PubMed · 13963164
The source did not provide an abstract. Follow the original record for more information.
Explore connections, maps & timelines
M FUJIMAKI. 1962. [The thrombotest].. https://pubmed.ncbi.nlm.nih.gov/13963164/
Cite the original work for its findings. Save a collection to share your selection of sources.
KEEP EXPLORING
Hypothermia has long been known to be a potent putative neuroprotectant. Experimental evidence and clinical experience show that hypothermia protects the brain from cerebral injury. Recent insights into the mechanisms of cerebral ischemia and reperfusion suggest reasons why hypothermia may be an ideal modality for stroke therapy. Hypothermia protects brain tissue in multiple ways. It retards energy depletion, reduces intracellular acidosis, lessens the ischemia related accumulation of excitotoxic neurotransmitters, and attenuates the influx of intracellular calcium. Additionally, hypothermia suppresses the generation of oxygen free radicals involved in secondary damage associated with reperfusion. It also suppresses the mechanisms related to blood-brain barrier degeneration and postischemic remodeling. The clinical application of therapeutic hypothermia and its limitations will be summarized in this paper. Therapeutic hypothermia is likely to undergo phase III clinical trials in various clinical settings. Novel technologies are being developed to optimize the safety and efficacy of this promising approach.
The maintenance of the equilibrium between coagulation and fibrinolysis is crucial for normal haemostasis. In contrast, pathologic consequences of imbalance manifest tendencies of bleeding or thrombosis. Procarboxypeptidase U (proCPU, TAFI) is recognized as an important link between the coagulation system and fibrinolysis. Following activation by thrombin (IIa), carboxypeptidase U (CPU) exerts an antifibrinolytic effect by abolishing the cofactor function of partially degraded fibrin in plasminogen (Pg) activation. This review article focuses on the role of the proCPU/CPU system in the balance between fibrin deposition and removal. How a disturbed system can lead to a higher thrombotic tendency is discussed, while CPU inhibition as a new drug target for fibrinolytic therapy is extensively reviewed.
The strive for more standardised and highly efficacious products is one of the important mainstays in modern haemotherapy. Coagulation active plasma for transfusion is the product of choice when treating hereditary or acquired isolated or complex coagulopathies, when no specific concentrate is available. The aim of this study was to perform an extensive biochemical comparison of the pharmaceutically licensed coagulation active plasma named Octaplas with an identical, but universally applicable, development product (Uniplas, working title) and single-donor fresh-frozen plasma (FFP) units subjected to a medical device treatment using a combination of methylene-blue dye and subsequent white-light exposure (MB plasma). Our study showed that there are differences in the biochemical characteristics between Octaplas and MB plasma, while Uniplas revealed the same quality as Octaplas. The variability of selected plasma proteins in the 20 individual MB plasma units tested was high compared to Octaplas/Uniplas. Beyond the reported decreased levels of protein S and plasmin inhibitor found in Octaplas/Uniplas, and the significant loss of fully functional fibrinogen in MB plasma and its impact on selected global coagulation parameters, the latter product additionally revealed several coagulation factor activities outside the ranges given for normal single-donor FFP. It is important for plasma prescribers to be aware of the major inherent differences between Octaplas and MB plasma.