Results 141 to 150 of about 5,646 (167)

Polymorphic cross-seeding amyloid assemblies of amyloid-β and human islet amyloid polypeptide

Physical Chemistry Chemical Physics, 2015
Epidemiological studies have shown that the development of Alzheimer's disease (AD) is associated with type 2 diabetes (T2D), but it still remains unclear how AD and T2D are connected.
Mingzhen, Zhang, Rundong, Hu, Hong, Chen, Yung, Chang, Jie, Ma, Guizhao, Liang, Jingyan, Mi, Yaru, Wang, Jie, Zheng   +8 more
openaire   +2 more sources

Volumetric properties of human islet amyloid polypeptide in liquid water

Physical Chemistry Chemical Physics, 2010
The volumetric properties of human islet amyloid polypeptide (hIAPP) in water were studied in a wide temperature range by computer simulations. The intrinsic density rho(p) and the intrinsic thermal expansion coefficient alpha(p) of hIAPP were evaluated by taking into account the difference between the volumetric properties of hydration and bulk water.
I, Brovchenko, M N, Andrews, A, Oleinikova   +2 more
openaire   +2 more sources

Oophorectomy promotes islet amyloid formation in human islet amyloid polypeptide transgenic mice.

Diabetes, 2001
Islet amyloid polypeptide (IAPP) (amylin) is the unique peptide component of the amyloid deposits found at autopsy in >90% of subjects with type 2 diabetes (1). These amyloid deposits are thought to replace islet mass and to thereby contribute to the -cell dysfunction of the disease.
R L, Hull, C B, Verchere, S, Andrikopoulos, F, Wang, J, Vidal, S E, Kahn   +5 more
openaire   +2 more sources

Cleavage agents for soluble oligomers of human islet amyloid polypeptide

JBIC Journal of Biological Inorganic Chemistry, 2008
Soluble oligomers of human islet amyloid polypeptide (h-IAPP) are implicated in the initiation of beta-cell apoptosis leading to type 2 diabetes mellitus (T2DM). Cleavage of the h-IAPP included in an oligomer may provide a novel method for reducing the level of h-IAPP oligomers, offering a new therapeutic option for T2DM. From the combinatorial library
Junghun, Suh, Woo Suk, Chei, Tae Yeon, Lee, Min Gyum, Kim, Sang Ho, Yoo, Keunhong, Jeong, Jae Young, Ahn   +6 more
openaire   +2 more sources

Silibinin inhibits the toxic aggregation of human islet amyloid polypeptide

Biochemical and Biophysical Research Communications, 2012
In type 2 diabetes mellitus (T2DM), misfolded human islet amyloid polypeptide (hIAPP) forms amyloid deposits in pancreatic islets. These amyloid deposits contribute to the dysfunction of β-cells and the loss of β-cell mass in T2DM patients. Inhibition of hIAPP fibrillization has been regarded as a potential therapeutic approach for T2DM.
Biao, Cheng, Hao, Gong, Xiaochao, Li, Yue, Sun, Xin, Zhang, Hong, Chen, Xinran, Liu, Ling, Zheng, Kun, Huang   +8 more
openaire   +2 more sources

Effects of Arginine on the Secretion of Insulin and Islet Amyloid Polypeptide in Humans

Pancreas, 1995
Islet amyloid polypeptide (IAPP) is synthesized in islet B cells and stored in the secretory granules. We examined whether IAPP and insulin are released in parallel in humans. Arginine hydrochloride (5 g) was injected intravenously at three glucose levels in 11 healthy 58-year-old female subjects.
H, Larsson, B, Ahrén
openaire   +2 more sources

Role of islet amyloid polypeptide secretion in insulin-resistant humans

Diabetologia, 1994
Although it is generally accepted that islet amyloid polypeptide is cosecreted with insulin, relatively few data on its kinetics are available. We therefore studied the dynamics of islet amyloid polypeptide release following oral and frequently sampled intravenous glucose tolerance tests in comparison to insulin and C-peptide using mathematical model ...
A, Kautzky-Willer, K, Thomaseth, G, Pacini, M, Clodi, B, Ludvik, C, Streli, W, Waldhäusl, R, Prager   +7 more
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Co-assembly of human islet amyloid polypeptide (hIAPP)/insulin

Chem. Commun., 2012
The pathogenesis of type II diabetes can be linked to cosecreted hIAPP/insulin interacting with cell membranes. Here we investigate the nanostructures by co-assembling hIAPP and insulin on surfaces. By tuning the hIAPP/insulin ratio, atomic force microscopy reveals the resulting nanostructure morphology changes from fibrils to oligomers, to annular ...
Liu, Peng, Zhang, Shuai, Chen, Mei-Sha, Liu, Qian, Wang, Chenxuan, Wang, Chen, Li, Yan-Mei, Besenbacher, Flemming, Dong, Mingdong; id_orcid 0000-0002-2025-2171   +8 more
openaire   +3 more sources

Cloning and expression of human islet amyloid polypeptide in cultured cells

Biochemical and Biophysical Research Communications, 2007
Efforts to clone amyloidogenic proteins in the cells often have resulted in cell death. We report successful cloning and expression of recombinant human islet amyloid polypeptide (hIAPP) in cultured mammalian cells. Amylin gets secreted, forms fibrils that are toxic to target cells like beta cells of rat and human.
Susinjan, Bhattacharya, J Naveena Lavanya, Latha, R, Kumresan, Shashi, Singh   +3 more
openaire   +2 more sources

Zinc stabilization of prefibrillar oligomers of human islet amyloid polypeptide

Chemical Communications, 2013
The aggregation of human islet amyloid polypeptide (hIAPP) has been linked to beta-cell death in type II diabetes. Zinc present in secretory granules has been shown to affect this aggregation. A combination of EXAFS, NMR, and AFM experiments shows that the influence of zinc is most likely due to the stabilization of prefibrillar aggregates of hIAPP.
Brender JR, Krishnamoorthy J, Messina GML, Deb A, Vivekanandan S, LA ROSA, Carmelo, Penner Hahn JE, Ramamoorthy A.   +7 more
openaire   +3 more sources