Stochastic process algebra model of amyloidogenic processing under the influence of SORLA

Studies based on the amyloid hypothesis have shown that the proteolytic breakdown of amyloidogenic processing is the main pathology of Alzheimer's disease (AD). In this study, we focused on the effect of receptor SORLA, a 230 kDa type-1 transmembrane glycoprotein, after binding with the amyloid...

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Main Authors: Dela Cruz, Michelle Andrea A., Tenio, Grazielle Joy C.
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Language:English
Published: Animo Repository 2016
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Online Access:https://animorepository.dlsu.edu.ph/etd_bachelors/13989
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Institution: De La Salle University
Language: English
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spelling oai:animorepository.dlsu.edu.ph:etd_bachelors-62542021-05-12T02:43:06Z Stochastic process algebra model of amyloidogenic processing under the influence of SORLA Dela Cruz, Michelle Andrea A. Tenio, Grazielle Joy C. Studies based on the amyloid hypothesis have shown that the proteolytic breakdown of amyloidogenic processing is the main pathology of Alzheimer's disease (AD). In this study, we focused on the effect of receptor SORLA, a 230 kDa type-1 transmembrane glycoprotein, after binding with the amyloid precursor protein (APP) in the Trans-Golgi Network (TGN). We built a Stochastic Process Algebra (SPA) model to capture receptor SORLA's behavior and understand its influence in the APP processing. Through SPA modeling approach, the amyloidogenic processing is modeled as concurrent systems in continuous time Markov chains. We fitted the simulations of our model to the data published by Schmidt and colleagues in 2012. We built a model that initially considers the amyloidogenic processing to occur only in the endosomes. Then, we extended it so that the amyloidogenic processing also occurs in the TGN. In our study, we are able to validate the hypothesis proposed in Willnow and Spoelgen's study that there might be an indirect interaction between SORLA and [3-secretase. This indirect interaction takes place when APP and the receptor SORLA reverses, the APP that unbinds with SORLA may be cleaved by the [3-secretase in the TGN. Our SPA model brought new insights about SORLA's effect on the amyloidogenic processing, particularly to [3-secretase in the TGN. 2016-01-01T08:00:00Z text https://animorepository.dlsu.edu.ph/etd_bachelors/13989 Bachelor's Theses English Animo Repository Amyloid beta-protein precursor Stochastic processes Algebra Mathematics
institution De La Salle University
building De La Salle University Library
continent Asia
country Philippines
Philippines
content_provider De La Salle University Library
collection DLSU Institutional Repository
language English
topic Amyloid beta-protein precursor
Stochastic processes
Algebra
Mathematics
spellingShingle Amyloid beta-protein precursor
Stochastic processes
Algebra
Mathematics
Dela Cruz, Michelle Andrea A.
Tenio, Grazielle Joy C.
Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
description Studies based on the amyloid hypothesis have shown that the proteolytic breakdown of amyloidogenic processing is the main pathology of Alzheimer's disease (AD). In this study, we focused on the effect of receptor SORLA, a 230 kDa type-1 transmembrane glycoprotein, after binding with the amyloid precursor protein (APP) in the Trans-Golgi Network (TGN). We built a Stochastic Process Algebra (SPA) model to capture receptor SORLA's behavior and understand its influence in the APP processing. Through SPA modeling approach, the amyloidogenic processing is modeled as concurrent systems in continuous time Markov chains. We fitted the simulations of our model to the data published by Schmidt and colleagues in 2012. We built a model that initially considers the amyloidogenic processing to occur only in the endosomes. Then, we extended it so that the amyloidogenic processing also occurs in the TGN. In our study, we are able to validate the hypothesis proposed in Willnow and Spoelgen's study that there might be an indirect interaction between SORLA and [3-secretase. This indirect interaction takes place when APP and the receptor SORLA reverses, the APP that unbinds with SORLA may be cleaved by the [3-secretase in the TGN. Our SPA model brought new insights about SORLA's effect on the amyloidogenic processing, particularly to [3-secretase in the TGN.
format text
author Dela Cruz, Michelle Andrea A.
Tenio, Grazielle Joy C.
author_facet Dela Cruz, Michelle Andrea A.
Tenio, Grazielle Joy C.
author_sort Dela Cruz, Michelle Andrea A.
title Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
title_short Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
title_full Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
title_fullStr Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
title_full_unstemmed Stochastic process algebra model of amyloidogenic processing under the influence of SORLA
title_sort stochastic process algebra model of amyloidogenic processing under the influence of sorla
publisher Animo Repository
publishDate 2016
url https://animorepository.dlsu.edu.ph/etd_bachelors/13989
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