Jezuitská lékárna v Telči vznikla pro potřeby zdejší koleje po roce 1657 a vytrvala i po zrušení Tovaryšstva Ježíšova v roce 1773, kdy ji poslední lékárník Ignác Lyro odkoupil a přemístil z klášterních prostor do jednoho z domů na náměstí. U příležitosti soupisu majetku a následného prodeje vznikl podrobný inventář veškerého lékárenského vybavení od skříní, přes laboratorní pomůcky až po jednotlivé suroviny a léky. Soupis je rozdělen na část simplicií a hotových léčiv, poslední strany zaznamenávají pomůcky a nádoby užívané k zpracování, výrobě léků a jejich uchovávání. Léčiva zahrnují různé části rostlin, minerály, drahokamy či části živočichů. Seznam je veden vesměs abecedně, někdy s vyčleněnými skupinami podle typu. Každá z položek je opatřena údajem o množství a ceně. Mnoho surovin přitom pochází ze zámoří, oblastí, kam zdejší jezuité odcházeli jako misionáři. Z původního bohatého zařízení se dochovaly pouze tři lékárenské skříně a několik nádob, především dýhových krabic a keramických stojatek. Dochované části lékárny spolu s inventářem dávají poměrně dobrou představu o vybavení i vybavenosti telčské jezuitské apatyky prodávající zboží z různých částí světa. Jezuitský konvent tak vykresluje jako důležité centrum pro obyvatele města nejen v polovině 18. století, jehož tradice zůstává ve zdejší lékárně dodnes.

The Jesuit pharmacy in Telč was founded after 1657 within the premises of the Jesuit cloister; it survived the dissolution of Jesuits in 1773 and thanks to its purchase by the last pharmacist Ignac Lyro it was relocated to one of the houses in the square. During the stocktaking of the property and its sale, a detailed inventory of pharmacy equipment was recorded, including cabinets, laboratory tools, ingredients or drugs. The inventory is divided into parts of ingredients and prepared medications, the last lists recording the tools and containers for its preparation, production and preservation. The ingredients contain various parts of plants, minerals, precious stones or even parts of animals. The list is written mainly in the alphabetical order, in some cases with specified types of groups. Every item is provided with information about its price and quantity. Many ingredients originated from overseas countries, the areas of Jesuit missionary activities. Of the former rich equipment, only three pharmacy cabinets and a few containers, mainly veneer boxes and ceramic drug jars, have survived. All these parts together with the inventory give us a comparatively clear notion about the equipment and even facilities of the Jesuit apothecary in Telč, which sold items from different parts of the world. The Jesuit convent seems to be an important centre for town inhabitants not only in the 18th century; its legacy has remained in the local pharmacy till today.

• Klíčová slova
• klášterní lékárny,
• MeSH
• dějiny 18. století MeSH
• dějiny lékárnictví MeSH
• farmaceutické pomocné látky dějiny   MeSH
• farmacie MeSH
• léčivé přípravky dějiny   MeSH
• léčivé rostliny MeSH
• lékárny * dějiny   organizace a řízení   MeSH
• náboženství MeSH
• zdravotnické prostředky MeSH
• Check Tag
• dějiny 18. století MeSH
• Publikační typ
• historické články MeSH
• práce podpořená grantem MeSH

Cryptosporidium parvum contains a unique fusion protein pyruvate:NADP+ oxidoreductase (CpPNO) that is composed of two distinct, conserved domains, an N-terminal pyruvate:ferredoxin oxidoreductase (PFO) and a C-terminal cytochrome P450 reductase (CPR). Unlike a similar fusion protein that localizes to the mitochondrion of the photosynthetic protist Euglena gracilis, CpPNO lacks an N-terminal mitochondrial targeting sequence. Using two distinct polyclonal antibodies raised against CpPFO and one polyclonal antibody against CpCPR, Western blot analysis has shown that sporozoites of C. parvum express the entire CpPNO fusion protein. Furthermore, confocal immunofluorescence and transmission electron microscopy confirm that CpPNO is localized within the cytosol rather than the relict mitochondrion of C. parvum. The distribution of this protein is not, however, strictly confined to the cytosol. CpPNO also appears to localize posteriorly within the crystalloid body.

• MeSH
• Cryptosporidium parvum cytologie   enzymologie   genetika   MeSH
• cytosol enzymologie   MeSH
• Euglena gracilis cytologie   enzymologie   MeSH
• financování organizované MeSH
• fluorescenční mikroskopie MeSH
• ketonoxidoreduktasy analýza   genetika   imunologie   MeSH
• konfokální mikroskopie MeSH
• NADPH-cytochrom c-reduktasa analýza   genetika   imunologie   MeSH
• organely enzymologie   MeSH
• protozoální proteiny analýza   MeSH
• pyruvátsynthasa analýza   genetika   imunologie   MeSH
• sporozoiti cytologie   enzymologie   MeSH
• transmisní elektronová mikroskopie MeSH
• zvířata MeSH
• Check Tag
• zvířata MeSH

Spermadhesins are proteins containing a characteristic CUB domain, originally isolated from seminal plasma and ejaculated spermatozoa in domestic animals. Boar spermadhesins are multifunctional proteins exhibiting ligand-binding abilities with various endogenous ligands present in the male and female reproductive tracts and may play a role in the reproduction process. Porcine spermadhesins (AQN, AWN, PSP protein families) are secreted mainly by the seminal vesicles, but their mRNAs have been found also in the cauda epididymis and prostate. Unlike AQN and AWN spermadhesins, localization of porcine seminal plasma (PSP) proteins in the boar reproductive tract has not been completely resolved. This work has focused on PSP protein expression and localization in the boar reproductive organs and on spermatozoa. Using specific rabbit polyclonal antibodies (anti-PSP I and anti-PSP II), PSP I and PSP II proteins were immunodetected in tissue extracts and in secretory tissues of cauda epididymis, prostate, seminal vesicles and Cowper's glands on the blots and by an indirect immunofluorescence technique, respectively. Moreover, the ability of PSP proteins to bind to epididymal spermatozoa indicated their presence on cauda epididymal and ejaculated spermatozoa. Porcine seminal plasma proteins bind to the sperm surface at ejaculation and may modulate several aspects of sperm activity during reproduction. PSP proteins are produced not only by seminal vesicles and prostate, but also by epididymis. However, their prospective role in sperm epididymal maturation is not clear. Further characterization of seminal plasma protein forms expressed in the individual reproductive organs will help to understand their subsequent role in the reproduction process.

• MeSH
• financování organizované MeSH
• mužské pohlavní orgány cytologie   metabolismus   MeSH
• prasata MeSH
• proteiny semenné plazmy biosyntéza   MeSH
• regulace genové exprese fyziologie   MeSH
• rozmnožování fyziologie   MeSH
• sperma metabolismus   MeSH
• spermie cytologie   metabolismus   MeSH
• zvířata MeSH
• Check Tag
• mužské pohlaví MeSH
• ženské pohlaví MeSH
• zvířata MeSH

Trypanosoma brucei has a complex life cycle during which its single mitochondrion is subjected to major metabolic and morphological changes. While the procyclic stage (PS) of the insect vector contains a large and reticulated mitochondrion, its counterpart in the bloodstream stage (BS) parasitizing mammals is highly reduced and seems to be devoid of most functions. We show here that key Fe-S cluster assembly proteins are still present and active in this organelle and that produced clusters are incorporated into overexpressed enzymes. Importantly, the cysteine desulfurase Nfs, equipped with the nuclear localization signal, was detected in the nucleolus of both T. brucei life stages. The scaffold protein Isu, an interacting partner of Nfs, was also found to have a dual localization in the mitochondrion and the nucleolus, while frataxin and both ferredoxins are confined to the mitochondrion. Moreover, upon depletion of Isu, cytosolic tRNA thiolation dropped in the PS but not BS parasites.

• MeSH
• aktivní transport - buněčné jádro MeSH
• buněčné jádro metabolismus   MeSH
• ferredoxiny metabolismus   MeSH
• jaderné lokalizační signály MeSH
• lyasy štěpící vazby C-S chemie   genetika   metabolismus   MeSH
• mitochondriální proteiny metabolismus   MeSH
• mitochondrie metabolismus   MeSH
• molekulární sekvence - údaje MeSH
• multimerizace proteinu MeSH
• proteiny asociované s jadernou matrix chemie   genetika   metabolismus   MeSH
• proteiny vázající železo metabolismus   MeSH
• protozoální proteiny chemie   genetika   metabolismus   MeSH
• sekvence aminokyselin MeSH
• Trypanosoma brucei brucei enzymologie   genetika   metabolismus   MeSH
• vazba proteinů MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH

Caspase-2 is an apical protease responsible for the proteolysis of cellular substrates directly involved in mediating apoptotic signaling cascades. Caspase-2 activation is inhibited by phosphorylation followed by binding to the scaffolding protein 14-3-3, which recognizes two phosphoserines located in the linker between the caspase recruitment domain and the p19 domains of the caspase-2 zymogen. However, the structural details of this interaction and the exact role of 14-3-3 in the regulation of caspase-2 activation remain unclear. Moreover, the caspase-2 region with both 14-3-3-binding motifs also contains the nuclear localization sequence (NLS), thus suggesting that 14-3-3 binding may regulate the subcellular localization of caspase-2. Here, we report a structural analysis of the 14-3-3ζ:caspase-2 complex using a combined approach based on small angle X-ray scattering, NMR, chemical cross-linking, and fluorescence spectroscopy. The structural model proposed in this study suggests that phosphorylated caspase-2 and 14-3-3ζ form a compact and rigid complex in which the p19 and the p12 domains of caspase-2 are positioned within the central channel of the 14-3-3 dimer and stabilized through interactions with the C-terminal helices of both 14-3-3ζ protomers. In this conformation, the surface of the p12 domain, which is involved in caspase-2 activation by dimerization, is sterically occluded by the 14-3-3 dimer, thereby likely preventing caspase-2 activation. In addition, 14-3-3 protein binding to caspase-2 masks its NLS. Therefore, our results suggest that 14-3-3 protein binding to caspase-2 may play a key role in regulating caspase-2 activation. DATABASE: The atomic coordinates and structure factors have been deposited in the Protein Data Bank, www.ww pdb.org (PDB ID codes 6GKF and 6GKG).

• MeSH
• cysteinové endopeptidasy chemie   metabolismus   MeSH
• fosforylace MeSH
• jaderné lokalizační signály * MeSH
• kaspasa 2 chemie   metabolismus   MeSH
• konformace proteinů MeSH
• lidé MeSH
• maloúhlový rozptyl MeSH
• molekulární modely MeSH
• proteiny 14-3-3 chemie   metabolismus   MeSH
• vazba proteinů MeSH
• vazebná místa MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH

NMDA receptors (NMDARs) are ionotropic glutamate receptors that play a key role in excitatory neurotransmission. The number and subtype of surface NMDARs are regulated at several levels, including their externalization, internalization, and lateral diffusion between the synaptic and extrasynaptic regions. Here, we used novel anti-GFP (green fluorescent protein) nanobodies conjugated to either the smallest commercially available quantum dot 525 (QD525) or the several nanometer larger (and thus brighter) QD605 (referred to as nanoGFP-QD525 and nanoGFP-QD605, respectively). Targeting the yellow fluorescent protein-tagged GluN1 subunit in rat hippocampal neurons, we compared these two probes to a previously established larger probe, a rabbit anti-GFP IgG together with a secondary IgG conjugated to QD605 (referred to as antiGFP-QD605). The nanoGFP-based probes allowed faster lateral diffusion of the NMDARs, with several-fold increased median values of the diffusion coefficient (D). Using thresholded tdTomato-Homer1c signals to mark synaptic regions, we found that the nanoprobe-based D values sharply increased at distances over 100 nm from the synaptic edge, while D values for antiGFP-QD605 probe remained unchanged up to a 400 nm distance. Using the nanoGFP-QD605 probe in hippocampal neurons expressing the GFP-GluN2A, GFP-GluN2B, or GFP-GluN3A subunits, we detected subunit-dependent differences in the synaptic localization of NMDARs, D value, synaptic residence time, and synaptic-extrasynaptic exchange rate. Finally, we confirmed the applicability of the nanoGFP-QD605 probe to study differences in the distribution of synaptic NMDARs by comparing to data obtained with nanoGFPs conjugated to organic fluorophores, using universal point accumulation imaging in nanoscale topography and direct stochastic optical reconstruction microscopy.SIGNIFICANCE STATEMENT Our study systematically compared the localization and mobility of surface NMDARs containing GFP-GluN2A, GFP-GluN2B, or GFP-GluN3A subunits expressed in rodent hippocampal neurons, using anti-green fluorescent protein (GFP) nanobodies conjugated to the quantum dot 605 (nanoGFP-QD605), as well as nanoGFP probes conjugated with small organic fluorophores. Our comprehensive analysis showed that the method used to delineate the synaptic region plays an important role in the study of synaptic and extrasynaptic pools of NMDARs. In addition, we showed that the nanoGFP-QD605 probe has optimal parameters for studying the mobility of NMDARs because of its high localization accuracy comparable to direct stochastic optical reconstruction microscopy and longer scan time compared with universal point accumulation imaging in nanoscale topography. The developed approaches are readily applicable to the study of any GFP-labeled membrane receptors expressed in mammalian neurons.

• MeSH
• hipokampus metabolismus   MeSH
• imunoglobulin G metabolismus   MeSH
• jednodoménové protilátky * metabolismus   MeSH
• králíci MeSH
• krysa rodu rattus MeSH
• neurony metabolismus   MeSH
• receptory N-methyl-D-aspartátu * metabolismus   MeSH
• savci MeSH
• synapse fyziologie   MeSH
• zvířata MeSH
• Check Tag
• králíci MeSH
• krysa rodu rattus MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH

It has become evident that epitranscriptome events, mediated by specific enzymes, regulate gene expression and, subsequently, cell differentiation processes. We show that methyltransferase-like proteins METTL3/METTL14 and N6-adenosine methylation (m6A) in RNAs are homogeneously distributed in embryonic hearts, and histone deacetylase (HDAC) inhibitors valproic acid and Trichostatin A (TSA) up-regulate METTL3/METTL14 proteins. The levels of METTL3 in mouse adult hearts, isolated from male and female animals, were lower in the aorta and pulmonary trunks when compared with atria, but METT14 was up-regulated in the aorta and pulmonary trunk, in comparison with ventriculi. Aging caused METTL3 down-regulation in aorta and atria in male animals. Western blot analysis in differentiated mouse embryonic stem cells (mESCs), containing 10-30 percent of cardiomyocytes, showed METTL3/METTL14 down-regulation, while the differentiation-induced increased level of METTL16 was observed in both wild type (wt) and HDAC1 depleted (dn) cells. In parallel, experimental differentiation in especially HDAC1 wild type cells was accompanied by depletion of m6A in RNA. Immunofluorescence analysis of individual cells revealed the highest density of METTL3/METTL14 in α-actinin positive cardiomyocytes when compared with the other cells in the culture undergoing differentiation. In both wt and HDAC1 dn cells, the amount of METTL16 was also up-regulated in cardiomyocytes when compared to co-cultivated cells. Together, we showed that distinct anatomical regions of the mouse adult hearts are characterized by different levels of METTL3 and METTL14 proteins, which are changed during aging. Experimental cell differentiation was also accompanied by changes in METTL-like proteins and m6A in RNA; in particular, levels and distribution patterns of METTL3/METTL14 proteins were different from the same parameters studied in the case of the METTL16 protein.

• MeSH
• adenosin analogy a deriváty   genetika   metabolismus   MeSH
• buněčná diferenciace MeSH
• HEK293 buňky MeSH
• HeLa buňky MeSH
• kardiomyocyty cytologie   metabolismus   MeSH
• lidé MeSH
• methyltransferasy metabolismus   MeSH
• myší embryonální kmenové buňky cytologie   metabolismus   MeSH
• myši inbrední C57BL MeSH
• myši MeSH
• stárnutí metabolismus   patologie   MeSH
• zvířata MeSH
• Check Tag
• lidé MeSH
• mužské pohlaví MeSH
• myši MeSH
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH

• MeSH
• nádory brzlíku genetika   patologie   MeSH
• nádory pleury genetika   patologie   MeSH
• nádory plic genetika   patologie   MeSH
• nádory srdce genetika   patologie   MeSH
• Publikační typ
• monografie MeSH

• Konspekt
• Patologie. Klinická medicína
• NLK Obory
• patologie
• pneumologie a ftizeologie
• kardiologie
• onkologie
• NLK Publikační typ
• publikace WHO

• MeSH
• krevní banky MeSH
• krevní transfuze MeSH
• péče o pacienta MeSH
• transfuzní lékařství MeSH
• Publikační typ
• kongresy MeSH
• zprávy MeSH

• Konspekt
• Patologie. Klinická medicína
• NLK Obory
• hematologie a transfuzní lékařství
• NLK Publikační typ
• brožury

• MeSH
• demografie MeSH
• Publikační typ
• statistiky MeSH
• Geografické názvy
• Československo MeSH

• Konspekt
• Demografie. Populace
• NLK Obory
• demografie