Since I see amyloid plaque as a serious limiting factor for a cure for
type 2 diabetes, I am providing the following:

Recent Abstracts (about one year or less since release):

Increased Dietary Fat Promotes Islet Amyloid Formation and ß-Cell
Secretory Dysfunction in a Transgenic Mouse Model of Islet Amyloid
http://diabetes.diabetesjournals.org/cgi/content/abstract/52/2/372

Replication Increases ß-Cell Vulnerability to Human Islet Amyloid
Polypeptide-Induced Apoptosis
http://diabetes.diabetesjournals.org/cgi/content/abstract/52/7/1701

Prevalence and Clinicopathological Characteristics of Islet Amyloid in
Chinese Patients With Type 2 Diabetes
http://diabetes.diabetesjournals.org/cgi/content/abstract/52/11/2759

Increased ß-Cell Apoptosis Prevents Adaptive Increase in ß-Cell Mass in
Mouse Model of Type 2 Diabetes
http://diabetes.diabetesjournals.org/cgi/content/abstract/52/9/2304

Full Articles:

Islet Amyloid Develops Diffusely Throughout the Pancreas Before Becoming
Severe and Replacing Endocrine Cells
http://diabetes.diabetesjournals.org/cgi/content/full/50/11/2514

"ISLET AMYLOID IN TYPE 2 DIABETES: OTHER COMPONENTS OF POTENTIAL
IMPORTANCE
ApoE binds triglyceride-rich lipoproteins and is important
in reverse cholesterol transport. The human apoE gene is polymorphic,
resulting in the expression of three different isoforms in humans. ...
We and evidence for apoE in islet amyloid. evidence for apoE in islet
amyloid (52,53). On immunocyto-chemistry, islet amyloid deposits
associated with type 2 diabetes fluoresce intensely for apoE
immunoreactivity, whereas islets from subjects with normal glucose
tolerance do not, suggesting that human islets normally do not contain
this apolipoprotein (Fig. 1). It would also appear that apoE is the
sole apolipoprotein present in islet amyloid deposits, because our
immunostaining studies have failed to demonstrate the presence of either
apoA and apoB in islets or amyloid deposits from either subjects with
normal glucose tolerance or those with hyperglycemia (S.E.K. et al.,
unpublished observations).
Although we were able to show that apoE is present in islet amyloid of
humans, monkeys, and our transgenic mice that develop islet amyloid, we
have been unable to demonstrate the presence of apoE mRNA in normal
human and mouse islets [i.e., genetic material from outside the islets]
(S.E.K. et al., unpublished observations), suggesting that its presence
in islet amyloid deposits results from its transport from a distant site
via the circulation rather than from its being a product of the
beta-cell, as is IAPP. Distant biosynthesis contrasts with the scenario
in Alzheimer’s disease, in which an abundance of apoE mRNA has been
demonstrated in astrocytes shown to synthesize and secrete the protein,
which is compatible with apoE production near the site of amyloid
deposition. Because it appears that the source of the apoE in islet
amyloid is extrapancreatic, it seems most likely that it is produced in
the liver, which is a major site of production of this apolipoprotein or
macrophages circulating through the islet. ... Based on these findings
in Alzheimer’s disease and our finding of apoE in islet amyloid, it is
very possible
that apoE participates in islet amyloidogenesis. ...
IS ISLET AMYLOID AN EARLY OR LATE EVENT IN THE
PATHOGENESIS OF TYPE 2 DIABETES?
... To our surprise, however, we found that two-thirds of our male
transgenic animals that had been consistently normoglycemic
also developed islet amyloid deposits, indicating that hyperglycemia is
not a prerequisite for islet amyloid formation.
DIETARY FAT: A UNIFYING HYPOTHESIS FOR THE ISLET
AMYLOID OF TYPE 2 DIABETES?
... The mechanism by which a high-fat diet produces beta-cell
dysfunction is not entirely clear. It may be related to exposure to
increased circulating levels of free fatty acids, to triglyceride
accumulation in the beta-cell, and ultimately to apoptosis of the cell.
... Based on the association between dietary fat intake and the
development of type 2 diabetes in humans, on the association between the
effect of increased dietary fat and a lack of beta-cell adaptation in
dogs and mice, and on our observation that an increase in dietary fat
induces islet amyloid in our human IAPP transgenic mice, we propose the
following hypothesis to explain the development of amyloid in type
diabetes (Fig. 5). Beta-Cell dysfunction is a necessity that may be
genetically determined and/or influenced by the environment. We propose
that any factor that impairs (pro)IAPP processing, sorting, storage,
secretion, or degradation may result in the initiation of islet amyloid
formation. The propensity for
this amyloidogenic product to form fibrils in subjects with type 2
diabetes and not in healthy subjects, rather than depending solely on
the absolute amount of IAPP being produced or released, may be due to
the release of incompletely processed pro-IAPP or to an alteration in
intragranular constituents resulting in reduced IAPP solubility. The
initiation of amyloid fibril formation would need only a minor
alteration in beta-cell function that would not necessarily be
associated with hyper-glycemia. Once a nidus of amyloid fibrils has
formed, the process is progressive, and amyloid can eventually be
visualized using electron microscopy and then with the typical staining
techniques using light microscopy. These amyloid fibrils result in the
loss of islet cell mass either through a direct toxic effect of
extracellular fibrils, as demonstrated in vitro, or by their progressive
space occupancy, which
may reduce the ability of nutrients to reach the cell, or may
destroy cells, simply by their occupying islet space. The toxic effect
of fibrils may be mediated through different mechanisms, such as
reactive oxygen species and apoptosis, as observed with other types of
amyloid,
such as that from Abeta in Alzheimer’s disease. As islet mass is
reduced, insulin release declines and progressive hyperglycemia ensues.
Hyperglycemia per se, by virtue of its ability to stimulate IAPP
biosynthesis, also feeds forward in a vicious cycle that results in
further islet amyloid development and beta-cell destruction. It has also
been suggested that glycation of IAPP by circulating glucose may enhance
amyloid fibril formation. The presence of apoE and perlecan in amyloid
fibrils, and their potential ability to stabilize these fibrils, suggest
that they also have a role in islet amyloidogenesis. Given that dietary
fat increases apoE biosynthesis, it seems plausible that this production
of enhanced apoE (and perlecan) may stabilize and could thus reduce
degradation of existing amyloid fibrils, thereby providing a mechanism
for continued amyloidogenesis and further promoting the ultimate
development of the clinical syndrome." Source: Islet amyloid: a
long-recognized but underappreciated pathological feature of type 2
diabetes
http://diabetes.diabetesjournals.org/cgi/reprint/48/2/241.pdf

Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid
Polypeptide
http://www.jbc.org/cgi/content/full/276/36/34156

Identification of a Heparin Binding Domain in the N-terminal Cleavage
Site of Pro-islet Amyloid Polypeptide
http://www.jbc.org/cgi/content/full/276/20/16611

The Prohormone Convertase Enzyme 2 (PC2) Is Essential for Processing
Pro-Islet Amyloid Polypeptide at the NH2-Terminal Cleavage Site
http://diabetes.diabetesjournals.org/cgi/content/full/50/3/534

May be of interest to you:

Insulin and Amylin Release Are Both Diminished in First-Degree Relatives
of Subjects With Type 2 Diabetes
http://care.diabetesjournals.org/cgi/content/full/25/2/292

Frank