The interaction between Ezrin & Aquaporin 2
(2020) KEMK10 20201Department of Chemistry
- Abstract
- Water is a large part of life on earth and is also a large part of the human body which is why it is so important. Aquaporins are water channels that transports water through a process called trafficking. Aquaporin 2 is one of these aquaporins and with a faulty trafficking or mutations it could lead to nephrogenic diabetes insipidus and severe dehydration. Ezrin is a protein in the body which FERM-domain has been seen to interact with proteins as well as AQP2. The study was conducted to see if AQP2 and ezrin had some interactions through MST analysis.
Two proteins were tested, the full-length ezrin and the FERM-domain which were stained with Alexa-488 dye. A 1:1 dilution series were made for the MST.The results concluded that AQP2 and... (More) - Water is a large part of life on earth and is also a large part of the human body which is why it is so important. Aquaporins are water channels that transports water through a process called trafficking. Aquaporin 2 is one of these aquaporins and with a faulty trafficking or mutations it could lead to nephrogenic diabetes insipidus and severe dehydration. Ezrin is a protein in the body which FERM-domain has been seen to interact with proteins as well as AQP2. The study was conducted to see if AQP2 and ezrin had some interactions through MST analysis.
Two proteins were tested, the full-length ezrin and the FERM-domain which were stained with Alexa-488 dye. A 1:1 dilution series were made for the MST.The results concluded that AQP2 and FL as well as FERM has an interaction.The KD was determined by a model in a computer program where it was 48±22 μM for FL and 405±548 μM for FERM. However the confidence interval for FERM was larger than the actual value making it unreliable. The results for FL and FERM should be approximately the same because it is said that AQP2 reacts with the FERM-domain. A study, although, has stated that residues in the C-terminus of ezrin are critical for interaction. More MST-studies has to be conducted to get a conclusive result with a larger dilution series and more tests. (Less) - Popular Abstract (Swedish)
- Vattenkanaler kallade akvaporiner finns i kroppen för att transportera vatten och därmed reguleras vattennivån i cellerna i kroppen. Denna process kallas trafficking vilket förenklat betyder att akvaporinen förflyttas och blir aktiverad eller avaktiverad för att öka eller minska flödet av vatten. Om denna process inte fungerar på ett korrekt sätt, kan diverse sjukdomar uppstå som orsakar problem för personen, t.ex. en försämrad förmåga att koncentrera urinet. Ezrin är ett protein som kan finnas i många delar av kroppen och har setts interagera med akvaporiner. Denna studie gjordes för att bestämma om ezrin och ett akvaporin som finns i en del av njurkanalerna kallat akvaporin 2 interagerar med varandra då detta skulle kunna påverka trafficking.
... (More) - Vattenkanaler kallade akvaporiner finns i kroppen för att transportera vatten och därmed reguleras vattennivån i cellerna i kroppen. Denna process kallas trafficking vilket förenklat betyder att akvaporinen förflyttas och blir aktiverad eller avaktiverad för att öka eller minska flödet av vatten. Om denna process inte fungerar på ett korrekt sätt, kan diverse sjukdomar uppstå som orsakar problem för personen, t.ex. en försämrad förmåga att koncentrera urinet. Ezrin är ett protein som kan finnas i många delar av kroppen och har setts interagera med akvaporiner. Denna studie gjordes för att bestämma om ezrin och ett akvaporin som finns i en del av njurkanalerna kallat akvaporin 2 interagerar med varandra då detta skulle kunna påverka trafficking.
Två versioner av ezrin renades fram, det ena var hela proteinet medan den andra versionen var ungefär halva proteinet vilket kallas FERM. Dessa renades fram med och interaktionen med akvaporin 2 kunde studeras i en MST som mäter hur molekylerna rör sig jämfört med varandra då en av dem är färgad med en fluroscerande färg. Resultatet var att en interaktion mellan ezrin och akvaporin 2 finns för båda versionerna vilket andra studier har pekat på. Det kunde med säkerhet sägas att hela ezrin-proteinet binder till akvaporin 2 medan det inte kan sägas med säkerhet hur bra FERM-delen av ezrin binder med akvaporin 2. För att bestämma med säkerhet och hur bra de faktiskt band till akvaporin 2, hade fler studier fått göras.
Dessa resultat kan användas för att vidareutveckla metoden samt bygga på resultaten. Genom detta kan man förstå trafficking mer och förståelsen kan leda till bättre mediciner för de sjukdomar orsakad av icke-fungerande trafficking. (Less)
Please use this url to cite or link to this publication:
http://lup.lub.lu.se/student-papers/record/9024842
- author
- Aulin, Hanna LU
- supervisor
- organization
- course
- KEMK10 20201
- year
- 2020
- type
- M2 - Bachelor Degree
- subject
- keywords
- Biochemistry, Biokemi, Aquaporins, AQP2, Ezrin, Trafficking
- language
- English
- id
- 9024842
- date added to LUP
- 2020-09-14 12:38:26
- date last changed
- 2020-09-14 12:38:26
@misc{9024842,
abstract = {{Water is a large part of life on earth and is also a large part of the human body which is why it is so important. Aquaporins are water channels that transports water through a process called trafficking. Aquaporin 2 is one of these aquaporins and with a faulty trafficking or mutations it could lead to nephrogenic diabetes insipidus and severe dehydration. Ezrin is a protein in the body which FERM-domain has been seen to interact with proteins as well as AQP2. The study was conducted to see if AQP2 and ezrin had some interactions through MST analysis.
Two proteins were tested, the full-length ezrin and the FERM-domain which were stained with Alexa-488 dye. A 1:1 dilution series were made for the MST.The results concluded that AQP2 and FL as well as FERM has an interaction.The KD was determined by a model in a computer program where it was 48±22 μM for FL and 405±548 μM for FERM. However the confidence interval for FERM was larger than the actual value making it unreliable. The results for FL and FERM should be approximately the same because it is said that AQP2 reacts with the FERM-domain. A study, although, has stated that residues in the C-terminus of ezrin are critical for interaction. More MST-studies has to be conducted to get a conclusive result with a larger dilution series and more tests.}},
author = {{Aulin, Hanna}},
language = {{eng}},
note = {{Student Paper}},
title = {{The interaction between Ezrin & Aquaporin 2}},
year = {{2020}},
}