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Sci Rep ; 8(1): 428, 2018 01 11.
Artigo em Inglês | MEDLINE | ID: mdl-29323145


Although xyloglucan (XyG) is reported to bind Aluminium (Al), the influence of XyG fucosylation on the cell wall Al binding capacity and plant Al stress responses is unclear. We show that Arabidopsis T-DNA insertion mutants with reduced AXY3 (XYLOSIDASE1) function and consequent reduced levels of fucosylated XyG are more sensitive to Al than wild-type Col-0 (WT). In contrast, T-DNA insertion mutants with reduced AXY8 (FUC95A) function and consequent increased levels of fucosylated XyG are more Al resistant. AXY3 transcript levels are strongly down regulated in response to 30 min Al treatment, whilst AXY8 transcript levels also repressed until 6 h following treatment onset. Mutants lacking AXY3 or AXY8 function exhibit opposing effects on Al contents of root cell wall and cell wall hemicellulose components. However, there was no difference in the amount of Al retained in the pectin components between mutants and WT. Finally, whilst the total sugar content of the hemicellulose fraction did not change, the altered hemicellulose Al content of the mutants is shown to be a likely consequence of their different XyG fucosylation levels. We conclude that variation in XyG fucosylation levels influences the Al sensitivity of Arabidopsis by affecting the Al-binding capacity of hemicellulose.

Proteínas de Arabidopsis/genética , Arabidopsis/crescimento & desenvolvimento , Fucose/metabolismo , Glucanos/química , Polissacarídeos/metabolismo , Xilanos/química , Alumínio , Arabidopsis/genética , Arabidopsis/metabolismo , Parede Celular/genética , Parede Celular/metabolismo , DNA Bacteriano/genética , Mutagênese Insercional , Raízes de Plantas/genética , Raízes de Plantas/crescimento & desenvolvimento , Raízes de Plantas/metabolismo , Xilosidases/genética , alfa-L-Fucosidase/genética
Chin Med J (Engl) ; 129(9): 1072-7, 2016 May 05.
Artigo em Inglês | MEDLINE | ID: mdl-27098793


BACKGROUND: Gaucher's disease (GD) is an autosomal recessive disorder caused by a deficiency of acid ß-glucosidase (glucocerebrosidase [GBA]) that results in the accumulation of glucocerebroside within macrophages. Many mutations have been reported to be associated with this disorder. This study aimed to discover more mutations and provide data for the genetic pattern of the gene, which will help the development of quick and accurate genetic diagnostic tools for this disease. METHODS: Genomic DNA was obtained from peripheral blood leukocytes of the patient and Sanger sequencing is used to sequence GBA gene. Sequence alignments of mammalian ß-GBA (GCase) and three-dimensional protein structure prediction of the mutation were made. A construct of this mutant and its compound heterozygous counterpart were used to measure GCase in vitro. RESULTS: GCase is relatively conserved at p.T219A. This novel mutation differs from its wild-type in structure. Moreover, it also causes a reduction in GCase enzyme activity. CONCLUSION: This novel mutation (c.655A>G, p.T219A) is a pathogenic missense mutation, which contributes to GD.

Doença de Gaucher/genética , Glucosilceramidase/genética , Mutação de Sentido Incorreto , Pré-Escolar , Glucosilceramidase/química , Humanos , Masculino , Modelos Moleculares , Estrutura Terciária de Proteína , Análise de Sequência de DNA
Yi Chuan ; 37(6): 510-6, 2015 06.
Artigo em Chinês | MEDLINE | ID: mdl-26351046


Gaucher's disease (GD) also named glucocerebroside lipidosis, is the most common kind of 1ysosomal storage disorder. It results from an autosomal recessive deficiency of the lysosomal enzyme acid ß-glucosidase/ ß-glucocerebrosidase (GBA), which is responsible for hydrolysis of glucocerebroside/glucosylceramide (GlcCer) into glucose and ceramide. Absent or reduced enzymatic activity of GBA leads to multisystemic accumulation of GlcCer in mononuclear phagocyte system and various tissues, such as brain, liver, spleen and so on, causing brain injury, liver splenomegaly, bone damage, the reduction of blood cells and individual growth retardation. GD type I could be treated by enzyme replacement therapy (ERT), but GD types II and III have not effective treatment. In this review, we summarize the recent progress on pathogenic mechanism and therapies in GD.

Doença de Gaucher/etiologia , Doença de Gaucher/terapia , Animais , Terapia de Reposição de Enzimas , Terapia Genética , Glucosilceramidase/genética , Glucosilceramidase/metabolismo , Humanos , Mutação
Bing Du Xue Bao ; 30(2): 109-18, 2014 Mar.
Artigo em Chinês | MEDLINE | ID: mdl-24923162


Five H9N2 avian influenza virus strains were isolated from the environmental samples in live poultry market in Qinghai Lake region from July to September, 2012. To evaluate the phylogenetic characteristics of these H9N2 isolates, the eight gene segments were amplified by RT-PCR and sequenced. The phylogenetic and molecular characteristics of the five strains were analyzed. The results showed that the HA genes of five strains shared 93. 2%-99. 1% nucleotide identities with each other, and the NA genes shared 94. 5%-99. 8% nucleotide identities. The HA cleavage site sequence of the A/environment/qinghai/ 017/2012 isolate was PSKSSRGLF, and the HA cleavage site sequences of the other four strains were all PSRSSRGLF. The HA receptor-binding site had the Q226L mutation. The M1 gene segment had the N30D and T215A mutations. The phylogenetic analysis showed that the five strains were similar to the virus A/chicken/Hunan/5260/2005 (H9N2) isolated in Hunan Province, China and were reassortant genotype viruses; the HA, NA, and NS genes belonged to the Y280-like lineage; the MP gene belonged to the G1-like lineage; the NP, PB1, PB2, and PA genes belonged to the F98-like lineage.

Genoma Viral , Vírus da Influenza A Subtipo H9N2/classificação , Vírus da Influenza A Subtipo H9N2/isolamento & purificação , Influenza Aviária/virologia , Filogenia , Doenças das Aves Domésticas/virologia , Animais , China , Genótipo , Vírus da Influenza A Subtipo H9N2/genética , Dados de Sequência Molecular , Aves Domésticas , Proteínas Virais/genética