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Role of antioxidant enzymes in cardioprotective regimens of cold acclimation
Špínová, Šárka ; Žurmanová, Jitka (advisor) ; Holzerová, Kristýna (referee)
The effect of cold on the organism depends on the degree of cold and its duration. Cold acclimation induces a thermoregulatory response, shivering thermogenesis and subsequently the development of non-shivering thermogenesis associated with the activation of brown adipose tissue. Exposure to mild cold in the form of hardening possesses beneficial effects on the whole organism and recently the cardioprotective effects of mild cold acclimation has been described. Increased antioxidant capacity has been demonstrated in the mechanism of cardioprotection induced by hypoxia. The aim of this thesis was to find out whether the protective effect of mild cold acclimatization (8 ± 1 řC) is associated with a change in the capacity of the antioxidant system. To achieve this goal, the protein levels of the main antioxidant enzymes (superoxide dismutase, catalase, glutathione peroxidase, thioredoxin, thioredoxin reductase, aconitase, heme oxygenase) were determined during acclimation to mild cold, specifically in 1-3-10 days and subsequently after 5 weeks, and after a 2-week recovery. The results showed changes in most of the antioxidant proteins, however the effect on cold-elicited cardioprotection must be further verified. Key words: heart, cold acclimation, superoxide dismutase, catalase, glutathione...
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Study of interaction between ASK1 kinase and thioredoxin.
Koláčková, Kateřina ; Obšil, Tomáš (advisor) ; Vaněk, Ondřej (referee)
MAP kinase signaling cascade plays an important role in the cellular response to various stress stimuli from the external environment. This signaling cascade is divided into three levels: MAP kinase kinase kinases (MAP3K) phosphorylate and thus activate MAP kinase kinases (MAP2K) and those subsequently phosphorylate and thus activate MAP kinase (MAPK) pathway, which regulates many cellular functions such as apoptosis, cell differentiation and morphogenesis. One of the important MAP3K is protein kinase ASK1 (Apoptosis signal-regulating kinase 1), which is an important regulator of cellular immune and stress responses. Given that the increased activity of ASK1 is related to the development of serious diseases such as cancer, cardiovascular and neurodegenerative diseases, ASK1 is an interesting target in the pharmacy in the development of new drugs. Human ASK1 consists of 1374 amino acids and is divided into three domains: a central Ser/Thr catalytic domain and two coiled-coil domains, of which the first is located at the N- and the second at the C-terminus of the molecule of this protein kinase. ASK1 is regulated by its binding partners, which include a small cellular redox protein thioredoxin (Trx-1), which binds to the N-terminal part of ASK1. Trx-1 is a potent antioxidant and so it protects cells...
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Diversity and functions of soluble electron transporting proteins
Alexová, Eliška ; Hrdý, Ivan (advisor) ; Mach, Jan (referee)
Electron transporting proteins serve to transfer electrons between various soluble and membrane bounded enzymes and proteins in biological processes as for example respiration, photosynthesis and different kinds of energy metabolism. Electron transporting proteins occur in every living organism. The active site of electron transporting proteins contains metal ions as iron and copper, thiol or flavin group. It uses this active site for electron transfer. The redox potential is connected with electron transfer because that is a relative tendency of molecule pairs and they are able to accept or donnate electrons. When the molecules have got more negative value of redox potential, then they have got better ability to donnate electrons. Ferredoxins with iron-sulfur cluster and cytochromes with heme group have got the lowest redox potential of electron transporting proteins. On the contrary cupredoxins with copper center have got the highest redox potential. Key words: cytochrome, flavodoxin, cupredoxin, ferredoxin, thioredoxin, glutaredoxin, rubredoxin
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Cellular localization and functional characterization of TTL proteins of Arabidopsis
Schier, Jakub ; Soukup, Aleš (advisor) ; Schwarzerová, Kateřina (referee)
This thesis focuses on the study of TTL protein family in the model species Arabidopsis thaliana. It sums up available published data on this so far poorly studied genes and presents newly gained experimental data. Main emphasis is given to TTLs cellular localization in possible relationship to their physiological function. Presented thesis comprises of in silico analysis of TTL proteins, but also the creation and microscopy analysis of TTL-mRuby2 and TTL-GFP fusion proteins in transient and permanent transformants. Powered by TCPDF (www.tcpdf.org)
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Study of interaction between ASK1 kinase and thioredoxin.
Koláčková, Kateřina ; Obšil, Tomáš (advisor) ; Vaněk, Ondřej (referee)
MAP kinase signaling cascade plays an important role in the cellular response to various stress stimuli from the external environment. This signaling cascade is divided into three levels: MAP kinase kinase kinases (MAP3K) phosphorylate and thus activate MAP kinase kinases (MAP2K) and those subsequently phosphorylate and thus activate MAP kinase (MAPK) pathway, which regulates many cellular functions such as apoptosis, cell differentiation and morphogenesis. One of the important MAP3K is protein kinase ASK1 (Apoptosis signal-regulating kinase 1), which is an important regulator of cellular immune and stress responses. Given that the increased activity of ASK1 is related to the development of serious diseases such as cancer, cardiovascular and neurodegenerative diseases, ASK1 is an interesting target in the pharmacy in the development of new drugs. Human ASK1 consists of 1374 amino acids and is divided into three domains: a central Ser/Thr catalytic domain and two coiled-coil domains, of which the first is located at the N- and the second at the C-terminus of the molecule of this protein kinase. ASK1 is regulated by its binding partners, which include a small cellular redox protein thioredoxin (Trx-1), which binds to the N-terminal part of ASK1. Trx-1 is a potent antioxidant and so it protects cells...
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Preparation of thioredoxin and thioredoxin-binding domain of protein kinase ASK1 for structural studies
Jarosilová, Kateřina ; Obšil, Tomáš (advisor) ; Kalábová, Dana (referee)
All living organisms are exposed to various forms of stress during their lifetime. This is probably the reason why an evolutionally well conserved the mitogen-activated protein kinase (MAPK) system of signaling cascades was formed to regulate cellular stress response. Those signaling pathways consist of three consecutive classes of protein kinases: MAP3K, MAP2K and MAPK. The signal is then transmitted from MAPK to another protein kinases and transcription factors. Apoptosis signal-regulating kinase 1 (ASK1) is a member of MAPK pathway, more specifically is classified as a member of the mitogen-activated protein kinase kinase kinase family (MAP3K). Human ASK1 consists of 1374 amino acids which are folded into several domains and sequence motives. The N-terminal coil-coiled domain (NCC), the serine/threonine kinase domain and the C-terminal coil-coiled domain (CCC) are three main domains. In addition, several regions responsible for the interaction between ASK1 and their binding partners have also been identified. The activity of ASK1 is regulated by various factors including thioredoxin and the 14-3-3 proteins, which function as inhibitors, and TNF receptor associated factors (TRAFs), which function as activators. The aim of this study was the preparation of six different expression constructs of...
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