title: Synuclein expression in the lizard Anolis carolinensis.
abstract: The synuclein (syn) family comprises three proteins: α-, β- and γ-syns. In humans, they are involved in neurodegenerative diseases such as Parkinson's disease and in tumors. Members of the syn family were sequenced in representative species of all vertebrates and the comparative analysis of amino acid sequences suggests that syns are evolutionarily conserved, but information about their expression in vertebrate lineages is still scarce and completely lacking in reptiles. In this study, the expression of genes coding for α-, β- and γ-syns was analyzed in the green lizard Anolis carolinensis by semiquantitative RT-PCR and Western blot. Results demonstrate good expression levels of the three syns in the lizard nervous system, similarly to human syns. This, together with the high identity between lizard and human syns, suggests that these proteins fulfill evolutionarily conserved functions. However, differences between lizard and humans in the expression of syn variants (two different variants of γ-syn were detected in A. carolinensis) and differences in some amino acids in key positions for the regulation of protein conformation and affinity for lipid and metal ions also suggest that these proteins may have acquired different functional specializations in the two lineages.
authors.affiliation: Department of Biology and Biotechnology "Charles Darwin", Sapienza University, 00161, Rome, Italy. mattia.toni@uniroma1.it.
authors.forename: Mattia
authors.identifier: 0000-0001-7167-4051
authors.initials: M
authors.lastname: Toni
authors.affiliation: Department of Biology and Biotechnology "Charles Darwin", Sapienza University, 00161, Rome, Italy.
authors.forename: Carla
authors.initials: C
authors.lastname: Cioni
authors.affiliation: Department of Biology and Biotechnology "Charles Darwin", Sapienza University, 00161, Rome, Italy.
authors.forename: Federica
authors.initials: F
authors.lastname: De Angelis
authors.affiliation: Department of Biochemical Sciences, Sapienza University, 00185, Rome, Italy.
authors.forename: Maria Carmela Bonaccorsi
authors.initials: MC
authors.lastname: di Patti
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D026481:Blotting, Far-Western; D001921:Brain / Q000378:metabolism; D019143:Evolution, Molecular; D005123:Eye / Q000378:metabolism; D015870:Gene Expression; D006801:Humans; D007413:Intestinal Mucosa / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008116:Lizards / Q000378:metabolism*; D008168:Lung / Q000378:metabolism; D009132:Muscles / Q000378:metabolism; D009206:Myocardium / Q000378:metabolism; D020033:Protein Isoforms; D017433:Protein Structure, Secondary; D012333:RNA, Messenger / Q000378:metabolism; D060888:Real-Time Polymerase Chain Reaction; D017386:Sequence Homology, Amino Acid; D013116:Spinal Cord / Q000378:metabolism; D051843:Synucleins / Q000378:metabolism*
chemical_list: D020033:Protein Isoforms; D012333:RNA, Messenger; D051843:Synucleins
keywords: Anolis carolinensis; Lizard; Parkinson’s disease; RT-PCR; Synuclein