|
|
Interplay between adenosine signaling and the circadian system
Škrle, Jan ; Bendová, Zdeňka (advisor) ; Houdek, Pavel (referee)
Sleep is regulated primarily by the two processes, by Process C and S. Process C represents circadian regulation by circadian system; Process S represents the homeostatic sleep drive. Circadian system controls the timing of many physiological functions including body temperature rhythms, locomotor activity rhythms, periodically changing hormones levels etc. Process C contributes to sleep regulation mainly by setting lower and upper thresholds for a sleep pressure. When the sleep pressure reaches one of these thresholds, falling asleep or waking is promoted. However, the sleep architecture is altered by a phase of endogenous oscillators as well. The homeostatic sleep drive is based on a sleep- wake history with the sleep pressure rising during a wakefulness and lowering during sleep. This mechanism is responsible for a modification in structure of a recovery sleep following a sleep deprivation. Due to the effects of adenosine on sleep regulation, adenosine signalling is considered to play a critical role in the homeostatic sleep drive. These two processes were thought to be independent of each other, but new data show that there is a reciprocal regulation between them. The aim of this work was to conclude, where these two processes meet, with a special attention on processes, where the adenosine...
|
|
|
The influence of intravenously administeres lactoferrin in early phase of coronnary thrombosis - histopathological analysis
Škrle, Jan ; Semecký, Vladimír (advisor) ; Mladěnka, Přemysl (referee)
Lactoferin (La) is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino acid sequence level and also the three dimensional conformation level with transferin. Afinity of Lf to iron is about 260times higher than that of transferin. Lf is present physiologically in exocrine secretions, eg.: tears, saliva, milk, sinovial fluid, seminal fluid and in the secondary granules of neutophils. The precise function of Lf in organism is considered to be very complex and is still a hot subject of scientific disputation. Lf was documented to act as antimicrobial, antiinflamatory and antitumoral agent. These effects are probably based on its iron chelating properties. Similarly La inhibits hydroxyl radical formation via Fenton reaction due to chelation of free iron. The catecholamine model of myocardial injury, represented by administration of synthetic catecholamine isoprenaline (ISO), posseses many pathophysiological similarities with acute myocardial infarction (AMI). The only possibility for myocardial tissue recovery in AMI represents the reperfusion of ischaemic myocardium. But this process is associated with tissue derangement due to burst of hydroxyl radical catalyzed by free iron (Fenton reaction). Therefore La has been proposed to have potentially positive effects in a catecholamine...
|
|
|
Effect of lactoferrin on macroscopical and histological features in different tissues in rats. II. Liver and kidneys.
Škrle, Jan ; Semecký, Vladimír (advisor) ; Mladěnka, Přemysl (referee)
Lactoferin is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino acid sequence level and also the three dimensional conformation level with transferin. Both proteins are classified in the family of iron-binding glykoproteins, named transferin family. Afinity of Lf to iron is about 260times higher than that of transferin. (1) Lf is present physiologically in exocrine secretions, eg. tears, saliva, milk, sinovial fluid, seminal fluid and in the secondary granules of neutophils. (6) The precise function of Lf in organism is considered to be very complex and is still a hot subject of scientific disputation. Lf was documented to act as antimicrobial, antiinflamatory and antitumoral agent. (15,17) Another of its properties is ability to inhibit hydroxyl radical formation via Fenton reaction. (20) Because of good technological properties and it's physiological occurence Lf can be used as a therapeutical agent.(6) In our experiment we studied the influence of Lf on macroscopical and histological features in liver and kidney of the sewer-rat. We used two-dose model of i.v. Lf ( 50mg/kg in one dose and 3x 20 mg/kg in three days). The tissues of both models were used for histopatological analysis. We observed significant patological changes in kidney and liver after i.v....
|
|
|
Effect of lactoferrin on macroscopical and histological features in different tissues in rats. II. Liver and kidneys.
Škrle, Jan ; Semecký, Vladimír (advisor) ; Mladěnka, Přemysl (referee)
Lactoferin is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino acid sequence level and also the three dimensional conformation level with transferin. Both proteins are classified in the family of iron-binding glykoproteins, named transferin family. Afinity of Lf to iron is about 260times higher than that of transferin. (1) Lf is present physiologically in exocrine secretions, eg. tears, saliva, milk, sinovial fluid, seminal fluid and in the secondary granules of neutophils. (6) The precise function of Lf in organism is considered to be very complex and is still a hot subject of scientific disputation. Lf was documented to act as antimicrobial, antiinflamatory and antitumoral agent. (15,17) Another of its properties is ability to inhibit hydroxyl radical formation via Fenton reaction. (20) Because of good technological properties and it's physiological occurence Lf can be used as a therapeutical agent.(6) In our experiment we studied the influence of Lf on macroscopical and histological features in liver and kidney of the sewer-rat. We used two-dose model of i.v. Lf ( 50mg/kg in one dose and 3x 20 mg/kg in three days). The tissues of both models were used for histopatological analysis. We observed significant patological changes in kidney and liver after i.v....
|
|
|
The influence of intravenously administeres lactoferrin in early phase of coronnary thrombosis - histopathological analysis
Škrle, Jan ; Semecký, Vladimír (advisor) ; Mladěnka, Přemysl (referee)
Lactoferin (La) is an 80-kDa iron-binding glykoprotein. It shares a high degree of homology at amino acid sequence level and also the three dimensional conformation level with transferin. Afinity of Lf to iron is about 260times higher than that of transferin. Lf is present physiologically in exocrine secretions, eg.: tears, saliva, milk, sinovial fluid, seminal fluid and in the secondary granules of neutophils. The precise function of Lf in organism is considered to be very complex and is still a hot subject of scientific disputation. Lf was documented to act as antimicrobial, antiinflamatory and antitumoral agent. These effects are probably based on its iron chelating properties. Similarly La inhibits hydroxyl radical formation via Fenton reaction due to chelation of free iron. The catecholamine model of myocardial injury, represented by administration of synthetic catecholamine isoprenaline (ISO), posseses many pathophysiological similarities with acute myocardial infarction (AMI). The only possibility for myocardial tissue recovery in AMI represents the reperfusion of ischaemic myocardium. But this process is associated with tissue derangement due to burst of hydroxyl radical catalyzed by free iron (Fenton reaction). Therefore La has been proposed to have potentially positive effects in a catecholamine...
|
guest ::
