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1.
Urologe A ; 61(1): 18-30, 2022 Jan.
Article in German | MEDLINE | ID: mdl-34605933

ABSTRACT

BACKGROUND: The insertion of a Foley catheter (FC) or a suprapubic catheter (SPC) in lifelong intent is an intervention with significant complications, comorbidities and impact on the further life that has not yet been analyzed. METHODOLOGY: The analysis was based on a validated assessment of catheter-related QoL with 25 items in 5 domains and applied to patients with a Foley or suprapubic catheter in lifelong indication and with the catheter in place for at least 3 months. Assessment data were enriched with information on the type and diameter of the catheter as well as demographic data. RESULTS: Questionnaires from 357 patients (260 male, 97 female, 193 with suprapubic catheter, 162 with Foley catheter, 2 no information) were included in the study. Patients with a Foley catheter were significantly older than patients with a suprapubic catheter (78.9 ± 11.1 years vs. 74.4. ± 12.6 years, p < 0.001). The average QoL score was 4.1 points on a scale from 1 (maximum impairment of QoL) to 5 (no impairment of QoL) indicating a moderately negative impact on QoL. Scores below the average were mainly driven and accompanied by a fear of urine leakage, urine odor, painful catheter changes and urinary infections increasing with age. Additionally, patients were worried about negative effects on their daily life activities due to the catheter. These worries seemed to be more pronounced in females with urinary incontinence, patients with a catheter size ≥ 18 Ch. and with an age of < 70 years. The type of catheter showed a greater impact on the QoL in females with suprapubic catheters when compared with males in contrast to patients with transurethral catheters. CONCLUSION: The results of the study provide further information for the medical clarification for patients and caregivers, having to decide between a lifelong catheter drainage or alternatives, such as provision of an aid or surgical recanalization.


Subject(s)
Quality of Life , Urinary Tract Infections , Aged , Female , Humans , Male , Urinary Bladder , Urinary Catheterization , Urinary Catheters
2.
J Cell Biol ; 155(2): 239-49, 2001 Oct 15.
Article in English | MEDLINE | ID: mdl-11591731

ABSTRACT

Cytokinesis requires membrane fusion during cleavage-furrow ingression in animals and cell plate formation in plants. In Arabidopsis, the Sec1 homologue KEULE (KEU) and the cytokinesis-specific syntaxin KNOLLE (KN) cooperate to promote vesicle fusion in the cell division plane. Here, we characterize AtSNAP33, an Arabidopsis homologue of the t-SNARE SNAP25, that was identified as a KN interactor in a yeast two-hybrid screen. AtSNAP33 is a ubiquitously expressed membrane-associated protein that accumulated at the plasma membrane and during cell division colocalized with KN at the forming cell plate. A T-DNA insertion in the AtSNAP33 gene caused loss of AtSNAP33 function, resulting in a lethal dwarf phenotype. atsnap33 plantlets gradually developed large necrotic lesions on cotyledons and rosette leaves, resembling pathogen-induced cellular responses, and eventually died before flowering. In addition, mutant seedlings displayed cytokinetic defects, and atsnap33 in combination with the cytokinesis mutant keu was embryo lethal. Analysis of the Arabidopsis genome revealed two further SNAP25-like proteins that also interacted with KN in the yeast two-hybrid assay. Our results suggest that AtSNAP33, the first SNAP25 homologue characterized in plants, is involved in diverse membrane fusion processes, including cell plate formation, and that AtSNAP33 function in cytokinesis may be replaced partially by other SNAP25 homologues.


Subject(s)
Arabidopsis Proteins/physiology , Arabidopsis/cytology , Carrier Proteins/physiology , Cell Division , Membrane Proteins/metabolism , Membrane Proteins/physiology , Plant Proteins , Vesicular Transport Proteins , Amino Acid Sequence , Arabidopsis/anatomy & histology , Arabidopsis/metabolism , Arabidopsis Proteins/genetics , Arabidopsis Proteins/metabolism , Carrier Proteins/genetics , Cell Cycle Proteins , Intracellular Membranes/chemistry , Membrane Fusion , Membrane Proteins/genetics , Molecular Sequence Data , Mutagenesis, Insertional , Mutation , Nerve Tissue Proteins/genetics , Nerve Tissue Proteins/physiology , Phenotype , Qa-SNARE Proteins , Qb-SNARE Proteins , Qc-SNARE Proteins , Sequence Homology, Amino Acid , Synaptosomal-Associated Protein 25 , Tissue Distribution , Two-Hybrid System Techniques
3.
Curr Opin Plant Biol ; 1(6): 486-91, 1998 Dec.
Article in English | MEDLINE | ID: mdl-10066634

ABSTRACT

In phragmoplast-assisted cytokinesis of somatic cells, vesicle fusion generates a cell plate that matures into a new cell wall and its flanking plasma membranes. Insight into this dynamic process has been gained in the past few years and additional molecular components of the basic machinery of cytokinesis have been identified. Specialized modes of cytokinesis occur in meiosis and gametophyte development, and recent studies indicate that they are genetically distinct from somatic cytokinesis.


Subject(s)
Cell Cycle , Plant Cells , Plant Development , Plants/ultrastructure , Subcellular Fractions
4.
Biol Chem Hoppe Seyler ; 370(3): 229-38, 1989 Mar.
Article in English | MEDLINE | ID: mdl-2653363

ABSTRACT

Fatty-acid-binding proteins are known to occur in the cytosol of mammalian cells and to bind fatty acids and their CoA-esters. Application of the postembedding protein A-gold labeling method with antibody against the hepatic type fatty-acid-binding protein (hFABP) to cross-sections of liver cells and a newly developed gel-chromatographic immunofluorescence assay established qualitatively (1) that hFABP in mitochondria was confined to outer mitochondrial membranes, (2) the presence of this protein in microsomes and (3) that nuclei were also filled with hFABP. Quantitative data elaborated with a non-competitive ELISA confirmed these results. A significant difference to the distribution of cardiac FABP in heart muscle cells, where this type of protein was found in cytosol, matrix and nuclei, was observed (Börchers et al. (1989) Biochim. Biophys. Acta, in the press). hFABP-containing rat liver microsomes were incubated with long-chain acyl-CoAs in the presence of hFABP (isolated from rat liver cytosol) in a study on the acylation of sn-glycerol-3-phosphate and lysophosphatidic acid. Both acyltransferases were stimulated by addition of hFABP to the incubation medium. The morphological, immunochemical as well as kinetic data infer a direct interaction of hFABP with microsomal membranes in liver cells.


Subject(s)
Carrier Proteins/metabolism , Liver/metabolism , Microsomes, Liver/metabolism , Neoplasm Proteins , Nerve Tissue Proteins , Phosphatidic Acids/biosynthesis , Acyltransferases/metabolism , Animals , Carrier Proteins/immunology , Cattle , Chromatography, Gel , Enzyme-Linked Immunosorbent Assay , Fatty Acid-Binding Protein 7 , Fatty Acid-Binding Proteins , Fluorescent Antibody Technique , Immunohistochemistry , In Vitro Techniques , Liver/cytology , Microscopy, Electron , Mitochondria, Liver/metabolism , Rats , Subcellular Fractions/enzymology , Subcellular Fractions/metabolism
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