AIMTo provide more molecular evidences for species relationship between Chuanxiong (Ligusticum chuanxiong Hort.) from China and Japanese Chuanxiong (Senkyu in Japanese) (Cnidium officinale Makino).

METHODSTo sequence such two genes as internal transcribed spacer (ITS) from nuclear rDNA and maturase for lysine (matK) in tRNA(lys) (UUU) intron from chloroplast DNA of both Ligusticum chuanxiong and Cnidium officinale using PCR direct sequencing and to analyze the sequence variation of two genes between these two species.

RESULTSThe matK gene sequence of Ligusticum chuanxiong and Cnidium officinale is 1268 bp in length, coding 422 amino acids of maturase protein. ITS gene sequence 699 bp, consisting of 54 bp of 18S rRNA-3', 215 bp of ITS1, 162 bp of 5.8S rRNA, 222 bp of ITS2, 46 bp of 26S rRNA-5'. Multiple sequence alignment shows that the sequence of two genes between dried crude drug and fresh voucher material of Ligusticum chuanxiong and Cnidium officinale, there is 1 variable site (T-->C) in matK (upstream at 595 nt) and ITS (ITS1 at 54 nt) between Ligusticum chuanxiong and Cnidium officinale.

CONCLUSIONBased on homology analysis of two genes plastid matK and nuclear ITS, the origin of Chuanxiong from China and Japan ought to be identical, the scientific name Cnidium officinale of Japanese Chuanxiong should be changed to Ligusticum chuanxiong.

Amino Acid Sequence ; Base Sequence ; China ; Cnidium ; genetics ; DNA, Plant ; analysis ; DNA, Ribosomal Spacer ; genetics ; Endoribonucleases ; genetics ; Japan ; Ligusticum ; genetics ; Molecular Sequence Data ; Nucleotidyltransferases ; genetics ; Phylogeny ; RNA, Ribosomal, 18S ; genetics ; Sequence Analysis ; Sequence Homology ; Terminology as Topic

Mutations in the Fused in sarcoma/Translated in liposarcoma gene (FUS/TLS, FUS) have been identified among patients with amyotrophic lateral sclerosis (ALS). FUS protein aggregation is a major pathological hallmark of FUS proteinopathy, a group of neurodegenerative diseases characterized by FUS-immunoreactive inclusion bodies. We prepared transgenic Drosophila expressing either the wild type (Wt) or ALS-mutant human FUS protein (hFUS) using the UAS-Gal4 system. When expressing Wt, R524S or P525L mutant FUS in photoreceptors, mushroom bodies (MBs) or motor neurons (MNs), transgenic flies show age-dependent progressive neural damages, including axonal loss in MB neurons, morphological changes and functional impairment in MNs. The transgenic flies expressing the hFUS gene recapitulate key features of FUS proteinopathy, representing the first stable animal model for this group of devastating diseases.
Aged ; Aging ; genetics ; metabolism ; pathology ; Amyotrophic Lateral Sclerosis ; genetics ; metabolism ; pathology ; Animals ; Animals, Genetically Modified ; Disease Models, Animal ; Drosophila melanogaster ; genetics ; metabolism ; Gene Expression ; Humans ; Microscopy, Electron, Scanning ; Motor Neurons ; metabolism ; pathology ; Mushroom Bodies ; metabolism ; pathology ; Mutant Proteins ; genetics ; metabolism ; Mutation ; Photoreceptor Cells, Invertebrate ; metabolism ; pathology ; Plasmids ; RNA-Binding Protein FUS ; genetics ; metabolism ; Recombinant Fusion Proteins ; genetics ; metabolism ; Retinal Degeneration ; pathology ; physiopathology ; Transfection