Kazuistika popisuje vývoj inkontinenčních obtíží u pacientky s diagnózou hyperaktivního močového měchýře od jejího stanovení přes nasazení terapie, její změnu pro nedostatečný efekt a následný ústup obtíží.
The case report describes the course of incontinence symptoms in a female patient diagnosed with overactive bladder, including the establishment of diagnosis, treatment initiation, its change due to insufficient effect, and subsequent subsiding of the symptoms.
- MeSH
- farmakoterapie metody MeSH
- lidé MeSH
- senioři MeSH
- urgentní inkontinence * diagnóza farmakoterapie terapie MeSH
- výsledek terapie MeSH
- Check Tag
- lidé MeSH
- senioři MeSH
- ženské pohlaví MeSH
- Publikační typ
- kazuistiky MeSH
BACKGROUND: The Nse1, Nse3 and Nse4 proteins form a tight sub-complex of the large SMC5-6 protein complex. hNSE3/MAGEG1, the mammalian ortholog of Nse3, is the founding member of the MAGE (melanoma-associated antigen) protein family and the Nse4 kleisin subunit is related to the EID (E1A-like inhibitor of differentiation) family of proteins. We have recently shown that human MAGE proteins can interact with NSE4/EID proteins through their characteristic conserved hydrophobic pocket. METHODOLOGY/PRINCIPAL FINDINGS: Using mutagenesis and protein-protein interaction analyses, we have identified a new Nse3/MAGE-binding domain (NMBD) of the Nse4/EID proteins. This short domain is located next to the Nse4 N-terminal kleisin motif and is conserved in all NSE4/EID proteins. The central amino acid residues of the human NSE4b/EID3 domain were essential for its binding to hNSE3/MAGEG1 in yeast two-hybrid assays suggesting they form the core of the binding domain. PEPSCAN ELISA measurements of the MAGEC2 binding affinity to EID2 mutant peptides showed that similar core residues contribute to the EID2-MAGEC2 interaction. In addition, the N-terminal extension of the EID2 binding domain took part in the EID2-MAGEC2 interaction. Finally, docking and molecular dynamic simulations enabled us to generate a structure model for EID2-MAGEC2. Combination of our experimental data and the structure modeling showed how the core helical region of the NSE4/EID domain binds into the conserved pocket characteristic of the MAGE protein family. CONCLUSIONS/SIGNIFICANCE: We have identified a new Nse4/EID conserved domain and characterized its binding to Nse3/MAGE proteins. The conservation and binding of the interacting surfaces suggest tight co-evolution of both Nse4/EID and Nse3/MAGE protein families.
- MeSH
- interakční proteinové domény a motivy MeSH
- intracelulární signální peptidy a proteiny chemie genetika metabolismus MeSH
- jaderné proteiny chemie MeSH
- konzervovaná sekvence MeSH
- lidé MeSH
- molekulární modely MeSH
- molekulární sekvence - údaje MeSH
- mutageneze cílená MeSH
- peptidové fragmenty chemie genetika metabolismus MeSH
- počítačová simulace MeSH
- proteiny buněčného cyklu genetika metabolismus MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- Schizosaccharomyces pombe - proteiny chemie MeSH
- Schizosaccharomyces MeSH
- sekvence aminokyselin MeSH
- substituce aminokyselin MeSH
- techniky dvojhybridového systému MeSH
- transportní proteiny chemie genetika metabolismus MeSH
- vazba proteinů MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- MeSH
- analýza potravin MeSH
- dietní tuky MeSH
- lidé MeSH
- mastné kyseliny chemie MeSH
- Check Tag
- lidé MeSH
- Geografické názvy
- Česká republika MeSH
