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The superiority of an extracellular fluid solution over Euro-Collins' solution for pulmonary preservation.

Limited donor supply is the major factor restricting the application of lung transplantation. A uniformly reliable method of lung preservation would improve donor organ availability. At present, Euro-Collins' solution, an intracellular fluid-type solution, is most widely used in organ preservation. However, we have previously shown that initial pulmonary flush with an extracellular-type solution (low-potassium dextran solution [LPD]) provided better pulmonary preservation than Euro-C. In the present study, we used an in vitro-ventilated, blood-perfused rabbit lung model to examine whether the mechanism for this improvement was related to the effect of LPD during pulmonary flush or its effect during storage. Rabbit lungs were harvested and stored after pulmonary flush with different solutions (group 1: 400 ml of LPD; group 2: 400 ml of Euro-C; group 4: 300 ml of Euro-C followed by 100 ml of LPD; n = 5 in each group). The lungs were then preserved at 10 degrees C for 18 hr and reperfused with fresh venous blood. After 10 min of reperfusion, lungs in group 1 showed the highest PO2 (group 1: 124.4 +/- 7.7 mmHg; group 2: 46.2 +/- 9.4 mmHg P less than 0.01). Lungs in both group 3 and group 4 showed better lung function and lower wet/dry weight ratio than those in group 2. We conclude that LPD provides better lung preservation by its effects both on pulmonary flush and on storage.

Animals↗

Familial Alzheimer's disease cells abnormally accumulate beta-amyloid-harbouring peptides preferentially in cytosol but not in extracellular fluid.

The proteolytic processing of beta-amyloid precursor protein (APP) was analyzed and compared for familial Alzheimer's disease and normal lymphoid cells, focusing on beta-amyloid-harbouring peptides and the extracellular fragments released into the medium. Tris/tricine gel electrophoresis of anti-beta A4-(8-17)-immunoprecipitated peptides and subsequent N-terminal amino acid sequencing revealed previously unidentified peptides; the 14-kDa peptide with a beta A4 N-terminus and the 12-kDa peptide with an Esch's-site N-terminus in the cytosols, and the same 12-kDa peptide predominating in the media. Moreover, some early onset familial Alzheimer's disease cells, but not normal cells, express a 4-kDa peptide with a beta-amyloid N-terminus in the cytosol. Two-dimensional gel electrophoresis of the extracellular APP peptides immunoprecipitated with anti-APP-(144-654)-peptide showed that familial Alzheimer's disease cells are deficient in processing, especially the 50-53-kDa peptides with the Kunitz-protease-inhibitor domain. This may reflect their unique expression of a serine protease identified as cleaving APP at the beta-amyloid N-terminus.

Alzheimer Disease↗

Subarachnoid blood infusion versus raised intracranial pressure: effects on the amino acid pattern in the extracellular fluid of the rabbit hippocampus.

In order to evaluate the role of a hemorrhage versus that of a transient increase in intracranial pressure in subarachnoid hemorrhage, the two components were induced separately in rabbits. Extracellular glutamate, sampled from the hippocampus with microdialysis, was used to evaluate the degree of CNS tissue damage. In four rabbits, autologous arterial blood was infused in the cisterna magna in a volume that would not affect the intracranial pressure. The other group of animals was infused with saline to elevate the intracranial pressure from 10 to > 100 mmHg. The increase of intracranial pressure per se did not induce significant changes in extracellular glutamate. However, 20-60 min after infusion of blood, a significant glutamate increase was recorded. Furthermore, aspartate, alanine, glycine and serine were also raised. The results indicate that blood in the subarachnoid space damages the brain primarily by inducing ischemia. Furthermore, the parameters employed gave no indication that an increase in intracranial pressure had a deleterious effect on CNS tissue.

Amino Acids↗