Muratani K

References (3)

Title : [Gene analysis of human cholinesterase variants]. - Muratani_1993_Japanese.J.Clin.Med_51_495
Author(s) : Muratani K , Hada T , Higashino K
Ref : Nippon Rinsho Japanese Journal of Clinical Medicine , 51 :495 , 1993
Abstract : People with genetic variants of cholinesterase (ChE) have been reported to have prolonged apnea with the use of myorelaxant succinylcholine. For the silent type variant ChE, two cases of mutation have been reported. In one case, the exon 2 of ChE gene was disrupted by a 342 bp insertion of Alu element. In the other case, a frame shift mutation was identified at Gly-117 (GGT-->GGAG) to create a stop codon at nucleotide 384. Dibucaine resistant ChE was examined and found to have a point mutation at nucleotide 209 (A-->G) that converted Asp-70 to Gly, and consequently reduced the affinity of ChE for choline esters. In addition, another two types of a point mutation reducing ChE activity were reported on K variant (Ala-539-->Thr) and a case of (Gly-365-->Arg) in a patient with liver cirrhosis.
ESTHER : Muratani_1993_Japanese.J.Clin.Med_51_495
PubMedSearch : Muratani_1993_Japanese.J.Clin.Med_51_495
PubMedID: 8464162

Title : A variant serum cholinesterase and a confirmed point mutation at Gly-365 to Arg found in a patient with liver cirrhosis - Hada_1992_Intern.Med_31_357
Author(s) : Hada T , Muratani K , Ohue T , Imanishi H , Moriwaki Y , Itoh M , Amuro Y , Higashino K
Ref : Intern Med , 31 :357 , 1992
Abstract : A 64-year-old man was admitted to our hospital because of possible liver cirrhosis. His serum cholinesterase was anomalously low with a delta pH of 0.1 (normal range; 0.8-1.1). His enzyme was more heat-labile than the normal controls. Km value of his enzyme for benzoylcholine was 1.1 x 10(-5) mol/l, while that for normal controls was 2.3 x 10(-6) mol/l. In addition, isozymic alteration of his enzyme was observed. Sequencing of the white blood cell DNA of the patient showed a point mutation at nucleotide 1093 (GGA to CGA), which changes codon 365 from glycine to arginine.
ESTHER : Hada_1992_Intern.Med_31_357
PubMedSearch : Hada_1992_Intern.Med_31_357
PubMedID: 1611188

Title : Inactivation of the cholinesterase gene by Alu insertion: possible mechanism for human gene transposition - Muratani_1991_Proc.Natl.Acad.Sci.U.S.A_88_11315
Author(s) : Muratani K , Hada T , Yamamoto Y , Kaneko T , Shigeto Y , Ohue T , Furuyama J , Higashino K
Ref : Proc Natl Acad Sci U S A , 88 :11315 , 1991
Abstract : The human cholinesterase (ChE) gene from a patient with acholinesterasemia was cloned and analyzed. By using ChE cDNA as a probe, four independent clones were isolated from a genomic library constructed from the patient's DNA. Sequencing analysis of all of the four clones revealed that exon 2 of the ChE gene was disrupted by a 342-base-pair (bp) insertion of Alu element, including a poly(A) tract of 38 bp, which showed 93% sequence homology with a current type of human Alu consensus sequence. Southern blot analysis showed that the Alu insertion occurred in both alleles of the patient and was inherited in the patient's family. This Alu insertion was flanked by 15-bp of target site duplication in exon 2 corresponding to positions 1062-1076 of ChE cDNA, indicating that an Alu element could have been integrated by retrotransposition. Thus, this case provides an important clue to the mechanism of inactivation of a gene by integration of a retrotransposon.
ESTHER : Muratani_1991_Proc.Natl.Acad.Sci.U.S.A_88_11315
PubMedSearch : Muratani_1991_Proc.Natl.Acad.Sci.U.S.A_88_11315
PubMedID: 1662391