Virtual simulation-enhanced triage training for Iraqi medical personnel.

Triage, establishing the priority of care among casualties in disaster management, is generally practiced using constructive tabletop or live exercises. Actual disasters involving multiple casualties occur rarely, offering little opportunity for gaining experience and competency assessment. When they do occur, response needs to be rapid and well-learned.

Sprouting and abnormal contacts of nonmedullated axons, and deposition of extracellular material induced by the amyloid precursor protein (APP) and other protease inhibitors.

We have reported that the local administration of serine protease inhibitors (amyloid precursor protein with the Kunitz insert (APP K+), aprotinin, and leupeptin) to the rat sciatic nerve determines a sprouting response of myelinated axons, proliferation of Schwann cells, and demyelination, 5 to 7 days later. Further study of these nerves with the electron microscope revealed (i) a sprouting response of nonmedullated axons, (ii) the appearance of fine axons with a few turns of compact myclin, (iii) abnormal contracts of axons with basal laminae, with fibroblast-like cells, and between them, (iv) the occurrence of hemidesmosome- and desmosome-like junctions between Schwann cell processes, and between Schwann cells and axons, and (v) the appearance of amorphous and fibrillary extracellular deposits alongside the axolemma. The adjacent proximal and distal segments were normal, i.

Secreted forms of beta-amyloid precursor protein protect against ischemic brain injury.

The beta-amyloid precursor protein (beta APP) is the source of the amyloid beta-peptide that accumulates in the brain in Alzheimer's disease. A major processing pathway for beta APP involves an enzymatic cleavage within the amyloid beta-peptide sequence that liberates secreted forms of beta APP (APPss) into the extracellular milieu. We now report that postischemic administration of these APPss intracerebroventricularly protects neurons in the CA1 region of rat hippocampus against ischemic injury.

Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein.

The beta-amyloid precursor protein (beta APP) is a membrane-spanning glycoprotein that is the source of the beta-amyloid peptide (beta AP) which accumulates as senile plaques in the brains of patients with Alzheimer's disease. beta APP is normally processed such that a cleavage occurs within the beta AP, liberating secreted forms of beta APP (APPss) from the cell. The neuronal functions of these forms are unknown.

Apolipoprotein E: phospholipid binding studies with synthetic peptides from the carboxyl terminus.

We have previously shown that the synthetic peptide apoE(129-169) forms lipid-peptide complexes with dimyristoylphosphatidylcholine (DMPC) with an L:P molar ratio of 125:1; the peptide in the isolated complex contains approximately 56% alpha-helicity. These results verify the presence of an amphipathic alpha-helix in this region of apoE as predicted by Chou-Fasman analysis and hydrophobicity calculations. To further define the lipid binding regions of apoE, we have synthesized four peptides, apoE(211-243), -(202-243), -(267-286), and -(263-286), from the carboxyl terminus of apoE and studied their lipid binding properties; apoE(202-243) contains two potential amphipathic helices.