FIND ARTICLE

Focal Adhesion Kinase osteoblast biology

Focal Adhesion Kinase - FAK ( focal adhesion kinase) belongs to the group of non-receptor protein tyrosine kinases . It occurs in the cytoplasm of most cells , including osteoblasts. At the time of its activation , the interaction of integrin associated protein extracellular matrix call is incorporated into platelet adhesion . FAK kinase in the presence of these structures is closely related to a function that plays in cellular processes such as adhesion, migration, proliferation . FAK -deficient cells show a much slower growth and reduced mobility.

Protein P53 - the guardian of the genome in viral infection

P53 is a multifunctional protein with a molecular weight of 53 kDa that is activated in response to a variety of cellular stresses . It contributes to the cell cycle arrest in the G1 phase and to induce apoptosis is involved in the regulation of gene transcription in the process of cell differentiation and angiogenesis , and its best-known function, repair of DNA damage . Necessary in situations of cellular stress , which might jeopardize the integrity of the genome , known as the " guardian of the genome " .

Aclarubicin - an alternative to anthracycline-resistant cells and generation

Aclarubicin is one of the derivatives of anthracycline drugs exhibiting less side effects in comparison with the commonly used anthracyclines Generation - doxorubicin and daunorubicin. This article presents the current knowledge of the molecular mechanisms of the cytotoxic effect of the ACL, such as the effect on the activity of topoisomerase I and II, the processes of replication and transcription. Also discussed was the impact of the ACL with the cell membrane, drug transport through the membrane and the plasma membrane involved in the acquisition of multidrug resistance.

Enigmatic three-peptydylpeptydaza second - protease for special tasks

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 .

Human papillomavirus and the process of apoptosis

The importance of the effect of infection with human papilloma virus (HPV) , and the processes of carcinogenesis, apoptosis has been the subject of many studies , but is still little understood. The study aims to present the current knowledge of the impact of HPV infection on selected aspects of the processes of life and death of cells. Apoptosis is a complex process which leads to cell death , wherein the protein plays an important role of BCL - 2 family , as well as the cell cycle regulatory proteins include P53 and pRB .

Suppression of apoptosis in virus infections chordopoks

Viruses , including poxvirus , are known to possess efficient mechanisms allowing them to escape from the immune system of the infected host. One such mechanism is the possibility of inducing or suppressive effects of viruses on programmed cell death ( apoptosis ) . In this paper, the characteristics of the different ways of suppression of apoptosis by gene products of some chordopokswirusów ( orthopoxvirus , Leporipoxvirus and molluscipokswirusów ) . For proteins that are involved in the suppression of apoptosis by caspase inhibitors include poxvirus ?

The role of zinc in the modulation of apoptosis

The article presents the current state of knowledge of zinc as a modulator of apoptosis. This important trace element in the form of a bivalent cation has the ability to both the inhibitor and inducer of apoptosis. Contribution of Zn2 + ions in the regulation of programmed cell death is still not fully understood. It is suggested that Zn2 + ions can interact with multiple sites in the cell signaling cascade during apoptosis. Supplementation with zinc acts as an inhibitor of apoptosis, while its removal or low level induces programmed death in many cells.

Programmed cell death (PCD) in the development of higher plants

The term " programmed cell death " or " programmed cell death " (PCD , programmed cell death called ) is determined genetically controlled process of cell death eukaryotic organisms , induced by endogenous or exogenous factors and implemented through the launch of the same cell molecular mechanisms leading to her death . PCD is a broader concept than apoptosis - the death of an animal cell with a distinctive morphotype and internukleosomalnym cutting nDNA , the main determinant biochemical execution phase .

Programmed cell death (PCD) in the development of higher plants

The term " programmed cell death " or " programmed cell death " (PCD , programmed cell death called ) is determined genetically controlled process of cell death eukaryotic organisms , induced by endogenous or exogenous factors and implemented through the launch of the same cell molecular mechanisms leading to her death . PCD is a broader concept than apoptosis - the death of an animal cell with a distinctive morphotype and internukleosomalnym cutting nDNA , the main determinant biochemical execution phase .

Heat shock proteins - molecular perpetual motion

Heat shock proteins [ called Heat shock proteins , HSP ] are proteins having the amino acid sequence of the most conservative in the biosphere . Play an important role in all prokaryotic and eukaryotic cells , protecting them from the harmful consequences of metabolic and environmental factors. Act as agents for the care of other proteins involved in folding of the polypeptide chains and de-interleaving , oligomerisation , translocation and degradation .

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The Editorial Board
Andrzej Łukaszyk - przewodniczący, Zofia Bielańska-Osuchowska, Szczepan Biliński, Mieczysław Chorąży, Aleksander Koj, Włodzimierz Korochoda, Leszek Kuźnicki, Aleksandra Stojałowska, Lech Wojtczak

Editorial address:
Katedra i Zakład Histologii i Embriologii Uniwersytetu Medycznego w Poznaniu, ul. Święcickiego 6, 60-781 Poznań, tel. +48 61 8546453, fax. +48 61 8546440, email: mnowicki@ump.edu.pl

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