Viroj Wiwanitkit
Wiwanitkit House, Bangkhae, Bangkok, Thailand.
DOI: 10.4103/0976-9668.92321

ABSTRACT

Background: Basically, (pro)renin acts via a specifi c receptor, (pro)renin receptor (PRR) binding between renin and prorenin, its inactive proenzyme form. The study on the molecular level of PRR can give useful knowledge to help understand many renal disorders. Method: Here, the author focuses on the stability of the PRR molecule. The mutation prone positions within the PRR molecule was assessed using standard reference technique. Result: The study showed there is no identifi ed mutation prone position within the PRR molecule. Conclusion: This imply the high stability of PRR. This means that PRR rarely undergoes mutation. The reported mutation in PRR should be a very rare episode and the study on the specifi c cause is warranted.

Keywords: (pro)renin receptor, mutation.

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