|星空彩票电脑版
%A ZHANG Nan，XING Yuan，ZHANG Wei %T
Molecular Structure，Cytotoxicity and Inhibitive Factors of Human Amylin%0 Journal Article %D 2016 %J ACTA NEUROPHARMACOLOGICA %R 10.3969/j.issn.2095-1396.2016.04.008 %P 50-64 %V 6 %N 4 %U {http://actanp.hebeinu.edu.cn/CN/abstract/article_328.shtml} %8 2016-08-26 %X Human amylin （hAmylin） is the major component of amyloid deposits in the pancreatic islets of patients with diabetes mellitus 2 （DM2）. Physiologically，mature hAmylin，a 37 amino acid peptide，is co-produced and co-secreted with insulin in a ratio of 1∶100 in islet β-cells. hAmylin is released in response to the stimuli that lead to insulin secretion. The monomeric hAmylin is an unstable and unfolded peptide which tends to accumulate and form oligomer or fibril. The unstable state of hAmylin monomer is closely related to hAmylin cytotoxicity. Accumulating evidences suggest that hAmylin amyloid accumulation that accompany DM2 is not just an insignificant phenomenon derived from the disease progression but that hAmylin aggregation induces processes that impair the functionality and the viability of β-cells. In this review，we particularly focus on hAmylin structure，hIAPP aggregation and hAmylin-membrane interactions. We will discuss recent findings on the mechanism of hAmylin-membrane damage and hIAPP-induced cell death. Finally，the development of successful anti-amyloidogenic agents that prevent hAmylin fibril formation have been discussed.