Ma YM

References (2)

Title : Lipopolysaccharide increased the acute toxicity of the Rhizoma coptidis extract in mice by increasing the systemic exposure to Rhizoma coptidis alkaloids - Ma_2011_J.Ethnopharmacol_138_169
Author(s) : Ma BL , Ma YM , Gao CL , Wu JS , Qiu FR , Wang CH , Wang XH
Ref : J Ethnopharmacol , 138 :169 , 2011
Abstract : ETHNOPHARMACOLOGICAL RELEVANCE: Rhizoma coptidis is used as an antidysenteric in clinics in China. However, patients suffering from dysentery are susceptible to the acute toxicity of Rhizoma coptidis. The current study investigates the effects of lipopolysaccharide (LPS), which are a key pathogenic factor in dysentery, on the acute toxicity of a Rhizoma coptidis extract in mice; possible mechanisms are proposed. MATERIALS AND METHODS: Acute toxicity and pharmacokinetic experiments in mice were conducted. The plasma concentration of Rhizoma coptidis alkaloids in mice was determined using liquid chromatography/tandem mass spectrometry. The activity of acetylcholinesterase (AChE) in the tissue homogenate was determined using an AChE determination kit. RESULTS: Pretreatment with LPS for 16 h increased the acute toxicity of the oral Rhizoma coptidis extract. Systemic exposure to Rhizoma coptidis alkaloids was also increased by LPS pretreatment. Neostigmine significantly increased whereas pyraloxime methylchloride reduced the acute toxicity of the Rhizoma coptidis extract. LPS pretreatment alone showed no significant effect on the activity of thoracoabdominal diaphragm AChE. However, it enhanced the inhibitory effect of the Rhizoma coptidis extract. LPS pretreatment did not affect the acute toxicity of various dosages of tail vein-injected berberine. CONCLUSIONS: LPS increased the acute toxicity of the oral Rhizoma coptidis extract in mice by increasing the systemic exposure to the Rhizoma coptidis alkaloids.
ESTHER : Ma_2011_J.Ethnopharmacol_138_169
PubMedSearch : Ma_2011_J.Ethnopharmacol_138_169
PubMedID: 21924335

Title : Cloning and expression of a novel retinoblastoma binding protein cDNA, RBBP10 - Chen_2002_Biochem.Genet_40_273
Author(s) : Chen JZ , Yang QS , Wang S , Meng XF , Ying K , Xie Y , Ma YM
Ref : Biochemical Genetics , 40 :273 , 2002
Abstract : A 2860-bp cDNA was isolated from a human fetal brain cDNA library by high throughput cDNA sequencing, which encodes a putative protein with 186 amino acids. The putative protein shares 90.7% identity with rat pBOG (3403163) and shares 93.4% identity with human RBBP9 (NP_006597.1). A conserved RB binding domain, L x C x E, located between residue 63 and 68 was recognized. Therefore, it was named RBBP10. Mapviewer analysis locates it on human chromosome 20q11.22. RBBP10 spans about 9.6 kb of the genome and consists of six exons and five introns. RT-PCR revealed that the gene was expressed widely in various human tissues, and the expression level is somewhat higher in tumor tissues than in normal tissues. But subsequent sequencing analysis did notfound any mutation of this in tumor tissues. The COS 7 cell transfected with the ORF of RBBP10 showed that the protein was distributed both in the cytoplasm and in the nucleus. Our results suggest that RBBP10 is the orthologue of the rat BOG gene (AF025819) and a paralogue of human RBBP9 (AF039564).
ESTHER : Chen_2002_Biochem.Genet_40_273
PubMedSearch : Chen_2002_Biochem.Genet_40_273
PubMedID: 12296629
Gene_locus related to this paper: human-RBBP9