Rabbit Muscle Actin Polymerization changes by Ultraviolet –B radiation

Anita Mukherjee,Arun Kumar Attri

doi:10.1038/npre.2009.2766.1

Anita Mukherjee, Arun Kumar Attri

Open Access

https://doi.org/10.1038/npre.2009.2766.1

Copy DOI

Abstract

AbstractIncrease in Ultraviolet-B flux from the Sun has the potential to alter the protein in mammals. Rabbit muscle was processed and filtered to extract G-actin, which was tested for its protein concentration before exposing to UV-B. It was found that polymerization of actin does get affected exposure of actin monomers to UV-B radiation. Inside the cell, there are many actin binding proteins which might be playing crucial role in G-actin to F-actin formation.

Highlights

Actin is an essential and highly conserved protein for the survival of both plant and animal cells
The most intensely studied function of actin filament is their role in providing the mechanochemical basis for contractions[1].Besides polymerized actin plays central role in mobile activities of all eukaryotic cells
In non muscle cells extensive depolymerization and repolymerization of cytoskeleton are likely to be continuous as well as regulated process where actin filaments disappear and reappear at different times and places as they are needed for specific functions

Summary

Introduction

Actin is an essential and highly conserved protein for the survival of both plant and animal cells. The filtered residue was extracted with 4 liters of 1mM EDTA at pH 7.0 by stirring for 10 minutes at 4 ̊ C. Further extraction was done with 8 liters of doubled distilled water for 5 minutes with stirring at 4 ̊ C. The polymerized actin was transferred in Beckman tubes and centrifuged at 40,000 rpm for 3 hours at 4 ̊ C.

Results

Conclusion