Kanno T

References (10)

Title : 2,3-Butandione 2-monoxime inhibits skeletal myosin II by accelerating ATP cleavage - Komatsu_2017_Biochem.Biophys.Res.Commun_490_849
Author(s) : Komatsu H , Koseki Y , Kanno T , Aoki S , Kodama T
Ref : Biochemical & Biophysical Research Communications , 490 :849 , 2017
Abstract : 2,3-Butandione 2-monoxime (BDM) is a widely used myosin inhibitor with an unclear mode of action. In this report, we investigated the mechanism of BDM oxime group nucleophilic reactivity on the phosphoester bond of ATP. BDM increased the ATPase activity of skeletal myosin subfragment 1 (S1) under conditions in which ATP cleavage is the rate-limiting step (K(+), EDTA-ATPase activity of native S1 and Mg(2+)-ATPase activity of trinitrophenylated S1 and partially unfolded S1). Furthermore, the effect of BDM on the S1-bound adenosine 5'-(beta,gamma-imido) triphosphate (AMPPNP) (31)P NMR spectrum suggests that BDM changes the microenvironment around the phosphorus atoms of myosin-bound nucleotide. A computational search for the BDM-binding site in the adenosine 5'-[gamma-thio] triphosphate (myosin-ATPgammaS) complex predicted that BDM is located adjacent to the nucleotide on myosin. Therefore, we propose that the BDM oxime group catalytically assists in ATP cleavage, thereby enhancing the ATPase activity of myosin in a manner analogous to pralidoxime-mediated reactivation of organophosphate-inactivated acetylcholinesterase. This is the first study suggesting that oxime provides catalytic assistance for ATP cleavage by an ATP-hydrolyzing enzyme.
ESTHER : Komatsu_2017_Biochem.Biophys.Res.Commun_490_849
PubMedSearch : Komatsu_2017_Biochem.Biophys.Res.Commun_490_849
PubMedID: 28648599

Title : [Investigative application of a laboratory database] - Kanno_2000_Rinsho.Byori__21
Author(s) : Kanno T
Ref : Rinsho Byori , :21 , 2000
Abstract : An end user computing system (EUC) is usually part of the laboratory information system. Effective use of this EUC system is described in this article. The first application of this system is for monitoring the turn-around time (TAT) of laboratory work flow. Precise time sequential data were analyzed using this end user computing system. Weekly fluctuations of TAT depended on the cyclic changes in requisition numbers of test samples. Another application of EUC was phenotype screening of genetic abnormalities. Screenings from high triglyceride and low HDL cholesterol were effective for the phenotype screening for genetic lipoprotein lipase abnormalities, and phenotype screening from high albumin cholinesterase ratio was effective for genetic abnormalities causing silent cholinesterase. Investigational application of EUC was demonstrated in two areas of laboratory research.
ESTHER : Kanno_2000_Rinsho.Byori__21
PubMedSearch : Kanno_2000_Rinsho.Byori__21
PubMedID: 11215171

Title : [Evaluation of screening methods for cholinesterase variants from daily laboratory data] - Feng_1999_Rinsho.Byori_47_749
Author(s) : Feng Y , Dey DC , Kondo A , Yonekawa O , Kanno T
Ref : Rinsho Byori , 47 :749 , 1999
Abstract : The genetic variants of the cholinesterase (ChE) are frequently misdiagnosed as a liver dysfunction. We compared three extraction methods for screening of ChE abnormalities. Employing these three methods, total 31 cases were found to be genetic abnormalities from 2985 patients of Hamamatsu University Hospital. We picked up 11 of candidates with low enzyme activities less than 100U/l as group 1 using the first method and effectively detected 9 cases (82%) with genetic abnormalities. The second extraction method was based on the ratio between Albumin (Alb) and ChE and subsequently, 48 of high risk patients were picked up as group 2 and 28 cases (58%) showed genetic abnormalities. Furthermore, all cases of group 1 were contained in the second group. The third method was based on the discrimination function from Alb and total cholesterol (TC) as group 3 and 32 cases were picked up. Fourteen cases (44%) out of them showed the genetic abnormalities using this method, and surprisingly, 13 cases (93%) of them were estimated to be K-variant. Although the three methods showed the different characteristics to extract genetic abnormalities of ChE, the second extraction method could pick up the largest population with genetic abnormalities. Further phenotypic extraction methods should be compared to understand the relationship between phenotype and genotype.
ESTHER : Feng_1999_Rinsho.Byori_47_749
PubMedSearch : Feng_1999_Rinsho.Byori_47_749
PubMedID: 10511807

Title : [The application of end user computing (EUC) for detection of lipoprotein lipase gene abnormality] - Li_1999_Rinsho.Byori_47_737
Author(s) : Li J , Kobori K , Kondo A , Yonekawa O , Kanno T
Ref : Rinsho Byori , 47 :737 , 1999
Abstract : Lipoprotein lipase (LPL) is an enzyme digesting lipoprotein triglyceride (TG) in peripheral blood vessels. Most patients with LPL deficiency show very high plasma TG and low HDL-C. To establish an effective computer-based screening system to identify individuals with genetic LPL disorders, we selected 50 subjects whose plasma TG was over 350mg/dl and HDL-C was lower than 35mg/dl from patients at Hamamatsu University Hospital. We applied End User Computing (EUC) of our laboratory system to select high risk subjects with LPL gene abnormalities. Polymerase chain reaction (PCR) products from LPL gene exons 2-9 were screened by single-strand conformation polymorphism (SSCP), direct DNA sequence analysis and restriction fragment length polymorphism (RFLP). We found a novel missense mutation (1223C-->G, S323C) in LPL gene exon 7 from three subjects. By PCR-mediated site-directed mutagenesis and restriction digestion, the three subjects were found to be heterozygous. In addition, we identified two other common mutations in Japanese employing the RFLP method. One was the 1595C-->G (S447X) in exon 9 from six subjects, two homozygous and four heterozygous individuals. The other was a mutation of intron 3 (C-->T transition) from four heterozygous subjects. Using EUC screening method, we detected genetic LPL abnormalities more easily. The frequency of the LPL gene mutation in the 50 high-risk subjects was 26%, and was estimated to be one out of 2,000 patients at our clinic. Using the EUC system to screen for LPL mutations was established to be an effective computer-based screening system to identify individuals with genetic abnormalities.
ESTHER : Li_1999_Rinsho.Byori_47_737
PubMedSearch : Li_1999_Rinsho.Byori_47_737
PubMedID: 10511805

Title : Butyrylcholinesterase genes in individuals with abnormal inhibition numbers and with trace activity: one common mutation and two novel silent genes - Dey_1998_Ann.Clin.Biochem_35_302
Author(s) : Dey DC , Maekawa M , Sudo K , Kanno T
Ref : Annals of Clinical Biochemistry , 35 :302 , 1998
Abstract : A random population was screened for abnormal dibucaine and fluoride numbers (DN & FN) to find some common mutations in butyrylcholinesterase (BCHE) gene. Of 2375 unrelated individuals, 10 were found to have low DN and FN and were selected for further studies. DNA analysis of these hypocholinesterasemics revealed that seven patients were heterozygous for missense mutation at codon 330 (TTA to ATA; BCHE*330I). The frequency of BCHE*330I mutation was calculated to be at least 0.29% among the Japanese. On the other hand, two novel mutations were found in three families and two individuals including probands whose enzyme activity was very low (silent gene). Polymerase chain reaction and single stranded conformation polymorphism (PCR-SSCP) and restriction fragment length polymorphism (PCR-RFLP) were used for identification of the common and known mutation types such as BCHE*250P (ACT to CCT), BCHE*365R (GGA to CGA), and BCHE*539T (GCA to ACA; K-polymorphism), whereas PCR-SSCP was used in combination with direct DNA sequencing for new mutations like BCHE*446V (TTT to GTT) and BCHE*451X (GAA to TAA).
ESTHER : Dey_1998_Ann.Clin.Biochem_35_302
PubMedSearch : Dey_1998_Ann.Clin.Biochem_35_302
PubMedID: 9547905
Gene_locus related to this paper: human-BCHE

Title : Genetic mutations of butyrylcholine esterase identified from phenotypic abnormalities in Japan - Maekawa_1997_Clin.Chem_43_924
Author(s) : Maekawa M , Sudo K , Dey DC , Ishikawa J , Izumi M , Kotani K , Kanno T
Ref : Clinical Chemistry , 43 :924 , 1997
Abstract : We have identified 12 kinds of genetic mutations of butyrylcholine esterase (BCHE) from phenotypic abnormalities, showing that BCHE activities were deficient or diminished in sera. These genetic mutations, detected by PCR-single-strand conformation polymorphism analysis and direct sequencing, consisted of one deletion (BCHE*FS4), nine missense (BCHE*24 M, *1005, *250P, *267R, *330I, *365R, *418S, *515C, *539T), and two nonsense mutations (BCHE*119STOP, *465STOP). All of the individuals deficient in serum BCHE activity were homozygous for silent genes (6 of 6). Fifty-eight percent of the individuals (31 of 53) with slightly reduced serum BCHE activity were heterozygous for silent genes. They also showed a higher frequency (47% as allele frequency) of the K-variant than the general population (17.5%). Finally, we confirmed low serum BCHE activity in 10 of 23 individuals heterozygous for silent genes.
ESTHER : Maekawa_1997_Clin.Chem_43_924
PubMedSearch : Maekawa_1997_Clin.Chem_43_924
PubMedID: 9191541

Title : Three different point mutations in the butyrylcholinesterase gene of three Japanese subjects with a silent phenotype: possible Japanese type alleles - Sudo_1996_Clin.Biochem_29_165
Author(s) : Sudo K , Maekawa M , Kanno T , Akizuki S , Magara T
Ref : Clinical Biochemistry , 29 :165 , 1996
Abstract : OBJECTIVE: To investigate genetic mutations in three Japanese subjects homozygous for silent butyrylcholinesterase mutations. METHODS AND RESULTS: One of them was compound heterozygous for two mutations; GGA(Gly) to CGA(Arg) at codon 365 (G365R) and CAA(Gln) to TAA(Ter) at codon 119 (Q119X). The other two subjects were homozygous for different missense mutations: CGT(Arg) to TGT(Cys) at codon 515 (R515C) and G365R, respectively. Simple identification methods for all of the mutations were developed and applied for family analysis and to control individuals. Two mutations, G365R and R515C, have been reported in the Japanese population, while the nonsense mutation Q119X was discovered in the present study. Genetic heterogeneity between human populations with regard to the butyrylcholinesterase gene was suggested.
CONCLUSIONS: Among the three mutations found in this investigation, one was novel, and none of these mutations have been reported outside Japan.
ESTHER : Sudo_1996_Clin.Biochem_29_165
PubMedSearch : Sudo_1996_Clin.Biochem_29_165
PubMedID: 8601326

Title : [Clinical significance of serum cholinesterase concentrations determined by enzyme-linked immunosorbent assay (ELISA)]. [Japanese] - Kotani_1996_Rinsho.Byori.Japanese.J.Clin.Pathol_44_965
Author(s) : Kotani K , Maekawa M , Hara K , Kanno T
Ref : Rinsho Byori Japanese Journal of Clinical Pathology , 44 :965 , 1996
Abstract : We developed a sensitive enzyme-linked immunosorbent assay (ELISA) for measurement of the protein mass of serum cholinesterase (CHE). In our ELISA system, a combination of a monoclonal antibody (a capture antibody) and an anti-CHE rabbit antibody (a second antibody) against CHE were used for the specific determination of CHE. The formed antigen-antibody complexes were detected with an alkaline phosphatase-labeled anti-rabbit IgG antibody. Using this ELISA system, we investigated for a possible relationship between the protein mass value and the catalytic activity of serum CHE in three patients groups with different clinical findings: control subjects selected randomly from outpatients (Group A), individuals with a low serum CHE activity including genetic variants (Group B) and patients with sarin poisoning (Group C). The CHE mass value correlated closely with the CHE activity in Group A, as previously reported. In Group B, a less significant correlation than in Group A was observed because both the CHE mass value and the CHE activity were disturbed at relatively lower levels. However, no discrepant cases were observed. On the other hand, in Group C, patients with serious sarin poisoning showed significant discrepancies between the mass value and activity of CHE before medical treatments, indicating that the inhalation of sarin did not affect the protein mass level but did affect the activity of serum CHE. As the patients recovered during the treatments, their CHE activities increased to the levels expected from the regression curve obtained with Group A, whereas the mass values were almost unchanged. In conclusion, protein mass determination of serum CHE provides valuable information concerning the target value of the serum CHE activity for the treatment of patients with organophosphate insecticide poisoning as well as for investigating the specific activity of genetic variants of serum CHE.
ESTHER : Kotani_1996_Rinsho.Byori.Japanese.J.Clin.Pathol_44_965
PubMedSearch : Kotani_1996_Rinsho.Byori.Japanese.J.Clin.Pathol_44_965
PubMedID: 97091514

Title : Genetic basis of the silent phenotype of serum butyrylcholinesterase in three compound heterozygotes - Maekawa_1995_Clin.Chim.Acta_235_41
Author(s) : Maekawa M , Sudo K , Kanno T , Kotani K , Dey DC , Ishikawa J , Izumi M , Etoh K
Ref : Clinica Chimica Acta , 235 :41 , 1995
Abstract : Three Japanese patients showed very low butyrylcholinesterase activity in their sera and appeared to be homozygous for silent genes for butyrylcholinesterase. From DNA analysis, all three patients were compound heterozygotes: GGA(Gly) to CGA(Arg) at codon 365 (G365R) and TTC(Phe) to TCC(Ser) at codon 418 (F418S) in patient 1, G365R and CGT(Arg) to TGT(Cys) at codon 515 (R515C) in patient 2 and ACT(Thr) to CCT(Pro) at codon 250 (T250P) and AGA(Arg) to TGA(Stop) at codon 465 (R465X) in patient 3. The K-variant, GCA(Ala) to ACA(Thr) at codon 539, was also found in patients 1 and 2. Simple identification methods for all the mutations were developed and applied to family analysis and control individuals. The mutant alleles (with silent gene and K-variant) were segregated as predicted by theory in pedigrees of patients 1 and 2. Four of the mutations, F418S, R515C, T250P and R465X, were initially discovered in Japan and genetic heterogeneity among the human population for the butyrylcholinesterase gene was suggested.
ESTHER : Maekawa_1995_Clin.Chim.Acta_235_41
PubMedSearch : Maekawa_1995_Clin.Chim.Acta_235_41
PubMedID: 7634491

Title : Butyrylcholinesterase K-variant in Japan: frequency of allele and associated enzyme activity in serum [letter] -
Author(s) : Izumi M , Maekawa M , Kanno T
Ref : Clinical Chemistry , 40 :1606 , 1994
PubMedID: 8045015