CONICET | Buscador de Institutos y Recursos Humanos

Consolidation is necessary to convert a short-term labile memory to a long-term and stable form. During consolidation, gene expression and de novo protein synthesis are regulated in order to produce key proteins in the maintenance of plastic changes produced during the acquisition of new information. Human β-amyloid, the main component in the neuritic plaques found in patients with Alzheimer decease, is generated by a cleavage of the beta-amyloid precursor protein. It has been proposed to cause memory deficiencies observed in this illness. Members of this family are synaptic proteins and have been associated with synaptogenesis and neuronal plasticity, both in vertebrates and in invertebrates. Here we partially cloned and sequenced beta-amyloid precursor protein like gene homologue in the crab Chasmagnathus, showing a 37% of identity with the fruit fly Drosophila melanogaster homologue and 23% with Homo sapiens but with much higher degree of sequence similarity in certain regions. We observed a wide distribution of chappl mRNA in nervous system as well as in muscle and in gills. We found two isoforms of the protein localizing in all tissues analyzed with the exception of muscles, were only one of the isoforms was found. Then we study gene and protein expression in long-term memory formation. We used a memory model well characterize behaviorally and mechanistically: the contextual-signal associative memory paradigm in this crab specie. We then studied the temporal course of gene expression during long-term memory consolidation, observing changes in different time points. We also studied the temporal course of chAPPL protein levels that correlated with the kinetic of gene expression. Immunofluorescence studies reveled localization of chAPPL in associative and sensory brain areas. The results obtained along this work suggest a role of chAPPL during long-term memory formation.