A direct fluorescence-based technique for cellular localization of amylin

被引:1
|
作者
Pillay, Karen [1 ]
Govender, Patrick [1 ]
机构
[1] Univ KwaZulu Natal, Sch Life Sci, ZA-4000 Durban, South Africa
基金
新加坡国家研究基金会;
关键词
amylin; carboxyfluorescein; RIN-5F; type II diabetes; ISLET AMYLOID POLYPEPTIDE; PEPTIDE-BASED INHIBITORS; FIBRIL FORMATION; DIABETES-MELLITUS; AMINO-ACID; BETA; MEMBRANE; TOXICITY; IAPP; DYSFUNCTION;
D O I
10.1002/bab.1113
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Amylin has been implicated in type II diabetes because of its inherent property to misfold into toxic aggregates. Although it has been shown that amylin interacts with cell membranes, no study to date has monitored the association process using a direct approach. The present study uses confocal microscopy to identify the localization of carboxyfluorescein-labeled amylin in RIN-5F cells. In addition, the size of the aggregates that are formed was evaluated using nanoparticle tracking analysis. In support of previous findings, amylin was observed to interact with and remain associated with the cell membrane. The cell membrane-associated aggregates spanned a size range of 130-800nm.
引用
收藏
页码:384 / 392
页数:9
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