Hamowanie wytwarzania adrenaliny -hal tu du dat???

spoko art bedzie lato bedziemy eksperymentowac...

nieodwracalne iMAO?

brzmi ciekawie

nie ma takich po***alo mu sie...

zbyt piękne zeby było prawdziwe

A na odwrót ? Jak podwyzszyc dosc znacznie adrenaline przed treningiem ?

Feta i efedryna powoduje wiekszy wyrzut noradrealiny niz adrealiny. Dluzsze stosownaie tego typu stymulantow powoduje zaburzenie stezenia noradrealiny w mozgu a to z koleji prowadzi do depresji i zahamowania psycho-ruchowego...

chcecie sobie poodpoczywac proponuje to co u mnie w szpitalu idze
najpierw Dormicum potem Norcuron ewentualnie Pavulon, dajeh Thiopental albo Brietal potem Sufentanyl i po zawodach

http://www.xasa.com/wiki/pl/wikipedia/i/in/inhibitory_monoaminooksydazy.html 

Monoamine oxidase (MAO) - Gerard J. Kleywegt

© 1997, G.J. Kleywegt

Amine oxidases are ubiquitous enzymes, found in both micro-organisms and higher organisms. Among the various types of amine oxidase, the mitochondrial flavoenzyme monoamine oxidase (MAO) is of special interest for neuropsychiatry. MAO is involved in the biodegradation of aromatic monoamines, including classical neurotransmitters such as serotonin, adrenalin, histamine, and dopamine, and appears to play a central role in several psychiatric and neurological disorders. In addition to its role in neurotransmitter metabolism, there is evidence that MAO has an important function as a scavenger of various other amines (e.g. , tyramine, octopamine, tryptamine). Further, MAO is able to oxidise a wide variety of primary, secondary, and tertiary amines of different chemical structures.

Irreversible and unspecific inhibitors of monoamine oxidase were the first modern anti-depressants, but due to their adverse side effects they have fallen into disuse. In recent years, the interest in reversible and irreversible MAO inhibitors (MAOIs) has been revived, in particular since the finding that the enzyme occurs in two forms, MAO-A and MAO-B. These two proteins are highly homologous (~70% sequence identity), but are encoded by separate genes on the X chromosome. The two forms differ in their substrate specificity, as well as their tissue and cell distribution in the central nervous system and peripheral organs, indicating that they may have distinct physiological functions.

Several reversible and irreversible inhibitors with relative selectivity for one of the MAO forms have been developed. They belong to various chemical classes with different modes of enzyme inhibition (e.g. , covalent mechanism-based interaction, pseudo-substrate inhibition, and non-covalent interaction). A major advantage of the new generation of MAOIs lies in their relatively mild side effects. However, despite the considerable progress in understanding the interactions of the two enzyme forms with their preferred substrates and inhibitors, no general rules are yet available for the rational design of potent and selective inhibitors of MAO-A and MAO-B.

The therapeutic effects of MAOIs fall into two categories. MAO-A inhibitors have been used mostly in the treatment of mental disorders, in particular depression. The only MAO-B inhibitor which has been extensively tested in human disorders is L-deprenyl. This drug, in particular in combination with L-dopa, leads to a moderate improvement in the management of some of the symptoms of Parkinson's disease, especially in its early stages. This drug also has a weak effect in the treatment of depression, and some beneficial action has been reported in patients with mild Alzheimer-type dementia, narcolepsy, attention-deficit disorders, and Lafora-type epilepsy.

The goal of this project is the determination of the three-dimensional, atomic structure of monoamine oxidase by means of X-ray crystallographic methods. Knowledge of this structure will facilitate the design of new, potent, and selective MAO inhibitors, which may eventually lead to new and effective drugs for the treatment of depression and possibly of other disorders. The implications of a successful structure determination of either or both MAO forms are evident. The crystal structure will reveal the overall fold of MAO (and possible relationships with other proteins), and the architecture of the active site and the substrate-binding site. Knowledge of the three-dimensional structure (and, ideally, a comparison of the structures of MAO-A and B) will facilitate the design of potent and selective MAO inhibitors, with potential applications in the treatment of clinical depression and Parkinson's disease. Further, there is a large body of biochemical and other data that awaits interpretation in the light of, and correlation with the high-resolution structure of MAO-A and/or MAO-B. Possible crystallographic follow-up studies are also obvious, namely the study of complexes of wild-type and mutant enzymes with substrate analogues, and with reversible and irreversible inhibitors.

The hard work in the crystallography lab is carried out by Dr Kristina Bäckbro (post-doc) and Emma Jakobsson (PhD student).

The project is a collaboration with:

Prof. Creed W. Abell and his associates (University of Texas at Austin) (WWW)
Prof. Jean C. Shih and her associates (University of Southern California) (WWW)

(Emma and Jean Shih's group in LA)

Kazam - wypada zrobic minimalny chociaz research zanim sie zasugeruje, ze komus sie poj ebalo.

kazam jesli chcesz byc wiotki jak szmata to polecam neuroleptyki nowej generacji najlepszy będzie risperidon (rispolept) bo ma najmniej efektów ubocznych
no chyba że chcesz nabrac DUUUUŻO MASY oczywiście nie mięsnieowej wtedy polecam olanzapinę (zyprexa)