[Multi-professional Clearing in a Model Project based on § 64b SGB V by the Example of Geriatric Psychiatry].

As part of the largest model project in Germany in accordance with § 64b SGB V at the Pfalzklinikum, a clearing concept was developed in the Clinic for Geriatric Psychiatry to ensure rapid and adequate diagnosis and effective referral to the further treatment setting. Retrospective data of all clearing cases from the first year are presented. In addition to demographic data and treatment diagnoses, the distribution of patients across settings providing further treatment is presented.

beta-amyloid precursor protein can be transported independent of any sorting signal to the axonal and dendritic compartment.

In neurons, amyloid precursor protein (APP) is localized to the dendritic and axonal compartment. Changes in subcellular localization affect secretase cleavage of APP, altering the generation of Abeta, and presumably also its pathogenic features. It was reported that APP is sorted initially to the axon and transcytosed subsequently to the somatodendritic compartment.

PAT1a modulates intracellular transport and processing of amyloid precursor protein (APP), APLP1, and APLP2.

Understanding the intracellular transport of the beta-amyloid precursor protein (APP) is a major key to elucidate the regulation of APP processing and thus beta-amyloid peptide generation in Alzheimer disease pathogenesis. APP and its two paralogues, APLP1 and APLP2 (APLPs), are processed in a very similar manner by the same protease activities. A putative candidate involved in APP transport is protein interacting with APP tail 1 (PAT1), which was reported to interact with the APP intracellular domain.