Caspase-3 activity inhibition in selenophilic ...

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Caspase-3 activity inhibition in selenophilic filamentous fungi

Name:Personal
Hannah Postma
Role :Text(marcrelator)
creator

Name:Personal
Dan Wu
Role :Text(marcrelator)
creator

Name:Personal
Dr. Ami Wangeline
Role :Text(marcrelator)
creator

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text
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Powerpoint/PDF
Origin Information Place
Laramie, Wyoming

University of Wyoming
(keyDate="yes")
4/24/2010

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born digital

abstract
Apoptosis is the process of programmed cell death that occurs in organisms. In the cell metabolic process, apoptotic imbalance can lead to many diseases, including cancer and Alzheimer's disease. Caspase-3 is a member of the interleukin-1b converting enzyme (ICE) family of cysteine proteases and several reports suggest that Caspase-3 is a fundamental component of the apoptotic signaling cascade. Our research used the CASPASE-3 Assay Kit for Drug Discovery (BioMol) to detect inhibition of activity of Caspase-3 by providing a substrate that is cleaved by caspase-3 producing a colorimetrically active product. Inhibition capacity was determined in total extracts from several of genera of selenophilic filamentous fungi cultured with and without Se. Absorbency was recorded over time, and the slopes were analyzed to determine activity while using a provided inhibitor and a non-inhibited control. Extracts from Absidia (zygomycota) and Fusarium (ascomycota) were both found to have high inhibition against the caspase-3 enzyme regardless of growth conditions and extraction method, where as inhibitory impact of other extracts seemed to correlate with extraction method. These inhibitors have the potential to impact apoptotic events when cell death is incorrectly triggered due to disease and we will attempt to elucidate the specific compounds in future studies.
note
From - Undergraduate Research Day 2010 - Celebration of Research - Abstracts
Subject
Undergraduate Research Day

Related Item:Host Title Information
Undergraduate Research Day 2010

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http://hdl.handle.net/10176/wyu:706

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http://digital.uwyo.edu/copyright.htm