Abstract

PKD is a founding member of CAMK group of kinases and there is ample evidence of its participation in important cellular process including stress. Due to the lack of specific inhibitors for its action in vivo, its protein targets are scarcely described. Even less is known about its role at regulating the transcription of target proteins. The miRNA are important regulators of protein expression and several groups are currently undertaking studies about its targets, enriching a database that will enable a better understanding of the networks in which they participate.In this work we aimed to identify miRNA that are modulated by hyperosmotic stress in 3T3 expressing PKD‐1 cells as a means to understand the PKD participation in this cellular process.We obtained the RNA from 3T3‐PKD‐1 cells and their control counterparts, without or with an hour challenge with 0.3M NaCl, and sought to identify the up‐ or down‐ regulated miRNA. This was performed using miRNA3.0 Affymetrix microchips, and analyzed with software provided.We found that miRNA that are exclusively regulated by the PKD action after the 0.3M NaCl challenge are: mir‐103, mir135, which are down‐regulated, and mir27a, which is up‐regulated.Some of the targets of the down regulated mir‐103 include Syntaxin‐17, which participates in the autophagosomes formation; inhibitory growth factor 5 which participates in proliferation; and cadherin‐11, which participates in shaping cell morphology. The mir‐135 has as targets complexin 1 that participates in vesicle transport. The up‐regulated mir‐27a has as targets the A2B adenosine receptors that help repair ischemia/reperfusion injury, the activin A receptor ‐type C and the Ubiquitin conjugating enzyme E2N and Polo‐like kinase that regulates the differentiation of various organs.Grant Funding Source: IN222014

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.