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Biomedical subjects

H Kunze

Publications and source records attributed to H Kunze.

At least 19 recordsLinked to original sources
PubMed2001

Psychiatric reform in Germany.

OBJECTIVE: To describe the ongoing process of German psychiatric reform and the structure and functioning of mental health services. METHOD: Information sources used include official reports describing mental health services, relevant publications related to organization and functioning of services. RESULTS: There has been far-reaching change in mental health care since the late 1960s: psychiatric hospitals have lost about 50% of their beds and one psychiatric hospital has been closed. One hundred and sixty-five general hospital psychiatric units have been built up. Out-patient, community and residential services have been developed. There is a lack of diversified residential and rehabilitation services, particularly for the most severely ill. Co-ordination of care is not always ensured, transfer of patients to remote nursing homes has occurred in some places. Carers and service users articulate their views to an increasing degree. CONCLUSION: Political and professional enthusiasm have been important in implementation of the German reform. Evolving it further will require major efforts.

Germany↗
PubMed1998

[Basic documentation: inpatient management in a region by a psychiatric hospital and a psychiatric department. Results of a joint evaluation].

A mental hospital and a psychiatric department of a general hospital in the region of Kassel have jointly analysed their basic documentation to produce an overview of hospital treatment of psychiatric patients in the region. Patients from the urban population occupy twice as many beds as those from the rural population which is a hint that standard bed-ratios per population are inadequate. Instead of the unsuitable official definition of duration of stay in hospital we used "days in hospital per person per year". Making allowance for groups of diagnoses this made possible interesting comparisons about the contributions of the two hospitals to the treatment of the psychiatric patients in the region. The two hospitals are not similar and the results show how the patients make use of the possibility of choosing the various specialities of the two hospitals.

Adult↗
PubMed1998

Assessing the quality of psychiatric hospital care: a German approach.

OBJECTIVE: The German Ministry of Health commissioned a nonprofit organization to develop a tool for assessing the quality of psychiatric hospital care. METHODS: The authors were members of an expert group established to develop an assessment tool that could be used by professional caregivers, patients, patients' relatives, managers, purchasers, and mental health care planners. RESULTS: A three-dimensional model was developed in which 23 quality standards may be applied to 28 areas of practice. For each application, questions can be asked at four levels to stimulate ongoing quality management: the individual treatment process, the individual outcome, the treatment unit, and the hospital as a whole. The authors provide sample questions to illustrate the approach. CONCLUSIONS: The approach to quality assessment embodied in the model is comprehensive and addresses ethical issues, but it is also complicated and difficult to handle. Unlike models developed in the United States, it is not intended to be objective or standardized, and it does not yield a score. To some extent, the model's approach to assessment may reflect German cultural values and traditions.

Consumer Advocacy↗
PubMed1997

On the mechanism of lysophospholipase activity of secretory phospholipase A2 (EC 3.1.1.4): deacylation of monoacylphosphoglycerides by intrinsic sn-1 specificity and pH-dependent acyl migration in combination with sn-2 specificity.

We show for the first time that secreted low-molecular weight phospholipase A2 (EC 3.1.1.4) catalyzes the deacylation of monoacylphosphoglycerides directly from the sn-1 position, although at a very low rate: purified phospholipase A2 enzymes from bee venom, crotalus atrox venom, and porcine pancreas hydrolyze the sn-1 ester bond in 1-palmitoyl-2-O-methyl-sn-glycero-3-phosphorylcholine. Hydrolytic rates with the corresponding isomer, 1-O-methyl-2-palmitoyl-sn-glycero-3-phosphorylcholine, are about 3-4 orders of magnitude higher. The similarities in Ca2+ requirement and inactivation profiles suggest that deacylation, albeit with different rates, from both sn-1 and sn-2 positions is catalyzed by the same catalytic site of phospholipase A2. Furthermore, evidence is provided that phospholipase A2-catalyzed 1-acyl lysophospholipid deacylation is mediated by sn-1-directed action, but above pH 7 acyl migration with subsequent enzyme-catalyzed hydrolytic cleavage from the sn-2 position contributes to the overall deacylation of monoacylphosphoglycerides, acyl migration becoming eventually the rate-limiting factor.

Acylation↗
PubMed1996

Subcellular distribution of glycosylphosphatidylinositol-specific phospholipase D in rat liver.

Glycosylphosphatidylinositol (GPI)-hydrolysing enzymes have been described in many mammalian tissues and body fluids; however, their site(s) of action and in vivo functions have remained unclear. In order to identify a possible intracellular site of GPI hydrolysis, we studied the subcellular distribution of GPI-hydrolysing activity in rat liver. We found that purified fractions from rat liver hydrolysed the GPI moieties of two GPI-anchored proteins with the specificity of a phospholipase D. This GPI-specific phospholipase D (GPI-PLD) activity was found to be highly enriched in a lysosomal fraction and showed a similar intracellular distribution to that of typical lysosomal enzymes. Our results indicate that lysosomes may represent a possible intracellular site of GPI-PLD action.

Animals↗
PubMed1994

Heterogeneity of Wistar rats with respect to acid beta-D-glucuronidase (EC 3.2.1.31) in liver.

Commercially available Wistar rats are genetically heterogeneous with respect to acid beta-D-glucuronidase (EC 3.2.1.31) in liver tissue: Of 43 rats studied, 27 animals exhibited only approximately 40% catalytic activity of the remaining group. Analysis by subcellular and density gradient fractionation, and polyacrylamide gel electrophoresis techniques showed that livers with high activity exhibit a dual enzyme distribution in lysosomes (app. 76%) and endoplasmic reticulum (named "microsomal enzyme form"; app. 24%), whereas those with low activity not only lack the microsomal enzyme form - presumably due to the absence of egasyn - but also display reduced lysosomal enzyme activity.

Animals↗
PubMed1993

Intralysosomal glycerophospholipid catabolism in liver: hydrolysis of amino alcohol-containing phospholipids and their metabolites.

Liver lysosomes were isolated from untreated rats and rats pretreated with Triton WR-1339. Purified lysosomes were also separated into lysosomal matrix and membrane fractions. With freshly prepared and frozen biological material, the lysosomal catabolism of various stereospecifically radiolabeled amino alcohol-containing glycerophospholipids and their potential metabolites was studied. Basically there was no qualitative difference in the formation of phospholipid metabolites in both preparations: after long-term incubation, free fatty acids, lysophospholipids, acyl-free phosphodiesters were detected, and to a far lesser extent, amino alcohol-containing phosphomonoesters and only traces of free amino alcohols. These findings indicate the presence of lysosomal phospholipases A as well as C and lysophospholipase(s), with pH optima of about 4.5, and they clearly exclude phospholipase D activity. Unfractionated lysosomes and their soluble as well as particulate subfractions were not capable of hydrolysing the acyl-free amino alcohol-containing phosphodiesters. These compounds must therefore be considered one of the end products of the intralysosomal catabolism of amino alcohol-containing phosphoglycerides. They are presumably cleared from the lysosomal compartment by an as yet unknown transport system in the lysosomal membrane. In liver, the extralysosomal site of their (Mg(2+)-dependent) hydrolysis seems to be the plasma membrane. By contrast, hydrolysis of glycero-3-phosphate and the amino alcohol-containing phosphomonoesters was catalysed in the lysosomal compartment, with a pH optimum of about 5.0, although at considerably lower rates than that of glycero-2-phosphate, a model substrate for lysosomal acid phosphatase.

Amino Alcohols↗