ABSTRACT
Background & Objective: The calcitonin gene-related peptide (CGRP) has a central role in the pathogenesis of migraine, but variations in CGRP-related genes, including the calcitonin gene-related polypeptide-alpha (CALCA) gene and the receptor activity modifying 1 (RAMP1) gene, have not been found to link with migraine in Australian population. The goals of this study were to determine whether variants in the two genes are related to migraine in Chinese population. Methods: Using a case-control approach, rs3781719 and rs145837941 in the CALCA gene and rs3754701 and rs7590387 at the RAMP1 locus was analyzed in a cohort of 504 migraine cases and 529 ethnically matched controls. Genotyping was performed using Sequenom MALDI-TOF mass spectrometry iPLEX platform. Results: The CALCA gene rs145837941 variant was not found in migraine or control group. No significant difference in genotypic and allelic distribution was observed in the other three polymorphisms between migraine cases and controls. All the three SNPs were also not selected as significant factors that independently contributed to susceptibility to migraine in multivariate analysis. In the subgroup analysis, the CALCA rs3781719 seemed to be a significant risk for migraine with aura, but was not statistically significant after FDR correction. Moreover, there was no synergistic relationship between the three SNPs in the multifactor dimensionality reduction analysis for explore locus–locus interactions. Conclusion: Our data suggested that variants in CALCA gene and RAMP1 gene were not associated with migraine in the Han-Chinese population.
Subject(s)
Calcitonin Gene-Related Peptide , Migraine DisordersABSTRACT
A fragment of chalcone synthase gene (SmCHS) was cloned from the cDNA library constructed in Saussurea medusa. The full-length cDNA sequence of SmCHS was obtained by RT-PCR. Sequence analysis showed that the full length of SmCHS was 1313 bp, containing an open reading frame (1170 bp) encoding 389 amino acids. The molecular weight of the protein was estimated to be 43 kDa. The prokaryotic expression plasmids pET28a(+)-SmCHS was constructed and transformed into Escherichia coli BL21(DE3) for expression. SDS-PAGE indicated that the fusion protein was expressed partially in soluble form after induction by IPTG. The recombinant protein was collected and purified by Ni-NTA affinity column. The enzymatic activity assay of the purified recombinant protein showed that the fusion protein had chalcone synthase activity. It could catalyze the condensation of a 4-coumaroyl-CoA with three malonyl-CoAs to produce naringenin chalcone.