Immunoterapiaren helburua da gaixoen immunitate-sistema indartuz minbizia bezalako gaitz larriak menderatzea. Horretarako, gaixoak maiz 2-interleukina (IL-2) deitzen den konposatu batekin tratatzen dira, izan ere molekula honek berebi-ziko ahalmena baitauka T-zelulen edo T linfozitoen hazkuntza sustatzeko. Zoritxarrez, IL-2ren erabilerak albo kalte desatseginak eragiten ditu gaixoetan, eta hauek ekiditeko ezinbestekoa da IL-2k T-zeluletan eragiten dituen molekula mailako aldaketak sakon aztertu eta ulertzea. Zelulen gainazalera heltzen diren seinaleak zelulan barrena ga-rraiatzen dira nagusiki proteinen behin behineko fosforilazioen bidez. Hori horrela, au-rreko lan batean, IL-2k T linfozitoetan pizten dituen seinalizazio-bidezidorrak aztertu genituen zelulen zitoplasman fosforilatzen diren proteinak masa espektrometriaren bi-dez identifikatuz. Oraingo lan honetan berriz, masa espektrometriaren laguntzaz aztertu da IL-2k nola erregulatzen duen T-zelulen nukleoko proteinen fosforilazio maila, izan ere horrek zuzenean eragingo baitu geneen erregulazioan eta horrenbestez baita zelu-laren patuan ere. Esperimentu bera 3 aldiz errepikatu ostean, gutxienez behin identifi-katu eta kuantifikatu dira lan honetan T-zelulen nukleoko proteinetan fosforilatutako 8.521 aminoazido, horietako haietako asko aurrez ezagutugabeak. Bestalde, ikusi da orkorrean berdinantzera mantentzen dela IL-2rekin tratatutako eta tratatu gabeko T-ze-luletako fosforilazio maila. Halere, azpimarragarria da IL-2ren ondorioz 391 aminoa-zidoren fosforilazio maila nabarmen aldatzen dela T-zelulen nukleoetan. Etorkizunean egingo diren ikerkuntzek argituko dute zein den IL-2ren menpeko fosforilazio hauen esanahi biologikoa.
Immunotherapy aims to fight against diseases such as cancer by boosting the immune system of the patients. For that purpose, patients are usually treated with a molecule called interleukin-2 (IL-2), which plays a pivotal role in modulating the im-mune system and specially in promoting the proliferation of T-cells. Unfortunately, ad-ministration of IL-2 is usually accompanied by severe side effects that must be over-come. To achieve this, it is mandatory to understand in detail the molecular effects triggered in T-cells upon IL-2 stimulation. It is known that signaling events initiated at the cell surface are mainly transduced inside the cell through transient phosphoryla-tions occurring in distinct proteins. For that reason our previous study focused on dis-secting the signaling pathways triggered in IL-2-treated T lymphocytes by studying the proteins that become tyrosine phosphorylation upon the stimuli using mass spectrome-try. In the present study, we aimed to unveil how IL-2 modulates the phosphorylation status of the nuclear proteins in T-cells, which ultimately will affect gene expression and the fate of the cell. Following a quantitative mass spectrometry-based approach a total of 8,521 phosphorylated aminoacids were quantified at least in one of the 3 repli-cas of the same experiment that were performed. Whereas the phosphorylation levels of most phosphosites remained unaffected in IL-2-treated and untreated T-cells, the phosphorylation status of 391 phosphosites was found to be dramatically modulated upon IL-2 stimulation. Further investigation will unveil the biological significance of such findings
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