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Shinji Satomura - One of the best experts on this subject based on the ideXlab platform.

  • high sensitivity Lens Culinaris agglutinin reactive alpha fetoprotein assay predicts early detection of hepatocellular carcinoma
    Journal of Gastroenterology, 2014
    Co-Authors: Takashi Kumada, Hidenori Toyoda, Toshifumi Tada, Seiki Kiriyama, Makoto Tanikawa, Yasuhiro Hisanaga, Akira Kanamori, Junko Tanaka, Chiaki Kagebayashi, Shinji Satomura
    Abstract:

    Prognosis of patients with hepatocellular carcinoma (HCC) remains poor because HCC is frequently diagnosed late. Therefore, regular surveillance has been recommended to detect HCC at the early stage when curative treatments can be applied. HCC biomarkers, including Lens Culinaris agglutinin-reactive fraction of alpha-fetoprotein (AFP-L3), are widely used for surveillance in Japan. A newly developed immunoassay system measures AFP-L3 % with high sensitivity. This retrospective study aimed to evaluate clinical utility of high-sensitivity AFP-L3 (hs-AFP-L3) as a predictor of early stage HCC in surveillance at a single site. Of consecutive 2830 patients in the surveillance between 2000 and 2009, 104 HCC-developed and 104 non-HCC patients were selected by eligibility criteria and propensity score matching. Samples were obtained from the HCC patients who had blood drawn annually for 3 years prior to HCC diagnosis. In the present study, hs-AFP-L3 was elevated 1 year prior to diagnosis in 34.3 % of patients. The survival rate of patients with the hs-AFP-L3 ≥ 7 % at 1 year prior to diagnosis was significantly lower than that of patients with hs-AFP-L3 < 7 %. Elevation of hs-AFP-L3 was early predictive of development of HCC even at low AFP levels and in absence of ultrasound findings of suspicious HCC. The hs-AFP-L3 should be added to surveillance programs with US because elevated hs-AFP-L3 may be a trigger to perform enhanced imaging modalities for confirmation of HCC.

  • Lens Culinaris agglutinin a reactive alpha fetoprotein as a marker for liver atrophy in fulminant hepatic failure
    Hepatology Research, 2003
    Co-Authors: Toshiharu Sakurai, Hiroyuki Marusawa, Shinji Satomura, Motoshige Nabeshima, Shinji Uemoto, Koichi Tanaka, Tsutomu Chiba
    Abstract:

    Liver atrophy is frequently found at autopsy of patients with fulminant hepatic failure (FHF). Imaging studies in patients with FHF demonstrate that estimation of total liver volume correlates with prognosis. In this study, in order to determine serum markers for evaluating liver atrophy, we measured the weight of whole livers resected from 31 transplant recipients with FHF, and assessed the relation between the liver weights and several prognostic markers. The level of liver atrophy was evaluated by calculating the ratio of the removed whole liver weight to the body weight of each recipient, and 16 major variables including several serological markers were analyzed among those recipients. We found that the serum Lens Culinaris agglutinin-A-reactive alpha-fetoprotein (AFP-L3) levels were significantly higher in patients with FHF than in those with other liver diseases. In FHF patients, the serum AFP-L3 level at the onset of encephalopathy was significantly higher in cases with mild atrophy than in those with severe atrophy (P<0.05). Notably, the residual liver volume was significantly correlated with the serum AFP-L3 level (Pearson's correlation coefficient=0.63), but not with AFP. In conclusion, AFP-L3 is a possible serum marker for evaluating liver atrophy and/or liver regeneration in patients with FHF.

  • clinical utility of Lens Culinaris agglutinin reactive alpha fetoprotein in small hepatocellular carcinoma special reference to imaging diagnosis
    Journal of Hepatology, 1999
    Co-Authors: Takashi Kumada, Seiki Kiriyama, Satoshi Nakano, Isao Takeda, Yasuhiro Sone, Kazuhiko Hayashi, Hiromasa Katoh, Tomonori Endoh, Toshi Sassa, Shinji Satomura
    Abstract:

    Abstract Background/Aims: Blood concentration levels of alpha-fetoprotein like the Lens Culinaris agglutinin-reactive fraction (AFP-L3) are a useful marker for predicting the long-term prognosis of hepatocellular carcinoma. This study investigated the relationship between serum AFP-L3 and various imaging modalities. Methods: Sixty-three patients with small hepatocellular carcinomas ≤2 cm in diameter were studied. Serum AFP-L3 concentrations were measured by lectin-affinity electrophoresis coupled with antibody-affinity blotting and expressed as % AFP-L3 (the percent of AFP-L3 as total AFP). A clinical "cutoff level" of 10% was used in this study to indicate the presence of hepatocellular carcinoma. Selective hepatic intraarterial digital subtraction angiography (DSA), ultrasonographic angiography with carbon dioxide microbubbles (USAG), and computed tomography during arterial portography (CTAP) were performed to evaluate the hemodynamics of hepatic nodules. Results: Fourteen (22.2%) of the 63 patients were positive for % AFP-L3. The % AFP-L3 levels ( n =45, 4.4%) of patients with hypervascular tumors were significantly higher than those ( n =15, 0.0%) of patients with isovascular or hypovascular tumors as determined by USAG ( p =0.0061). The % AFP-L3 levels ( n =53, 4.4%) of patients with a negative portal blood supply were significantly higher than the % AFP-L3 levels ( n =7, 0.0%) of patients with a positive portal blood supply as determined by CTAP ( p =0.0140). The % AFP-L3 levels of patients with tumors with a long doubling time (DT) were significantly lower than for patients with tumors with a short DT ( p =0.0176). Conclusion: AFP-L3 is a positive indicator which may be more specific for small advanced hepatocellular carcinoma.

  • prognostic significance of Lens Culinaris agglutinin a reactive alpha fetoprotein in small hepatocellular carcinomas
    Gastroenterology, 1996
    Co-Authors: Fumihiko Yamashita, Shinji Satomura, Masatoshi Tanaka, Kyuichi Tanikawa
    Abstract:

    Abstract BACKGROUND & AIMS: Lens Culinaris agglutinin A-reactive fraction of alpha-fetoprotein (AFP-L3) has been reported to be a useful marker in the early diagnosis of hepatocellular carcinoma (HCC). The aim of this study was to evaluate the prognostic value of AFP-L3 for HCC. METHODS: Fifty-five patients with HCC whose AFP-L3 levels were negative before initial therapy were studied. AFP-L3 levels were measured by lectin- affinity electrophoresis coupled with antibody-affinity blotting. RESULTS: Of the 55 patients, 28, 15, and 12 underwent percutaneous ethanol injection, transcatheter arterial embolization, and hepatectomy, respectively. Thirty-two (58.2%) of the 55 patients maintained a negative AFP-L3 status during the study, and 23 patients (41.8%) became positive for AFP-L3 during posttreatment observation. Multiple recurrences of HCC and portal vein tumor thrombus were observed significantly more often in patients with positive AFP-L3 than in those with negative AFP-L3 status (P CONCLUSIONS: AFP-L3 seems to be a significant marker of poor prognosis for HCC. (Gastroenterology 1996 Oct;111(4):996-1001)

Albert Vandenberg - One of the best experts on this subject based on the ideXlab platform.

  • soil and weather conditions associated with plant damage from post emergent metribuzin in lentil Lens Culinaris in southern australia
    Crop & Pasture Science, 2019
    Co-Authors: Albert Vandenberg, Larn Mcmurray, C Preston, J G Paull
    Abstract:

    Multiple field experiments and a controlled-environment temperature study were conducted to investigate soil and weather conditions responsible for herbicide phytotoxicity in lentil (Lens Culinaris Medik.) from post-emergent application of metribuzin. A linear relationship was observed between plant injury (% necrosis) and metribuzin rate in all 12 environments, but in only 11 environments for anthesis dry weight and nine environments for both plant density and grain yield. Grain-yield reduction from label metribuzin rates of 135 g a.i. ha–1 for sand and 285 g a.i. ha–1 for clay ranged from 0% to 32% and 0% to 67%, respectively, across all environments. Principal component analysis of soil and weather factors around the time of herbicide application suggested that metribuzin-induced plant damage in lentil was due to a combination of multiple soil and weather factors. However, heavy rainfall within 10 days of herbicide application, particularly on light-textured soils or where soil moisture was low, was most strongly linked to plant damage. Experiments targeting the impact of reductions in temperature post-metribuzin application showed no effect, and of light intensities pre- and post-metribuzin application showed low effects on plant-damage measures. Because rainfall in the 10 days after application is a major determinant of metribuzin damage in winter-grown lentil in southern Australia, a higher level of selective tolerance to metribuzin than that present in commercial cultivars is needed for its safe post-emergent use. Early and late measures of plant damage will be required to assess accurately plant tolerance to post-emergent metribuzin application in lentil.

  • induced novel psba mutation ala251 to thr in higher plants confers resistance to psii inhibitor metribuzin in Lens Culinaris
    Pest Management Science, 2019
    Co-Authors: Albert Vandenberg, Larn Mcmurray, C Preston, Dili Mao, Kirstin E Bett, J G Paull
    Abstract:

    BACKGROUND Weed competition is a major limitation to worldwide lentil (Lens Culinaris Medik.) production in part due to limited effective safe herbicide options. Metribuzin is a photosystem II inhibiting herbicide that provides broad spectrum weed control, however it causes excessive injury in lentil. Dose response analysis of photosystem II inhibiting herbicides and DNA sequencing of the psbA chloroplast gene occurred to quantify the spectrum and mechanism of herbicide resistance in two ethyl-methanesulfonate (EMS) induced mutant lentils. RESULTS Compared to susceptible parent PBA Flash, the level of metribuzin resistance was 33-fold for mutant M043 and 10-fold for M009. No improvement in resistance occurred in either mutant to bromoxynil, diuron, bromacil and atrazine herbicides. Nucleotide sequencing of the psbA gene of both mutants identified a substitution at position 751 compared to PBA Flash. The resulting deduced amino acid sequence indicated an Ala251 Thr substitution as being most likely responsible for the high level of metribuzin resistance. CONCLUSIONS The Ala251 Thr substitution discovered in this study is unique in mutagenized higher plants and the first report of an induced psbA target site mutation in higher plants. This target site metribuzin resistance is likely to have a significant impact on lentil production in Australia and worldwide. © 2019 Society of Chemical Industry.

  • genotype specific responses to the effects of commercial trichoderma formulations in lentil Lens Culinaris ssp Culinaris in the presence and absence of the oomycete pathogen aphanomyces euteiches
    Biocontrol Science and Technology, 2017
    Co-Authors: Pratibha Prashar, Albert Vandenberg
    Abstract:

    ABSTRACTMembers of the endophytic fungal genus Trichoderma have been established as plant-beneficial microbes and are most successful commercial biologicals in the form of bio-fertilisers, biocontrol agents, and growth stimulators. We report the variable interactions among different lentil genotypes and Trichoderma strains in both the presence and absence of biotic stress (root-rot pathogen Aphanomyces euteiches). Two commercial Trichoderma formulations, namely RootShield® (RS) and RootShield® Plus (RSP) based on T. harzianum T22 and T. virens G41, respectively, were evaluated for control of Aphanomyces root rot and plant growth promotion in 23 wild and cultivated lentil genotypes. No significant disease control was recorded with either formulation in any lentil genotype. Significant genotype-specific plant growth promotion was observed in terms of root and shoot development and leaf parameters in a genotype-specific manner. Genotypes of Lens Culinaris and Lens tomentosus, both in the primary lentil gene ...

  • Iron Fortification of Lentil (Lens Culinaris Medik.) to Address Iron Deficiency
    Nutrients, 2017
    Co-Authors: Rajib Podder, Bunyamin Tar’an, Carol J. Henry, Diane M. Dellavalle, Robert T. Tyler, Albert Vandenberg
    Abstract:

    Iron (Fe) deficiency is a major human health concern in areas of the world in which diets are often Fe deficient. In the current study, we aimed to identify appropriate methods and optimal dosage for Fe fortification of lentil (Lens Culinaris Medik.) dal with FeSO4·7H2O (ferrous sulphate hepta-hydrate), NaFeEDTA (ethylenediaminetetraacetic acid iron (III) sodium salt) and FeSO4·H2O (ferrous sulphate mono-hydrate). We used a colorimetric method to determine the appearance of the dal fortified with fortificants at different Fe concentrations and under different storage conditions. Relative Fe bioavailability was assessed using an in vitro cell culture bioassay. We found that NaFeEDTA was the most suitable fortificant for red lentil dal, and at 1600 ppm, NaFeEDTA provides 13–14 mg of additional Fe per 100 g of dal. Lentil dal sprayed with fortificant solutions, followed by shaking and drying at 75 °C, performed best with respect to drying time and color change. Total Fe and phytic acid concentrations differed significantly between cooked unfortified and fortified lentil, ranging from 68.7 to 238.5 ppm and 7.2 to 8.0 mg g−1, respectively. The relative Fe bioavailability of cooked fortified lentil was increased by 32.2–36.6% compared to unfortified cooked lentil. We conclude that fortification of lentil dal is effective and could provide significant health benefits to dal-consuming populations vulnerable to Fe deficiency.

  • genetic diversity of cultivated lentil Lens Culinaris medik and its relation to the world s agro ecological zones
    Frontiers in Plant Science, 2016
    Co-Authors: Hamid Khazaei, Albert Vandenberg, Rebecca J Mcgee, Clarice J Coyne, Carolyn T Caron, Michael J Fedoruk, Marwan Diapari, Kirstin E Bett
    Abstract:

    Assessment of genetic diversity and population structure of germplasm collections plays a critical role in supporting conservation and crop genetic enhancement strategies. We used a cultivated lentil (Lens Culinaris Medik.) collection consisting of 352 accessions originating from 54 diverse countries to estimate genetic diversity and genetic structure using 1194 polymorphic single nucleotide polymorphism (SNP) markers which span the lentil genome. Using principal coordinate analysis, population structure analysis and UPGMA cluster analysis, the accessions were categorized into three major groups that prominently reflected geographical origin (world’s agro-ecological zones). The three clusters complemented the origins, pedigrees and breeding histories of the germplasm. The three groups were a) South Asia (sub-tropical savannah), b) Mediterranean and c) northern temperate. Based on the results from this study, it is also clear that breeding programs still have considerable genetic diversity to mine within the cultivated lentil, however, surveyed South Asian and Canadian germplasm revealed narrow genetic diversity.

Marcello Duranti - One of the best experts on this subject based on the ideXlab platform.

  • inhibitory properties and solution structure of a potent bowman birk protease inhibitor from lentil Lens Culinaris l seeds
    FEBS Journal, 2006
    Co-Authors: Enzio Ragg, Valerio Galbusera, Alessio Scarafoni, Armando Negri, Gabriella Tedeschi, Alessandro Consonni, Fabio Sessa, Marcello Duranti
    Abstract:

    Bowman–Birk serine protease inhibitors are a family of small plant proteins, whose physiological role has not been ascertained as yet, while chemopreventive anticarcinogenic properties have repeatedly been claimed. In this work we present data on the isolation of a lentil (Lens Culinaris, L., var. Macrosperma) seed trypsin inhibitor (LCTI) and its functional and structural characterization. LCTI is a 7448 Da double-headed trypsin/chymotrypsin inhibitor with dissociation constants equal to 0.54 nm and 7.25 nm for the two proteases, respectively. The inhibitor is, however, hydrolysed by trypsin in a few minutes timescale, leading to a dramatic loss of its affinity for the enzyme. This is due to a substantial difference in the kon and k*on values (1.1 µm−1·s−1 vs. 0.002 µm−1·s−1), respectively, for the intact and modified inhibitor. A similar behaviour was not observed with chymotrypsin. The twenty best NMR structures concurrently showed a canonical Bowman–Birk inhibitor (BBI) conformation with two antipodal β-hairpins containing the inhibitory domains. The tertiary structure is stabilized by ion pairs and hydrogen bonds involving the side chain and backbone of Asp10-Asp26-Arg28 and Asp36-Asp52 residues. At physiological pH, the final structure results in an asymmetric distribution of opposite charges with a negative electrostatic potential, centred on the C-terminus, and a highly positive potential, surrounding the antitryptic domain. The segment 53–55 lacks the anchoring capacity found in analogous BBIs, thus rendering the protein susceptible to hydrolysis. The inhibitory properties of LCTI, related to the simultaneous presence of two key amino acids (Gln18 and His54), render the molecule unusual within the natural Bowman–Birk inhibitor family.

  • Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens Culinaris, L.) seeds
    'Wiley', 2006
    Co-Authors: Enzio Ragg, Valerio Galbusera, Alessio Scarafoni, Armando Negri, Gabriella Tedeschi, Alessandro Consonni, F.a. Sessa, Marcello Duranti
    Abstract:

    Bowman-Birk serine protease inhibitors are a family of small plant proteins, whose physiological role has not been ascertained as yet, while chemopreventive anticarcinogenic properties have repeatedly been claimed. In this work we present data on the isolation of a lentil (Lens Culinaris, L., var. Macrosperma) seed trypsin inhibitor (LCTI) and its functional and structural characterization. LCTI is a 7448 Da double-headed trypsin/chymotrypsin inhibitor with dissociation constants equal to 0.54 nM and 7.25 nM for the two proteases, respectively. The inhibitor is, however, hydrolysed by trypsin in a few minutes timescale, leading to a dramatic loss of its affinity for the enzyme. This is due to a substantial difference in the kon and k*on values (1.1 microM-1.s-1 vs. 0.002 microM-1.s-1), respectively, for the intact and modified inhibitor. A similar behaviour was not observed with chymotrypsin. The twenty best NMR structures concurrently showed a canonical Bowman-Birk inhibitor (BBI) conformation with two antipodal beta-hairpins containing the inhibitory domains. The tertiary structure is stabilized by ion pairs and hydrogen bonds involving the side chain and backbone of Asp10-Asp26-Arg28 and Asp36-Asp52 residues. At physiological pH, the final structure results in an asymmetric distribution of opposite charges with a negative electrostatic potential, centred on the C-terminus, and a highly positive potential, surrounding the antitryptic domain. The segment 53-55 lacks the anchoring capacity found in analogous BBIs, thus rendering the protein susceptible to hydrolysis. The inhibitory properties of LCTI, related to the simultaneous presence of two key amino acids (Gln18 and His54), render the molecule unusual within the natural Bowman-Birk inhibitor family

Kyuichi Tanikawa - One of the best experts on this subject based on the ideXlab platform.

  • prognostic significance of Lens Culinaris agglutinin a reactive alpha fetoprotein in small hepatocellular carcinomas
    Gastroenterology, 1996
    Co-Authors: Fumihiko Yamashita, Shinji Satomura, Masatoshi Tanaka, Kyuichi Tanikawa
    Abstract:

    Abstract BACKGROUND & AIMS: Lens Culinaris agglutinin A-reactive fraction of alpha-fetoprotein (AFP-L3) has been reported to be a useful marker in the early diagnosis of hepatocellular carcinoma (HCC). The aim of this study was to evaluate the prognostic value of AFP-L3 for HCC. METHODS: Fifty-five patients with HCC whose AFP-L3 levels were negative before initial therapy were studied. AFP-L3 levels were measured by lectin- affinity electrophoresis coupled with antibody-affinity blotting. RESULTS: Of the 55 patients, 28, 15, and 12 underwent percutaneous ethanol injection, transcatheter arterial embolization, and hepatectomy, respectively. Thirty-two (58.2%) of the 55 patients maintained a negative AFP-L3 status during the study, and 23 patients (41.8%) became positive for AFP-L3 during posttreatment observation. Multiple recurrences of HCC and portal vein tumor thrombus were observed significantly more often in patients with positive AFP-L3 than in those with negative AFP-L3 status (P CONCLUSIONS: AFP-L3 seems to be a significant marker of poor prognosis for HCC. (Gastroenterology 1996 Oct;111(4):996-1001)

Enzio Ragg - One of the best experts on this subject based on the ideXlab platform.

  • inhibitory properties and solution structure of a potent bowman birk protease inhibitor from lentil Lens Culinaris l seeds
    FEBS Journal, 2006
    Co-Authors: Enzio Ragg, Valerio Galbusera, Alessio Scarafoni, Armando Negri, Gabriella Tedeschi, Alessandro Consonni, Fabio Sessa, Marcello Duranti
    Abstract:

    Bowman–Birk serine protease inhibitors are a family of small plant proteins, whose physiological role has not been ascertained as yet, while chemopreventive anticarcinogenic properties have repeatedly been claimed. In this work we present data on the isolation of a lentil (Lens Culinaris, L., var. Macrosperma) seed trypsin inhibitor (LCTI) and its functional and structural characterization. LCTI is a 7448 Da double-headed trypsin/chymotrypsin inhibitor with dissociation constants equal to 0.54 nm and 7.25 nm for the two proteases, respectively. The inhibitor is, however, hydrolysed by trypsin in a few minutes timescale, leading to a dramatic loss of its affinity for the enzyme. This is due to a substantial difference in the kon and k*on values (1.1 µm−1·s−1 vs. 0.002 µm−1·s−1), respectively, for the intact and modified inhibitor. A similar behaviour was not observed with chymotrypsin. The twenty best NMR structures concurrently showed a canonical Bowman–Birk inhibitor (BBI) conformation with two antipodal β-hairpins containing the inhibitory domains. The tertiary structure is stabilized by ion pairs and hydrogen bonds involving the side chain and backbone of Asp10-Asp26-Arg28 and Asp36-Asp52 residues. At physiological pH, the final structure results in an asymmetric distribution of opposite charges with a negative electrostatic potential, centred on the C-terminus, and a highly positive potential, surrounding the antitryptic domain. The segment 53–55 lacks the anchoring capacity found in analogous BBIs, thus rendering the protein susceptible to hydrolysis. The inhibitory properties of LCTI, related to the simultaneous presence of two key amino acids (Gln18 and His54), render the molecule unusual within the natural Bowman–Birk inhibitor family.

  • Inhibitory properties and solution structure of a potent Bowman-Birk protease inhibitor from lentil (Lens Culinaris, L.) seeds
    'Wiley', 2006
    Co-Authors: Enzio Ragg, Valerio Galbusera, Alessio Scarafoni, Armando Negri, Gabriella Tedeschi, Alessandro Consonni, F.a. Sessa, Marcello Duranti
    Abstract:

    Bowman-Birk serine protease inhibitors are a family of small plant proteins, whose physiological role has not been ascertained as yet, while chemopreventive anticarcinogenic properties have repeatedly been claimed. In this work we present data on the isolation of a lentil (Lens Culinaris, L., var. Macrosperma) seed trypsin inhibitor (LCTI) and its functional and structural characterization. LCTI is a 7448 Da double-headed trypsin/chymotrypsin inhibitor with dissociation constants equal to 0.54 nM and 7.25 nM for the two proteases, respectively. The inhibitor is, however, hydrolysed by trypsin in a few minutes timescale, leading to a dramatic loss of its affinity for the enzyme. This is due to a substantial difference in the kon and k*on values (1.1 microM-1.s-1 vs. 0.002 microM-1.s-1), respectively, for the intact and modified inhibitor. A similar behaviour was not observed with chymotrypsin. The twenty best NMR structures concurrently showed a canonical Bowman-Birk inhibitor (BBI) conformation with two antipodal beta-hairpins containing the inhibitory domains. The tertiary structure is stabilized by ion pairs and hydrogen bonds involving the side chain and backbone of Asp10-Asp26-Arg28 and Asp36-Asp52 residues. At physiological pH, the final structure results in an asymmetric distribution of opposite charges with a negative electrostatic potential, centred on the C-terminus, and a highly positive potential, surrounding the antitryptic domain. The segment 53-55 lacks the anchoring capacity found in analogous BBIs, thus rendering the protein susceptible to hydrolysis. The inhibitory properties of LCTI, related to the simultaneous presence of two key amino acids (Gln18 and His54), render the molecule unusual within the natural Bowman-Birk inhibitor family