stress evaluated in trained elderly subjects in response to amaximal exercise stress test (MEST).

Sixteen elderly persons (aged 72.5 years), were randomlyassigned to two different groups: a training group (EMRT for 12weeks) and a control group. Plasma redox homeostasis (totalantioxidant status, (TAS) and glutathione (GSH)), oxidative damage(malondialdheyde (MDA) and protein carbonylation levels), andrepair system (Hsp70 and Hsp27 expression in leukocytes) wereevaluated before and after the maximal exercise stress test.

MEST lead to an increase of all the parameters related tooxidative stress. However, after the EMRT, the training groupshowed a less pronounced increase in oxidative stress parametersfollowing the maximal exercise stress test compared to controlgroup. A 25% reduction (po0.05) were found in GSSG levels andGSH/GSSG ratio was increased by 20% (po0.05) compared tocontrol group. MDA and protein carbonylation levels were 25 %reduced respect those found in control group. Hsp70 and Hsp27expression showed a lower protein basal levels in the trainedgroup, however, for both groups any significant induction of HSPswas not recognized within 24 hours after MEST.

Our data show that, in trained elderly subjects, the EMRTprotocol is able to induce a cellular adaptation allowing them torespond more effectively to an acute oxidative stress than theaged-matched sedentary subjects. Hence, the EMRT protocol maybe considered an effective workout that can improve the generaladaptive response to oxidative stress contributing to the overallhealth of the older people.

http://dx.doi.org/10.1016/j.freeradbiomed.2013.08.153

Heat Shock Protein 90 role in oxidized proteinaggregates

J.P. Castro a,b,c,n, T. Jung c, H. Almeida a,b, T. Grune c

a Departamento de Biologia Experimental, Faculdade de Medicina daUniversidade do Porto, Portugalb IBMC-Instituto Biologia Molecular e Celular, Porto, Portugalc Institute of Nutrition, Friedrich Schiller University Jena, Jena, Germany

Protein carbonylation, the most frequent type of proteinoxidation, which often results from oxidative stress conditions,leads to an irreversible non-enzymatic protein modification anddysfunction. Cells recycle these proteins and prevent their accu-mulation, using the proteasome. However, if protein oxidationformation rate exceeds proteasome capacity, oxidized proteinsform insoluble, undegradable, high molecular weight, proteinaggregates that may cause senescence or apoptosis.

We have recently shown oxidized protein aggregates formation ina T cell line model after several hours of oxidative stress leading toproteasome inhibition and proliferation arrest. However, the under-lying mechanism that follows these disturbances remains elusive.

We hypothesized that molecular chaperones as hsp90 andhsp70 would have a role in this process as they are known to beinvolved in cellular proteostasis by forwarding proteins to refold-ing or degradation depending on triage decision; in fact, theirprecise role on oxidized proteins (or oxidized aggregates) in thissetting is largely unexplored. Therefore to provide insights on thatmodel, we decided to investigate hsp90/70 involvement.

After exposing cells to oxidative stress for 24h, followed byrecovery up to 216h, preliminary results indicate a role of hsp90,but not hsp70, involvement. In fact, there was a co-localization ofhsp90 and protein aggregates shown by immunocytochemistry. In

addition, in Western blots against hsp90 (constitutive form around84 kDa), there was a positive band in the stacking zone suggestinghigh molecular weight aggregates binding. Interestingly, furtheranalysis revealed that it contained an unexpected hsp90 bandaround 73 kDa, suggesting an isoform with a specific role inprotein aggregates establishment.

This band may be an inducible form of hsp90, which will beclarify by mass spectrometry after purifying aggregates frominsoluble fractions, a work that is currently in progress. Also, wehope to verify its role in vivo as well, as we hypothesize that thismay also take place. Studies with organisms models should follow.

http://dx.doi.org/10.1016/j.freeradbiomed.2013.08.154

SESSION 12

How to Write a Great Research Paper, and Get itAccepted by a Good Journal

Anthony Newman

Life Sciences Department, Elsevier, Amsterdam, The Netherlands.E-mail address: a.newman@elsevier.com

Background: Knowing the best way of structuring your paperwhen writing it, and the most appropriate journal to send it to,really helps in getting your paper accepted. Also understandinghow editors and publishers think and what they expect, andknowing how the peer review process works, is invaluable insightinto the publishing process.

Results: After attending this workshop, one in the ElsevierPublishing Connect Workshop series, participants will have a clearidea of the steps needed to be taken before starting to write apaper. They will also be able to plan writing manuscripts using thelogical step sequence – not the sequence in which the paper willbe read. Authors are also made aware of what aspects of theirpapers Editors and Publishers look at critically, and to ensure thatin taking care of these areas, their papers are much more likely tobe accepted. Dealing with referees’ comments and the art of politerebuttal are also described such that these can be used to improvethe submitted paper suitably. Sensitive areas such as publishingethics, plagiarism, duplicate publishing, etc are also clearlyexplained such that participants have a clear understanding ofwhat is allowed, and what is not allowed.

Conclusions: These insights into the publishing and peer-review process will enable the participants to be more confidentas an author in the world of science publishing, and will help themget their papers published more easily, and help them to progresstheir career.

http://dx.doi.org/10.1016/j.freeradbiomed.2013.08.155

TRAINING SCHOOL 1

Combinatorial approaches and models in the study ofhuman ageing in vitro and in vivo: emphasis onCaenorhabditis elegans as a model organism

N. Chondrogianni

National Hellenic Research Foundation, Institute of Biology, MedicinalChemistry and Biotechnology, Athens, Greece

Abstract / Free Radical Biology and Medicine 65 (2013) S1–S22S20