6533b870fe1ef96bd12cf16a

RESEARCH PRODUCT

Reversible stress-induced lipid body formation in fast twitch rat myofibers

Mika KaakinenKalervo MetsikköP. RahkilaMika T. Nevalainen

subject

Caveolin 3Blotting WesternGolgi ApparatusBiologyEndoplasmic ReticulumSemliki Forest virusRats Sprague-Dawleychemistry.chemical_compoundSarcolemmaBacterial ProteinsAnimalsCells CulturedSarcolemmaLipogenesisEndoplasmic reticulumCell BiologyTunicamycinBrefeldin AEndoplasmic Reticulum StressLipid Metabolismmusculoskeletal systembiology.organism_classificationFusion proteinRatsCell biologyCaveolin 3Luminescent ProteinsProtein TransportSarcoplasmic ReticulumCholesterolBiochemistrychemistryMuscle Fibers Fast-TwitchVirusesUnfolded protein responseFemale

description

We analyzed the existence of lipid bodies (LBs) in the fast twitch rat flexor digitorum brevis (FDB) myofibers and found that these structures were scarce. However, isolation procedure of the myofibers, heath shock, viral infection or the glycosylation inhibitor tunicamycin induced formation of the LBs, which were stationary structures flanking Z lines. We next infected FDB myofibers with recombinant Semliki Forest virus expressing caveolin 3-yellow fluorescent protein (cav3-YFP) since this chimeric protein was targeted to the LBs facilitating their further analysis. Photobleaching experiments showed that the LBs recovered cav 3-YFP extremely slowly, indicating that they were not continuous with the endoplasmic/sarcoplasmic reticulum. We found, however, that cav3-YFP could move from the LBs to the sarcolemma and this phenomenon was sensitive to Brefeldin A, suggesting that the chimeric protein could be returned from the LBs to the endoplasmic reticulum.

yearjournalcountryeditionlanguage
2012-10-01Experimental Cell Research
https://doi.org/10.1016/j.yexcr.2012.06.019