Characterization of the beta amyloid precursor protein-like gene in the central nervous system of the crab Chasmagnathus. Expression during memory consolidation

• Autores: Fustiñana, M.S.; Ariel, P.; Federman, N.; Freudenthal, R.; Romano, A.
• Año de publicación: 2010
• Idioma: inglés
• Tipo de recurso: artículo
• Fuente: BMC Neurosci. 2010;11
• Materia: amyloid precursor protein; beta amyloid precursor protein like protein; messenger RNA; unclassified drug; amyloid precursor protein; complementary DNA; messenger RNA; amino acid sequence; amino terminal sequence; animal experiment; animal tissue; antenna I neuropil; antenna II nerve; article; association cortex; associative memory; brain region; carboxy terminal sequence; central nervous system; Chasmagnathus granulatus; ciliary ganglion; controlled study; crab; cranial nerve; deutocerebrum; Drosophila melanogaster; gene expression profiling; gene sequence; gill; glycosylation; immunofluorescence; innervation; long term memory; male; memory consolidation; model; molecular cloning; molecular weight; muscle; neuropil; nonhuman; nucleotide sequence; oculomotor nerve; protein domain; protein expression; protein localization; protocerebrum; sensory cortex; sequence homology; supraesophageal ganglion; tegumentary nerve; thoracic ganglion; tissue distribution; tritocerebrum; animal; biosynthesis; Brachyura; central nervous system; genetics; immunohistochemistry; immunoprecipitation; memory; metabolism; molecular genetics; physiology; reverse transcription polymerase chain reaction; Western blotting; Amino Acid Sequence; Amyloid beta-Protein Precursor; Animals; Base Sequence; Blotting, Western; Brachyura; Central Nervous System; Cloning, Molecular; DNA, Complementary; Immunohistochemistry; Immunoprecipitation; Male; Memory; Molecular Sequence Data; Reverse Transcriptase Polymerase Chain Reaction; RNA, Messenger
• Institución: Universidad Nacional de Buenos Aires. Facultad de Ciencias Exactas y Naturales

Background: Human β-amyloid, the main component in the neuritic plaques found in patients with Alzheimer's disease, is generated by cleavage of the β-amyloid precursor protein. Beyond the role in pathology, members of this protein family are synaptic proteins and have been associated with synaptogenesis, neuronal plasticity and memory, both in vertebrates and in invertebrates. 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 for the maintenance of plastic changes produced during the acquisition of new information.Results: Here we partially cloned and sequenced the beta-amyloid precursor protein like gene homologue in the crab Chasmagnathus (cappl), 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 cappl mRNA in the nervous system as well as in muscle and gills. The protein localized in all tissues analyzed with the exception of muscle. Immunofluorescence revealed localization of cAPPL in associative and sensory brain areas. We studied gene and protein expression during long-term memory consolidation using a well characterized memory model: the context-signal associative memory in this crab species. mRNA levels varied at different time points during long-term memory consolidation and correlated with cAPPL protein levels. Conclusions: cAPPL mRNA and protein is widely distributed in the central nervous system of the crab and the time course of expression suggests a role of cAPPL during long-term memory formation. © 2010 Fustiñana et al; licensee BioMed Central Ltd.
Fil:Fustiñana, M.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Federman, N. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Freudenthal, R. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.
Fil:Romano, A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina.