type II diabetes because of its inherent property to misfold into toxic aggregates. Although it has been shown that amylin interacts with cell membranes, no study to date has monitored the association process using a direct approach. The present study uses confocal microscopy to identify the localization of carboxyfluorescein-labeled amylin in RIN-5F cells. In addition, the size of the aggregates that are formed was evaluated using nanoparticle tracking analysis. In support of previous findings, amylin was observed to interact with and remain associated with the cell membrane. The cell membrane-associated aggregates spanned a size range of 130-800 nm.