Ohue T

References (3)

Title : Increase of fucosylated serum cholinesterase in relation to high risk groups for hepatocellular carcinomas - Ohkura_1994_Cancer.Res_54_55
Author(s) : Ohkura T , Hada T , Higashino K , Ohue T , Kochibe N , Koide N , Yamashita K
Ref : Cancer Research , 54 :55 , 1994
Abstract : Serum cholinesterase (ChE) (E.C. 3.1.1.8) is a glycoprotein which has 36 potential sites of asparagine-N-linked sugar chains. The structures of oligosaccharides released from ChE on hydrazinolysis were studied by serial lectin affinity column chromatography, exoglycosidase digestion, and methylation analysis. Seventy-three % of the sugar chains occurred as biantennary oligosaccharides and the remainder as C-2 and C-2,4/C-2,6 branched tri- and tetraantennary oligosaccharides. Several percentages of the Lewis X antigenic determinant and fucosylated mannose core were linked to them, and their sialic acid residues were linked to nonreducing terminal galactose residues at the C-3 and C-6 positions. Aleuria aurantia lectin-reactive ChE with the Lewis X antigenic determinant increased in hepatocellular carcinomas and liver cirrhosis compared with chronic hepatitis; on the other hand, Aleuria aurantia lectin-reactive ChE did not change significantly after transcatheter arterial embolization and was not related to the serum levels of alpha-fetoprotein and carcinoembryonic antigen in patients with hepatocellular carcinomas. Accordingly, the analysis of Aleuria aurantia lectin-reactive ChE is clinically useful for differentiating liver cirrhosis from chronic hepatitis and to identify high risk groups for hepatocellular carcinomas, i.e., cirrhotic patients in Child's A grade.
ESTHER : Ohkura_1994_Cancer.Res_54_55
PubMedSearch : Ohkura_1994_Cancer.Res_54_55
PubMedID: 8261462

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