ABSTRACT
As in other countries, suicides are a matter of great concern in The Netherlands. This article addresses suicide-prevention measures in prisons in The Netherlands. It focuses primarily on screening, monitoring, incapacitation, psychological support, and transferal to specialized institutions. In addition, it asks which practices are common, which can be improved, and the limitations of certain strategies. Relatively speaking, The Netherlands does not appear to be doing too badly in terms of preventive measures, although there is room for improvement.
Subject(s)
Cross-Cultural Comparison , Prisoners , Suicide Prevention , Adult , Crisis Intervention , Female , Humans , Male , Mass Screening , Netherlands/epidemiology , Prisoners/psychology , Prisoners/statistics & numerical data , Referral and Consultation , Risk Factors , Suicide/psychology , Suicide/statistics & numerical dataABSTRACT
The endocytic activity of chick myotubes in cultures was investigated. Differentiated myotubes internalized the fluid-phase marker horseradish peroxidase in membrane-bound particles which typically displayed reaction product at the inner surface of the vesicle. Pulse-chase experiments demonstrated a rapid decrease in the number of horseradish peroxidase-containing vesicles and a redistribution from a uniform to a perinuclear pattern. Horseradish peroxidase uptake was extensively inhibited by incubation at 0-4 degrees C consistent with an endocytic mechanism. To further characterize the process, the fate of labeled protein was investigated. Following uptake [3H] hemoglobin A was extensively degraded (40-50%) to acid-soluble products within 10 h. Degradation displayed a biphasic pattern with a rapid early phase followed by a much slower second phase. The decreasing rate of proteolysis can be accounted for, in part, by a simultaneous exocytosis of a substantial fraction (25-30%) of acid-insoluble label from myotubes. The lysosomotropic agents methylamine, monensin, and chloroquine significantly inhibited (23-75%) proteolysis, indicating a lysosomal site of degradation. Part of the inhibitory effect results from an increase in exocytosis in the presence of these agents. Degradation of endocytosed [3H]hemoglobin A was not inhibited by insulin. In contrast degradation of endogenous myotube proteins was inhibited (40%) by insulin and blocked by methylamine. These results suggest that cultured myotubes possess a coupled endocytic/exocytic pathway for macromolecules and that a fraction of the internalized substrate is degraded by an insulin-insensitive lysosomal pathway.
