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Melvin R Hayden1,2, Suresh the 1 last update 06 Jul 2020 C Tyagi3
Melvin R Hayden1,2, Suresh C Tyagi3

  1. Department of Cardiovascular Atherosclerosis, Metabolism and Aging. Camdenton Community Health Center. Camdenton, MO, USA
  2. Preceptor in Family Medicine, Department of Family and Community Medicine, University of Missouri Columbia, MO, USAPreceptor in Family Medicine, Department of Family and Community Medicine, University of Missouri Columbia, MO, USA
  3. Department of Physiology and Biophysics, University of Mississippi Medical Center. Jackson, MS, USA
Corresponding Author
Melvin R Hayden
Department of Cardiovascular Atherosclerosis
Metabolism and Aging
Camdenton Community Health Center
P.O. Box 1140
Highway 5 North
Camdenton, Missouri 65020
USA
Phone +1-573.346.3019
E-mail [email protected]
Received 02 March 2001 Accepted 23 April 2001
 
Visit for more related articles at JOP. Journal of the Pancreas

Abstract

Amyloid deposits within the islet of the pancreas have been known for a century. In 1987, the islet amyloid precursor polypeptide (IAPP) amylin (a 37 amino acid) was discovered. Recently there has been an explosion of amylin’s importance in the development of type 2 diabetes mellitus (T2DM). This review is intended to share what is understood about amylin derived amyloid and the role it plays in T2DM. Whether islet amyloid is an epiphenomenona, a tombstone, or a trigger it leaves an indelible footprint in greater that 70% of the patients with T2DM. There is current data supporting the damaging role of intermediate sized toxic amyloid particles to the beta cell resulting in a beta cell defect which contributes to a relative deficiency or loss of insulin secretion. Within the islet there is an intense redox stress which may be associated with the unfolding of amylin’s native secondary structure compounding its amyloidogenic properties. In addition to the beta cell defect there may be an absorptive defect as a result of amyloid deposition in the basement membranes which form an envelope around the inta-islet capillary endothelium. We have an opportunity to change our current treatment modalities with newer medications and we should attempt to diagnose T2DM earlier and use these newer treatment strategies in combination to decrease glucotoxicity without elevating endogenous insulin and amylin. In the 21st century our goal should be to prevent remodeling, save the pancreatic islet, conquer islet amyloid, and amyloid diabetes.

 

Keywords
Amyloid; Apoptosis; Diabetes Mellitus; Diabetes Mellitus, Non-Insulin- Dependent; Glucose (toxicity) ; Insulin; Insulin Resistance; Islets of Langerhans; Oxidation- Reduction; Pancreas; Pancreatic Polypeptide; Reactive Oxygen Species

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AD: Alzheimer’s disease; AT- 1: angiotensin-1; CAPPP: Captopril Prevention Project; CRP: C-reactive protein; DECODE: Diabetes Epidemiology Collaborative analysis Of Diagnostic criteria in Europe; GAGs: glycosaminoglycans; GITS: gastrointestinal therapeutic system; HbA1c: hemoglobin A glycosylated c; hIAPP: human islet amyloid polypeptide; HOPE: Heart Outcomes Prevention Evaluation; IAPP: islet amyloid polypeptide; IGT: impaired glucose tolerance; NIDDM: non insulin dependent diabetes mellitus; PC: proprotein convertase; PDAY: Pathological Determinants of Atherosclerosis in Youth; PKC: protein kinase C; RAAS: renin– angiotensin–aldosterone–system; ROS: reactive oxygen species; RR: relative risk; SAA: serum amyloid A; SAP: serum amyloid P; T2DM: type 2 diabetes mellitus; UKPDS: United Kingdom Prospective Diabetes Study; WOSCOPS: West of Scotland Coronary Prevention Study

Historical Background and Introduction
2001 marks a century since Eugene L Opie first described the presence of a hyaline staining substance currently referred to as islet amyloid and noted its association with diabetes mellitus (Figure 1) [1]. In 1869, Paul Langerhans was the first to describe the endocrine pancreas and how these bundled cells appeared to be suspended and unconnected in an ocean of acinar cells (exocrine pancreas). Laguesse in 1893 named these mysterious cells the islands or islets of Langerhans (iles de Langerhans) to honor his colleague. Oskar Minkowski in 1889 made the discovery that connected the pancreas and diabetes in his depancreatized dogs [2]. In 1901, while at Johns Hopkins University, Eugene L Opie supplied a missing link by showing a pathological connection between diabetes and hyaline degeneration within the islet Langerhans had previously described.
The amyloidal nature of this hyaline material was established by Ahronheim in 1943 and confirmed by alkaline Congo red staining by Ehrlick JC and Ratner IM in 1961 [3, 4]. Westermark P in 1973 was able to demonstrate the fibrillar structure with the use of electron microscopy [5].
By 1987, two contemporary investigators (Westermark P and Cooper GJS) in separate laboratories discovered that this hyaline staining material consisted of a 37 amino acid monomer referred to as islet amyloid polypeptide (IAPP) by Westermark P and named amylin in 1988 by Cooper GJS (Figure 2) [6, 7].
Currently, there is a need to become more familiar with the relation of amylin’s overproduction and abnormal processing, storage and/or secretion with subsequent amylin derived amyloid deposition resulting in an alteration in structure and function within the islet and the associated beta cell dysfunction seen in type 2 diabetes mellitus (T2DM).
On January 26th, 2001 the Center for Disease Control in Atlanta, Georgia released to the major television networks world news that we are in the midst of an epidemic of pandemic proportions regarding T2DM. Due to the exponential growth of T2DM globally we will have to acknowledge, as did Opie, the disease process of remodeling of the endocrine pancreas associated with T2DM [8].

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We were instructed in medical school to include amyloidosis in our differential diagnosis for those patients with unexplained organ failure such as cardiac, hepatic, and renal failure. We were also told that we would not be expected to see many cases of amyloidosis unless we were cardiologists, nephrologists, or hematologists. Currently, this dictum should be pondered as T2DM and Alzheimer’s disease (AD) are two very common diseases that are growing exponentially as our society ages and they share a commonality. Amyloid is the common thread interweaving the two and is central to their origins and transforming histological changes. There may even be an association between them as Gregg EW and Narayan Venkat KM have suggested in their article [9]. We may need to add to our list of diabetic –opathies the term “cognopathy”.
Islet amyloid is considered by many to be an epi-phenomenon. Could amyloid be a “tombstone” or a “trigger” or a combination of both in regards to these two exponentially growing diseases? [10]. Whether or not it is causal (a trigger), or a bystander (a tombstone) or a combination we know that islet amyloid is being deposited in up to 70-90% of patients with T2DM and we must continue to study this phenomenon and better understand its plight [11, 12]. Amyloid is literally defined as being “starchlike” from the Greek root word amylo because these areas turned blue when iodine was applied to the tissue. This definition however is a misnomer as amyloid is a proteinaceous extracellular deposit resulting from the polymerization of polypeptides which undergo aggregation into antiparallel crossed beta pleated sheets. A characteristic feature of amyloid histologically is the positive staining with Congo red and birefringence on viewing with polarized light. Electron microscopy reveals interlacing bundles of parallel arrays of fibrils with a diameter of 7-10 nanometers (Figure 3). X-Ray diffraction reveals the adjacent amyloid fibrils to be organized as antiparallel crossed beta-pleated sheets. Amyloid is classically made up of the following.
Fibrillary (polypeptide) protein: Amyloidogenic polypeptides. Each form of amyloid has its own unique fibrillary polypeptide structure and these individual polypeptides serve as a monomeric unit of the polymerized aggregated beta-pleated sheet structures. In this article we are discussing the unique polypeptide amylin a 37 amino acid structure. Alzheimer''Alessio DA, Verchere CB, Kahn SE, Hoagland V, Baskin DG, Palmiter RD, Ensinck JW. Pancreatic expression and secretion of human islet amyloid polypeptide in a transgenic mouse. Diabetes 1994; 43:1457-61. [95046959] 
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