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  • 1
    Electronic Resource
    Electronic Resource
    Purification and characterization of calmodulin-dependent multifunctional protein kinase from smooth muscle: isolation of caldesmon kinase (1990)
    s.l. : American Chemical Society
    Biochemistry 29 (1990), S. 11242-11248 
    Details
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1021/bi00503a013
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  • 2
    Electronic Resource
    Electronic Resource
    Veratridine-induced phosphorylation and activation of tyrosine hydroxylase, and synthesis of catecholamines in cultured bovine adrenal medullary cells (1989)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 339 (1989), S. 653-659 
    Details
    ISSN: 1432-1912
    Keywords: Adrenal medulla ; Catecholamine synthesis ; Protein kinase C ; Tyrosine hydroxylase ; Veratridine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The mechanism of the synthesis of catecholamines by veratridine was studied in cultured bovine adrenal medullary cells. (1) Veratridine increased the phosphorylation and activity of tyrosine hydroxylase as well as the synthesis of [14C]catecholamines from [14C]tyrosine, all of which were inhibited by tetrodotoxin. Veratridine-induced activation of tyrosine hydroxylase and synthesis of [14C]catecholamines were reduced in 20 mmol/l extracellular Na+ or in Ca2+-free medium. (2) 12-O-Tetradecanoylphorbol-13-acetate (TPA), an activator of protein kinase C, increased the synthesis of [14C]catecholamines. In the presence of TPA, veratridine did not produce any additional increase in [14C]catecholamine synthesis. In protein kinase C-deficient cells which were prepared by pretreatment with 1 μ ol/1 TPA for 24 h, TPA failed to increase [14C]catecholamine synthesis and veratridine-induced [14C]catecholamine synthesis was suppressed by 50%. (3) Polymyxin B, an inhibitor of protein kinase C and N-(6-aminohexyl)-5-chloro-l-naphthalenesulfonamide (W-7), an inhibitor of calmodulin, inhibited veratridine-stimulated synthesis of [14C]catecholamines as well as veratridine-induced influx of 22Na+ and 45Ca2+ with similar potencies. (4) In digitonin-permeabilized cells, polymyxin B attenuated the activation of tyrosine hydroxylase caused by Ca2+. These results suggest that veratridine-induced synthesis of catecholamines and activation of tyrosine hydroxylase were mediated by Ca2+-dependent phosphorylation of this enzyme, and protein kinase C may be responsible, at least in part, for this process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00168658
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  • 3
    Electronic Resource
    Electronic Resource
    Ancient Origin of the Null Allele se 428 of the Human ABO-Secretor Locus (FUT2) (2000)
    Springer
    Journal of molecular evolution 50 (2000), S. 243-248 
    Details
    ISSN: 1432-1432
    Keywords: Key words:FUT2 gene — Secretor gene —α(1,2)Fucosyltransferase — Old polymorphism — Balancing selection — Neutrality test
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract. In human populations, a null allele having several nucleotide differences from the wild-type allele is segregating at the FUT2 locus (the ABO-Secretor locus) encoding α(1,2)fucosyltransferase. To estimate the age of the most recent common ancestor (MRCA) of these two alleles, we sequenced FUT2 homologues from chimpanzee, gorilla, orangutan, and green monkey. Since we did not detect acceleration or any heterogeneity in the substitution rate at this locus among these species, the age of the MRCA was estimated to be around 3 MYA, assuming the divergence time of human and chimpanzee to be 5 MYA. We developed a simple test to examine whether or not the old age of the MRCA of the FUT2 is consistent with that expected for two divergent neutral alleles sampled from a random mating population. An application of the test to the data at FUT2 indicated that the age of the MRCA is too old to be explained by the simple neutral assumptions, although our test depends on accurate estimation of the divergence time of human and chimpanzee in units of twice the human population size. Various possibilities including balancing selection are discussed to explain this old age of the MRCA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002399910028
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  • 4
    Electronic Resource
    Electronic Resource
    Extensive polymorphism of the FUT2 gene in an African (Xhosa) population of South Africa (1998)
    Springer
    Human genetics 〈Berlin〉 103 (1998), S. 204-210 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The human secretor type α(1,2)fucosyltrans-ferase gene (FUT2) polymorphism was investigated in Xhosa and Caucasian populations of South Africa by polymerase chain reaction–restriction fragment length polymorphism and DNA sequencing. Six new base substitutions were found in the coding region of FUT2. A single base (C) deletion at nucleotide 778, which led to a frame shift and produced a stop codon at codon 275, was responsible for the enzyme inactivation. Three nonsynonymous base substitutions, A40G (Ile14Val), C379T (Arg127Cys), and G481A (Asp161Asn), and two synonymous base substitutions, A375G (Glu125) and C480T (His160), were also identified in functional alleles. As a result, seven new alleles, Se 40 , Se 481 , Se 40,481 , Se 357,480 , Se 357,379,480 , Se 375 , and se 357,480,778 were identified. Population studies revealed that an allele containing a nonsense mutation G428A (Trp143stop) (se 428 ) was the common null allele in both Xhosa and Caucasian populations, whereas an allele containing a missense A385T (Ile129Phe) mutation (se 357,385 ), which is the common null allele in Orientals, was found to be absent from both populations. The heterozygosity rates of FUT2 genotypes were as high as 0.75 in the Xhosa population and 0.65 in the Caucasian population. Therefore, the extensive polymorphism and race specificity of the FUT2 gene make it suitable for application as a new tool in genetic studies of modern human evolutionary history.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050808
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  • 5
    Electronic Resource
    Electronic Resource
    Five novel missense mutations of the Lewis gene (FUT3) in African (Xhosa) and Caucasian populations in South Africa (1998)
    Springer
    Human genetics 〈Berlin〉 102 (1998), S. 675-680 
    Details
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Five novel missense mutations, viz., C304 A, T370 G, G484 A, G667 A, and G808 A, in the Lewis gene (FUT3) were detected in African (Xhosa) and Caucasian individuals in South Africa. These single base substitutions may result in changes in amino acid residues from Gln102 to Lys in the 304 mutation, Ser124 to Ala in the 370 mutation, Asp162 to Asn in the 484 mutation, Gly223 to Arg in the 667 mutation, and Val270 to Met in the 808 mutation. Out of the five novel mutations identified in this investigation, four new alleles (le 484,667 , le 484,667,808 , Le 304 , and Le 370 ) were determined in the Xhosa population and two new alleles (le 202,314,484 and Le 304 ) in the Caucasian population. The determination of α(1,3/1,4)fucosyltransferase activity, after transfection of plasmids containing the new alleles into COS7 cells, suggested that alleles le 484,667 and le 484,667,808 encoded an inactive enzyme, and that alleles Le 304 and Le 370 encoded a functional enzyme. In addition, we also examined the incidence of five common alleles, Le 59 , le 59,508 , le 59,1067 , le 202,314 , and le 1067 in two populations by the polymerase chain reaction/restriction fragment length polymorphism method and compared differences in the allele frequencies of FUT3 among three ethnic groups (Orientals, Africans, and Caucasians).
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004390050760
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  • 6
    Electronic Resource
    Electronic Resource
    Veratridine causes the Ca2+-dependent increase in diacylglycerol formation and translocation of protein kinase C to membranes in cultured bovine adrenal medullary cells (1992)
    Springer
    Naunyn-Schmiedeberg's archives of pharmacology 346 (1992), S. 76-81 
    Details
    ISSN: 1432-1912
    Keywords: Amiloride ; Calcium ; Diacylglycerol ; Protein kinase C ; Veratridine
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Our previous studies suggested that protein kinase C is involved in the veratridine (an activator of voltage-dependent Na+ channels)-induced phosphorylation and activation of tyrosine hydroxylase as well as the synthesis of catecholamines in adrenal medulla (Uezono et al. 1989). In the present study, we investigated whether treatment of cultured bovine adrenal medullary cells with veratridine causes the accumulation of diacylglycerol, a physiological activator of protein kinase C and the translocation of protein kinase C from cytosol to membrane, a process required for protein kinase C activation. Veratridine (100 μmol/l) increased diacylglycerol level about 2.2 fold in a monophasic manner, with peaking at 5 min and declining toward the basal level within 20 min. Veratridine also increased membrane protein kinase C from 15.6% to 26.9% of total protein kinase C in a timecourse similar to that of diacylglycerol accumulation. Both stimulatory effects of veratridine were inhibited by tetrodotoxin and not observed in Ca2+-free, EGTA-containing medium. Amiloride, an inhibitor of Na+/Ca2+ and Na+/H+ exchange, did not alter veratridine-induced events. These results suggest that veratridine-induced Ca2+ influx contributes to the accumulation of diacylglycerol and the activation of protein kinase C in adrenal medullary cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00167574
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  • 7
    Electronic Resource
    Electronic Resource
    Significance of each of three missense mutations, G484A, G667A, and G808A, present in an inactive allele of the human Lewis gene (FUT3) for α(1,3/1,4)fucosyltransferase inactivation (1998)
    Springer
    Glycoconjugate journal 15 (1998), S. 961-967 
    Details
    ISSN: 1573-4986
    Keywords: α(1,3/1,4)fucosyltransferase ; Fuc-TIII ; Lewis-negative allele ; Chimera ; Mutation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Recently, we found three novel missense mutations, G484A (Asp162Asn), G667A (Gly223Arg), and G808A (Val270Met), present in a Lewis-negative allele (le484,667,808) from an African (Xhosa) population. To define the relative contribution of each of the three mutations in the le484,667,808 allele for inactivation of the FUT3-encoded enzyme, we made chimeric FUT3 containing each of the three mutations. A transient expression study indicated that COS7 cells transfected with the FUT3 construct containing the G484A mutation expressed the Lewis antigen and had about 20% enzyme activity as compared with COS7 cells transfected with the wild type FUT3 allele, whereas COS7 cells transfected with the FUT3 construct containing either the G667A mutation or the G808A mutation did not express the Lewis antigen and showed no detectable α(1,3/1,4)fucosyltransferase activity. These results suggest that the G667A and/or the G808A missense mutations of FUT3 alleles are responsible for the inactivation of the FUT3-encoded enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1006981724233
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  • 8
    Electronic Resource
    Electronic Resource
    The Fusion Gene at the ABO-Secretor Locus (FUT2): absence in Chinese populations (1999)
    Springer
    Journal of human genetics 44 (1999), S. 181-184 
    Details
    ISSN: 1435-232X
    Keywords: Key words ABO ; Secretor ; FUT2 ; Fusion gene ; Japanese
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract The fusion gene (se fus ) is a null allele of the secretor type α (1, 2) fucosyltransferase gene (FUT2) and was first found in a Japanese population. It has not yet been reported in any other ethnic population. In the present study, we investigated the distribution of the fusion gene of the FUT2 locus in five populations from three ethnic groups in East Asia. The fusion gene was found in two additional Japanese populations with a high frequency (0.0551 in Okinawa and 0.0792 in Akita) and, for the first time outside Japan, in a Korean population, at a very low frequency (0.0063 in Seoul). In contrast, we found no fusion gene in two Chinese populations. These findings showed that the FUT2 fusion gene was ubiquitous in Japanese, but was rare in neighboring populations, suggesting that the FUT2 fusion gene had emerged from within the Japanese. Additionally, a new null allele with a C-to-T substitution at nucleotide 658 was found in one individual native of southern China.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s100380050138
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