Autorka uvádí syndrom CAN - jeho historii, charakteristiku, diagnostické postupy, terapii a prevenci.
The author presents a CAN syndrome - its history, characterization, diagnostic process, terapy and prevention.
- MeSH
- Child MeSH
- Humans MeSH
- Adolescent MeSH
- Neurotic Disorders etiology MeSH
- Child Behavior Disorders etiology MeSH
- Child, Preschool MeSH
- Sex Work MeSH
- Psychophysiologic Disorders etiology MeSH
- Risk MeSH
- Child Abuse, Sexual classification prevention & control education MeSH
- Check Tag
- Child MeSH
- Humans MeSH
- Adolescent MeSH
- Child, Preschool MeSH
- Publication type
- Review MeSH
ix, 94 s. : tab.
Autor uvádí tři formy komerčně sexuálního zneužití dětí, tj. dětskou pornografii, prostituci a únosy dětí. Zařazuje tuto nozologickou jednotku k syndromu CAN. Předpokládá se, že touto formou sexuálního zneužívání je zasaženo 1% dětí.
The author presents three forms of sexual children's abuse trafficking, i.e. children's pornography, prostitution and children's kidnapping. He classified this nozologic issue with a CAN syndrome. It is presumed that 1% of children to be afflicted by this form of abuse.
- MeSH
- Child MeSH
- Humans MeSH
- Adolescent MeSH
- Sex Work statistics & numerical data MeSH
- Child Abuse, Sexual prevention & control statistics & numerical data MeSH
- Check Tag
- Child MeSH
- Humans MeSH
- Adolescent MeSH
- Geographicals
- Czech Republic MeSH
- MeSH
- Criminology MeSH
- Humans MeSH
- Human Trafficking * MeSH
- Sex Offenses MeSH
- Criminal Law * MeSH
- Check Tag
- Humans MeSH
- Geographicals
- Slovakia MeSH
Trafficking of proteins and lipids within the plant endomembrane system is essential to support cellular functions and is subject to rigorous regulation. Despite this seemingly strict regulation, endomembrane trafficking needs to be dynamically adjusted to ever-changing internal and environmental stimuli, while maintaining cellular integrity. Although often overlooked, the versatile second messenger Ca2+is intimately connected to several endomembrane-associated processes. Here, we discuss the impact of electrostatic interactions between Ca2+and anionic phospholipids on endomembrane trafficking, and illustrate the direct role of Ca2+sensing proteins in regulating endomembrane trafficking and membrane integrity preservation. Moreover, we discuss how Ca2+can control protein sorting within the plant endomembrane system. We thus highlight Ca2+signaling as a versatile mechanism by which numerous signals are integrated into plant endomembrane trafficking dynamics.
Endomembrane traffic in eukaryotic cells functions partially as a means of communication; delivery of membrane in one direction has to be balanced with a reduction at the other end. This effect is typically the case during the defence against pathogens. To combat pathogens, cellular growth and differentiation are suppressed, while endomembrane traffic is poised towards limiting the pathogen attack. The octameric exocyst vesicle-tethering complex was originally discovered as a factor facilitating vesicle-targeting and vesicle-plasma membrane (PM) fusion during exocytosis prior to and possibly during SNARE complex formation. Interestingly, it was recently implicated both in animals and plants in autophagy membrane traffic. In animal cells, the exocyst is integrated into the mTOR-regulated energy metabolism stress/starvation pathway, participating in the formation and especially initiation of an autophagosome. In plants, the first functional link was to autophagy-related anthocyanin import to the vacuole and to starvation. In this concise review, we summarize the current knowledge of exocyst functions in autophagy and defence in plants that might involve unconventional secretion and compare it with animal conditions. Formation of different exocyst complexes during undisturbed cell growth, as opposed to periods of cellular stress reactions involving autophagy, might contribute to the coordination of endomembrane trafficking pathways.
The trafficking dynamics of uromodulin (UMOD), the most abundant protein in human urine, play a critical role in the pathogenesis of kidney disease. Monoallelic mutations in the UMOD gene cause autosomal dominant tubulointerstitial kidney disease (ADTKD-UMOD), an incurable genetic disorder that leads to kidney failure. The disease is caused by the intracellular entrapment of mutant UMOD in kidney epithelial cells, but the precise mechanisms mediating disrupted UMOD trafficking remain elusive. Here, we report that transmembrane Emp24 protein transport domain-containing (TMED) cargo receptors TMED2, TMED9, and TMED10 bind UMOD and regulate its trafficking along the secretory pathway. Pharmacological targeting of TMEDs in cells, in human kidney organoids derived from patients with ADTKD-UMOD, and in mutant-UMOD-knockin mice reduced intracellular accumulation of mutant UMOD and restored trafficking and localization of UMOD to the apical plasma membrane. In vivo, the TMED-targeted small molecule also mitigated ER stress and markers of kidney damage and fibrosis. Our work reveals TMED-targeting small molecules as a promising therapeutic strategy for kidney proteinopathies.
- MeSH
- Humans MeSH
- Membrane Glycoproteins metabolism genetics MeSH
- Mutation MeSH
- Mice MeSH
- Protein Transport * MeSH
- Uromodulin * metabolism genetics MeSH
- Animals MeSH
- Check Tag
- Humans MeSH
- Mice MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
In plants, membrane compartmentalization requires vesicle trafficking for communication among distinct organelles. Membrane proteins involved in vesicle trafficking are highly dynamic and can respond rapidly to changes in the environment and to cellular signals. Capturing their localization and dynamics is thus essential for understanding the mechanisms underlying vesicular trafficking pathways. Quantitative mass spectrometry and imaging approaches allow a system-wide dissection of the vesicular proteome, the characterization of ligand-receptor pairs and the determination of secretory, endocytic, recycling and vacuolar trafficking pathways. In this review, we highlight major proteomics and imaging methods employed to determine the location, distribution and abundance of proteins within given trafficking routes. We focus in particular on methodologies for the elucidation of vesicle protein dynamics and interactions and their connections to downstream signalling outputs. Finally, we assess their biological applications in exploring different cellular and subcellular processes.
xiii, 370 s. : il.
- Keywords
- Nukleus,
- MeSH
- Biological Transport MeSH
- Cell Nucleus MeSH
- Cell Communication MeSH
- Signal Transduction MeSH
- Conspectus
- Biochemie. Molekulární biologie. Biofyzika
- NML Fields
- molekulární biologie, molekulární medicína
- fyziologie
The P2X7 receptor (P2X7R) is a member of the ATP-gated ion channel family that exhibits distinct electrophysiological and pharmacological properties. This includes low sensitivity to ATP, lack of desensitization, a sustained current growth during prolonged receptor stimulation accompanied with development of permeability to large organic cations, and the coupling of receptor activation to cell blebbing and death. The uniquely long C-terminus of P2X7R accounts for many of these receptor-specific functions. The aim of this study was to understand the role of conserved ectodomain cysteine residues in P2X7R function. Single- and double-point threonine mutants of C119-C168, C129-C152, C135-C162, C216-C226, and C260-C269 cysteine pairs were expressed in HEK293 cells and studied using whole-cell current recording. All mutants other than C119T-P2X7R responded to initial and subsequent application of 300-μM BzATP and ATP with small amplitude monophasic currents or were practically nonfunctional. The mutagenesis-induced loss of function was due to decreased cell-surface receptor expression, as revealed by assessing levels of biotinylated mutants. Coexpression of all double mutants with the wild-type receptor had a transient or, in the case of C119T/C168T double mutant, sustained inhibitory effect on receptor trafficking. The C119T-P2X7R mutant was expressed on the plasma membrane and was fully functional with a slight decrease in the sensitivity for BzATP, indicating that interaction of liberated Cys168 with another residue rescues the trafficking of receptor. Thus, in contrast to other P2XRs, all disulfide bonds of P2X7R are individually essential for the proper receptor trafficking.
- MeSH
- Cysteine biosynthesis genetics physiology MeSH
- HEK293 Cells MeSH
- Conserved Sequence * MeSH
- Rats MeSH
- Humans MeSH
- Mutation physiology MeSH
- Receptors, Purinergic P2X7 genetics metabolism MeSH
- Protein Transport physiology MeSH
- Animals MeSH
- Check Tag
- Rats MeSH
- Humans MeSH
- Animals MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Research Support, N.I.H., Intramural MeSH
