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Interactions of human islet amyloid polypeptide with lipid structure of different curvatures

Theoretical & Applied Mechanics Letters 2020年第6期10卷 412-418页

作者： Le Mei Wenhui Shen Xuwei Wu Jie Liu Dechang Li Baohua Ji Biomechanics and Biomaterials Laboratory Department of Applied MechanicsBeijing Institute of TechnologyBeijing 100081China Institute of Applied Mechanics Department of Engineering MechanicsZhejiang UniversityHangzhou 310027China

Curvature is one of the most important features of lipid membranes in living cells,which significantly influences the structure of lipid membranes and their interaction with *** the human islet amyloid polypeptide(h IAPP),an important protein related to the pathogenesis of type II diabetes,as an example,we performed molecular dynamics(MD)simulations to study the interaction between the protein and the lipid structures with varied *** found that the lipids in the high curvature membrane pack loosely with high *** h IAPP initially forms H-bonds with the membrane surface that anchored the protein,and then inserts into the membrane through the hydrophobic interactions between the residues and the hydrophobic tails of the lipids.h IAPP can insert into the membrane more deeply with a larger curvature and with a stronger binding *** result provided important insights into the mechanism of the membrane curvature-dependent property of proteins with molecular details.

关键词： Lipid membrane Curvature human islet amyloid polypeptide Molecular dynamics

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A pancreatic player in dementia:pathological role for islet amyloid polypeptide accumulation in the brain

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Neural Regeneration Research 2023年第10期18卷 2141-2146页

作者： Angelina S.Bortoletto Ronald J.Parchem Center for Cell and Gene Therapy Stem Cell and Regenerative Medicine CenterDepartment of NeuroscienceDepartment of Molecular and Cellular BiologyTranslational Biology and Molecular Medicine ProgramMedical Scientist Training ProgramBaylor College of MedicineHoustonTXUSA

Type 2 diabetes mellitus patients have a markedly higher risk of developing *** multiple factors contribute to this predisposition,one of these involves the increased secretion of amylin,or islet amyloid polypeptide,that accompanies the pathophysiology of type 2 diabetes *** amyloid polypeptide accumulation has undoubtedly been implicated in various forms of dementia,including Alzheimer’s disease and vascular dementia,but the exact mechanisms underlying islet amyloid polypeptide’s causative role in dementia are *** this review,we have summarized the literature supporting the various mechanisms by which islet amyloid polypeptide accumulation may cause neuronal damage,ultimately leading to the clinical symptoms of *** discuss the evidence for islet amyloid polypeptide deposition in the brain,islet amyloid polypeptide interaction with other amyloids implicated in neurodegeneration,neuroinflammation caused by islet amyloid polypeptide deposition,vascular damage induced by islet amyloid polypeptide accumulation,and islet amyloid polypeptide-induced *** are very few therapies approved for the treatment of dementia,and of these,clinical responses have been controversial at ***,investigating new,targetable pathways is vital for identifying novel therapeutic strategies for treating *** such,we conclude this review by discussing islet amyloid polypeptide accumulation as a potential therapeutic target not only in treating type 2 diabetes mellitus but as a future target in treating or even preventing dementia associated with type 2 diabetes mellitus.

关键词： Alzheimer’s disease amylin amyloid dementia diabetes human islet amyloid polypeptide islet amyloid polypeptide protofibrils type 2 diabetes mellitus vascular dementia

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Amylin amyloid as shells protecting immune attack

Amylin amyloid as shells protecting immune attack

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第十二届全国免疫学学术大会

作者： Qiao Yongchao Wang Min Pan Yan-hong Chen Yin-ling Zhang Xiao-xi Zhao Hai-lu Guilin Medical Universitiy

Objective:The monomelic proteins of human islet amyloid polypeptide(hIAPP) highly expressed in human pancreatic islets could trigger self-oligomerization which could independently causes fibril formation and facilitate disease progression in type 2 diabetes mellitus(T2 DM) patients,here,we proved that the existence of amyloid oligomers in human pancreatic islets could protect pancreas islet from inflammatory cell ***:Serial tissue sections(4 mm) of pancreas were obtained from a 75-year lady autopsy with lymphoplasmacytic sclerosing pancreatitis and stained for CD3,CD4,CD8,and CD20,from a 70-year gentleman autopsy with pancreatic endocrine tumor and stained for leukocyte common antigen,glucagon and IAPP,from a 46-year lady autopsy with pancreatic insulinoma and stained for amyloid deposits and insulin,and from an 84-year gentleman autopsy with type 2 diabetes and stained for CD68,CD3,CD20,and ***:As we found that the pancreas islet in T2 DM shows less infiltrating lymphocytes(mononuclear macrophage,T cell and B cell) in the protection of amylin compared with the duct(all pamyloid deposits coexists with diminished chronic inflammatory infiltrates and expression of insulin by tumor cells(pamyloid-free islet,the amyloid-affected islet shows less chronic inflammatory infiltrates(pamyloid oligomers in human pancreatic islets could protect immune attack of lymphocytes and delay the progress of T2 *** effort is needed to investigate the clinical implications of the amyloid oligomerization in the pathogenesis of type 2 diabetes.

关键词： Amylin amyloid human islet amyloid polypeptide Type 2 diabetes

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