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Tri- II is a great peptydylpeptydaza cytoplasmic protease complex structure that cuts off the free end of the tripeptides of amino oligopeptides also has some activity endoproteolytic . TPPII cells present in all eukaryotes examined . Its structure is faithfully preserved by evolution . Proteasome participates with other peptidases and cytoplasmic protein degradation processes , but the specific substrates and the method of controlling TPPII activity have not yet fully understood . Both overexpression TPPII is detrimental to cells and the inhibition of gene transcription TPPII . In the first case there is a disturbance in the control of cell cycle , which promotes the neoplastic transformation , in the second case the cells divide more slowly , and have defects kariokinezy . TPPII plays in different tissues specific functions by participating in the process of lipogenesis , cachexia , nerve transmission , antigen presentation , and oncogenesis .
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Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

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