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The proteolytic activity of insulin-degrading enzyme: a mass spectrometry study

✍ Scribed by Giuseppe Grasso; Enrico Rizzarelli; Giuseppe Spoto

Publisher
John Wiley and Sons
Year
2009
Tongue
English
Weight
230 KB
Volume
44
Category
Article
ISSN
1076-5174

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✦ Synopsis

Abstract

The prominent role that insulin‐degrading enzyme (IDE) has on amyloidogenic peptides degradation has recently boosted a lot of attention toward this enzyme. Although many substrates are known to be degraded by IDE, little is known about the changes in the proteolytic activity of the enzyme upon modification of environmental factors.

In a previous work we have already shown the great potentiality of atmospheric pressure/laser desorption ionization‐mass spectrometry (AP/MALDI‐MS) for studying the interaction between IDE and insulin. Here, the activity of IDE was investigated regarding cleavage sites' preferentiality upon modification of environmental factors by AP/MALDI‐MS. The roles that IDE/insulin concentration ratio, reaction time, adenosine 5′‐triphosphate (ATP) and metal ions (Zn and Cu) have on the insulin cleavage pattern produced by IDE are investigated and a plausible interpretation involving the proteolytic action of the different IDE oligomeric forms is proposed. Copyright © 2009 John Wiley & Sons, Ltd.

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✍ Giuseppe Grasso; Enrico Rizzarelli; Giuseppe Spoto 📂 Article 📅 2007 🏛 John Wiley and Sons 🌐 English ⚖ 290 KB

## Abstract The prominent role that insulin degrading enzyme (IDE) has in the clearance of insulin as well as of other molecules such as amyloid‐β has recently drawn much interest in the scientific community toward this protease. In order to give an insight into the manner of interaction of IDE wit