Results 131 to 140 of about 5,646 (167)

Amyloid protein in somatostatinoma differs from human islet amyloid polypeptide

Acta Endocrinologica, 1991
Abstract. Amyloid deposits in somatostatinomas are rare observations. To examine the characteristics of this amyloid, we compared amyloid deposits in a somatostatinoma to those found in pancreatic tissue in patients with Type II diabetes mellitus and in insulinomas, using immunohistochemical techniques and specific antibodies to islet amyloid ...
H, Ohsawa, A, Kanatsuka, Y, Tokuyama, T, Yamaguchi, H, Makino, S, Yoshida, H, Horie, A, Mikata, Y, Kohen   +8 more
openaire   +2 more sources

Amyloid aggregation and deposition of human islet amyloid polypeptide at membrane interfaces

The FEBS Journal, 2014
Amyloid deposition of human islet amyloid polypeptide (hIAPP) within the islets of Langerhans is a pathological feature of type 2 diabetes mellitus. Substantial evidence indicates that the membrane‐mediated aggregation and subsequent deposition of hIAPP are linked to dysfunction and death of pancreatic β‐cells, but the molecular processes of hIAPP ...
Kenji, Sasahara, Kenichi, Morigaki, Kyoko, Shinya   +2 more
openaire   +2 more sources

The Role of His-18 in Amyloid Formation by Human Islet Amyloid Polypeptide

Biochemistry, 2005
The 37-residue islet amyloid polypeptide (IAPP) is the major protein component of the amyloid deposits found in type-II diabetes. IAPP is stored in a relatively low pH environment in the pancreatic secretory granules prior to its release to the extracellular environment. Human IAPP contains a single histidine at position 18.
Andisheh, Abedini, Daniel P, Raleigh
openaire   +2 more sources

Human Islet Amyloid Polypeptide Accumulates at Similar Sites in Islets of Transgenic Mice and Humans

Diabetes, 1994
The cellular mechanisms responsible for conversion of islet amyloid polypeptide (IAPP) into insoluble amyloid deposits in non-insulin-dependent diabetes mellitus (NIDDM) are not clear. Overexpression of IAPP and the amino acid sequence of human IAPP (hIAPP) have both been implicated.
E J, de Koning, J W, Höppener, J S, Verbeek, C, Oosterwijk, K L, van Hulst, C A, Baker, C J, Lips, J F, Morris, A, Clark   +8 more
openaire   +2 more sources

Triterpenoids impede the fibrillation and cytotoxicity of human islet amyloid polypeptide

International Journal of Biological Macromolecules, 2022
The inhibition of human islet amyloid polypeptide (hIAPP) deposition to block its toxicity is an important strategy for the prevention and treatment of type II diabetes mellitus (T2DM).Natural compounds with pharmacological properties and low toxicity can serve as a good point to discover potential inhibitors of protein misfolding, which may be useful ...
Ting Zheng, Yanan Wang, Cong Zhao, Jufei Xu, Xiangyi Huang, Weihong Du   +5 more
openaire   +2 more sources

New Human Islet Amyloid Polypeptide Fragments Susceptible to Aggregation

Chemistry & Biodiversity, 2020
AbstractHuman Islet Amyloid Polypeptide (hIAPP) plays a key role in the pathogenesis of type II diabetes. The aim of this research was to search for new amyloidogenic fragments of hIAPP. An initial attempt to predict the amyloidogenic cores of polypeptides/proteins using five different computer programs did not provide conclusive results. Therefore, we
Kamil Rozniakowski, Andrzej Fraczyk, Krystian Galecki, Joanna Wietrzyk, Beata Filip‐Psurska, Justyna Fraczyk, Zbigniew J. Kaminski, Beata Kolesinska   +7 more
openaire   +2 more sources

Islet amyloid polypeptide in human insulinomas. Evidence for intracellular amyloidogenesis

Diabetes, 1994
Amyloid deposits that characteristically form in the pancreatic islets of patients with non-insulin-dependent diabetes mellitus (NIDDM) and in insulinomas are both derived from islet amyloid polypeptide (IAPP). Evidence from previous studies has suggested that deposition of IAPP-derived amyloid is related to inherent amyloidogenic sequences present ...
T D, O'Brien, A E, Butler, P C, Roche, K H, Johnson, P C, Butler   +4 more
openaire   +2 more sources

Procyanidine resists the fibril formation of human islet amyloid polypeptide

International Journal of Biological Macromolecules, 2021
Human islet amyloid polypeptide (hIAPP) is widely studied due to its close correlation with the pathogenic mechanism of type II diabetes mellitus (T2DM). Bioflavonoids have been used in the neurodegeneration and diabetes studies. However, the structure-activity relationship remains unclear in many of these compounds.
Jufei, Xu, Ting, Zheng, Xiangyi, Huang, Yanan, Wang, Guowei, Yin, Weihong, Du   +5 more
openaire   +2 more sources

Sensitivity of Amyloid Formation by Human Islet Amyloid Polypeptide to Mutations at Residue 20 [PDF]

Journal of Molecular Biology, 2012
Islet amyloid polypeptide (IAPP, amylin) is responsible for amyloid formation in type 2 diabetes and in islet cell transplants. The only known natural mutation found in mature human IAPP is a Ser20-to-Gly missense mutation, found with small frequency in Chinese and Japanese populations. The mutation appears to be associated with increased risk of early-
Ling-Hsien Tu, Rehana Akter, Ann Marie Schmidt   +2 more
exaly   +3 more sources

Islet amyloid polypeptide (IAPP) and pro-IAPP immunoreactivity in human islets of Langerhans

Diabetes Research and Clinical Practice, 1989
Islet amyloid polypeptide (IAPP) is a 37-amino-acid putative hormone which is expressed by islet B-cells and most probably is co-released with insulin. IAPP is synthesized as an 89-amino-acid prepropeptide in which IAPP is flanked by two short peptides. The two short peptides are ultimately cleaved off at basic residues.
P, Westermark, U, Engström, G T, Westermark, K H, Johnson, J, Permerth, C, Betsholtz   +5 more
openaire   +2 more sources