Database : MEDLINE
Search on : D08.811.277.450.483.180.750.500 [DeCS Category]
References found : 36 [refine]
Displaying: 1 .. 10   in format [Large]

page 1 of 4 go to page            

  1 / 36 MEDLINE  
              next record last record
select
to print
Photocopy
Full text
PMID:29235819
Author:Olkhovych NV; Gorovenko NG
Title:Determination of frequencies of alleles, associated with the pseudodeficiency of lysosomal hydrolases, in population of Ukraine.
Source:Ukr Biochem J; 88(5):96-106, 2016 Sep-Oct.
ISSN:2409-4943
Country of publication:Ukraine
Language:eng
Abstract:The pseudodeficiency of lysosomal hydrolases described as a significant reduction in enzyme activi­ty in vitro in clinically healthy individuals, can lead to diagnostic errors in the process of biochemical analysis of lysosomal storage disease in case of its combination with pathology of another origin. Pseudodeficiency is mostly caused by some non-pathogenic changes in the corresponding gene. These changes lead to the in vitro lability of the enzyme molecule, whereas in vivo the enzyme retains its functional activity. To assess the prevalence of the most common lysosomal hydrolases pseudodeficiency alleles in Ukraine, we have determined the frequency of alleles c.1055A>G and c.* 96A>G in the ARSA gene, substitutions c.739C>T (R247W) and c.745C>T (R249W) in the HEXA gene, c.1726G>A (G576S) and c.2065G>A (E689K) in the GAA gene, c.937G>T (D313Y) in the GLA1 gene and c.898G>A (A300T) in the IDUA gene in a group of 117 healthy individuals from different regions of the country and 14 heterozygous carriers of pathogenic mutations in the HEXA gene (parents of children with confirmed diagnosis of Tay-Sachs disease). The total frequency of haplotypes, associated with arylsulfatase A pseudodeficiency, in healthy people in Ukraine (c.1055G/c.*96G and c.1055G/c.*96A haplotypes) was 10.3%. The frequency of c.739C>T (R247W) allele, associated with hexo­saminidase A pseudodeficiency, among Tay-Sachs carriers from Ukraine was 7.1%. The total frequency of α-glucosidase pseudodeficiency haplotypes in healthy individuals in Ukraine (c.1726A/c.2065A and c.1726G/c.2065A haplotypes) was 2.6%. No person among examined individuals with the substitution c.937G>T (D313Y) in the GLA1 gene and c.898G>A (A300T) in the IDUA gene was found. The differential diagnostics of lysosomal storage diseases requires obligatory determination of the presence of the pseudodeficiency alleles, particularly the ones with high incidence in the total population. Ignoring phenomenon of pseudodeficiency may lead to serious diagnostic errors.
Publication type:JOURNAL ARTICLE
Name of substance:EC 3.1.6.8 (Cerebroside-Sulfatase); EC 3.2.1.20 (GAA protein, human); EC 3.2.1.20 (alpha-Glucosidases); EC 3.2.1.22 (alpha-Galactosidase); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain); EC 3.2.1.76 (IDUA protein, human); EC 3.2.1.76 (Iduronidase)


  2 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:27362553
Author:Mehta N; Lazarin GA; Spiegel E; Berentsen K; Brennan K; Giordano J; Haque IS; Wapner R
Address:1 Counsyl , South San Francisco, California.
Title:Tay-Sachs Carrier Screening by Enzyme and Molecular Analyses in the New York City Minority Population.
Source:Genet Test Mol Biomarkers; 20(9):504-9, 2016 Sep.
ISSN:1945-0257
Country of publication:United States
Language:eng
Abstract:BACKGROUND AND AIMS: Carrier screening for Tay-Sachs disease is performed by sequence analysis of the HEXA gene and/or hexosaminidase A enzymatic activity testing. Enzymatic analysis (EA) has been suggested as the optimal carrier screening method, especially in non-Ashkenazi Jewish (non-AJ) individuals, but its utilization and efficacy have not been fully evaluated in the general population. This study assesses the reliability of EA in comparison with HEXA sequence analysis in non-AJ populations. METHODS: Five hundred eight Hispanic and African American patients (516 samples) had EA of their leukocytes performed and 12 of these patients who tested positive by EA ("carriers") had subsequent HEXA gene sequencing performed. RESULTS: Of the 508 patients, 25 (4.9%) were EA positive and 40 (7.9%) were inconclusive. Of the 12 patients who were sequenced, 11 did not carry a pathogenic variant and one carried a likely deleterious mutation (NM_000520.4(HEXA):c.1510C>T). CONCLUSIONS: High inconclusive rates and poor correlation between positive/inconclusive enzyme results and identification of pathogenic mutations suggest that ethnic-specific recalibration of reference ranges for EA may be necessary. Alternatively, HEXA gene sequencing could be performed.
Publication type:JOURNAL ARTICLE
Name of substance:EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain)


  3 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:27033294
Author:Steiner KM; Brenck J; Goericke S; Timmann D
Address:Universitatsklinikum Essen Klinik fur Neurologie, Essen, Nordrhein-Westfalen, Germany.
Title:Cerebellar atrophy and muscle weakness: late-onset Tay-Sachs disease outside Jewish populations.
Source:BMJ Case Rep; 2016, 2016 Mar 31.
ISSN:1757-790X
Country of publication:England
Language:eng
Publication type:CASE REPORTS; JOURNAL ARTICLE
Name of substance:EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain)


  4 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:26401073
Author:Miklavcic JJ; Hart TD; Lees GM; Shoemaker GK; Schnabl KL; Larsen BM; Bathe OF; Thomson AB; Mazurak VC; Clandinin MT
Address:John J Miklavcic, Glen K Shoemaker, Vera C Mazurak, M Tom Clandinin, Alberta Institute for Human Nutrition, University of Alberta, Edmonton AB T6G 2R1, Canada.
Title:Increased catabolism and decreased unsaturation of ganglioside in patients with inflammatory bowel disease.
Source:World J Gastroenterol; 21(35):10080-90, 2015 Sep 21.
ISSN:2219-2840
Country of publication:United States
Language:eng
Abstract:AIM: To investigate whether accelerated catabolism of ganglioside and decreased ganglioside content contribute to the etiology of pro-inflammatory intestinal disease. METHODS: Intestinal mucosa from terminal ileum or colon was obtained from patients with ulcerative colitis or inflammatory Crohn's disease (n = 11) undergoing bowel resection and compared to control samples of normal intestine from patients with benign colon polyps (n = 6) and colorectal cancer (n = 12) in this observational case-control study. Gangliosides and phospholipids of intestinal mucosa were characterized by class and ceramide or fatty acid composition using liquid chromatography triple-quad mass spectrometry. Content and composition of ganglioside classes GM1, GM3, GD3, GD1a, GT1 and GT3 were compared among subject groups. Content and composition of phospholipid classes phosphatidylcholine (PC) and phosphatidylethanolamine were compared among subject groups. Unsaturation index of individual ganglioside and phospholipid classes was computed and compared among subject groups. Ganglioside catabolism enzymes beta-hexosaminidase A (HEXA) and sialidase-3 (NEU3) were measured in intestinal mucosa using western blot and compared among subject groups. RESULTS: Relative GM3 ganglioside content was 2-fold higher (P < 0.05) in intestine from patients with inflammatory bowel disease (IBD) compared to control intestine. The quantity of GM3 and ratio of GM3/GD3 was also higher in IBD intestine than control tissue (P < 0.05). Control intestine exhibited 3-fold higher (P < 0.01) relative GD1a ganglioside content than IBD intestine. GD3 and GD1a species of ganglioside containing three unsaturated bonds were present in control intestine, but were not detected in IBD intestine. The relative content of PC containing more than two unsaturated bonds was 30% lower in IBD intestine than control intestine (P < 0.05). The relative content of HEXA in IBD intestine was increased 1.7-fold (P < 0.05) and NEU3 was increased 8.3-fold (P < 0.01) compared to normal intestine. Intestinal mucosa in IBD is characterized by increased GM3 content, decreased GD1a, and a reduction in polyunsaturated fatty acid constituents in GD3, GD1a and PC. CONCLUSION: This study suggests a new paradigm by proposing that IBD occurs as a consequence of increased metabolism of specific gangliosides.
Publication type:JOURNAL ARTICLE; OBSERVATIONAL STUDY; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Fatty Acids, Unsaturated); 0 (G(M3) Ganglioside); 0 (Gangliosides); 0 (Phosphatidylcholines); 0 (Phosphatidylethanolamines); 12707-58-3 (ganglioside, GD1a); 62010-37-1 (ganglioside, GD3); EC 3.2.1.18 (Neu3 protein, human); EC 3.2.1.18 (Neuraminidase); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain)


  5 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
Full text
PMID:26175473
Author:Anheuser S; Breiden B; Schwarzmann G; Sandhoff K
Address:LIMES Institute, Membrane Biology and Lipid Biochemistry Unit, Kekulé-Institut für Organische Chemie und Biochemie, Universität Bonn, D-53121 Bonn, Germany.
Title:Membrane lipids regulate ganglioside GM2 catabolism and GM2 activator protein activity.
Source:J Lipid Res; 56(9):1747-61, 2015 Sep.
ISSN:1539-7262
Country of publication:United States
Language:eng
Abstract:Ganglioside GM2 is the major lysosomal storage compound of Tay-Sachs disease. It also accumulates in Niemann-Pick disease types A and B with primary storage of SM and with cholesterol in type C. Reconstitution of GM2 catabolism with ß-hexosaminidase A and GM2 activator protein (GM2AP) at uncharged liposomal surfaces carrying GM2 as substrate generated only a physiologically irrelevant catabolic rate, even at pH 4.2. However, incorporation of anionic phospholipids into the GM2 carrying liposomes stimulated GM2 hydrolysis more than 10-fold, while the incorporation of plasma membrane stabilizing lipids (SM and cholesterol) generated a strong inhibition of GM2 hydrolysis, even in the presence of anionic phospholipids. Mobilization of membrane lipids by GM2AP was also inhibited in the presence of cholesterol or SM, as revealed by surface plasmon resonance studies. These lipids also reduced the interliposomal transfer rate of 2-NBD-GM1 by GM2AP, as observed in assays using Förster resonance energy transfer. Our data raise major concerns about the usage of recombinant His-tagged GM2AP compared with untagged protein. The former binds more strongly to anionic GM2-carrying liposomal surfaces, increases GM2 hydrolysis, and accelerates intermembrane transfer of 2-NBD-GM1, but does not mobilize membrane lipids.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Ceramides); 0 (G(M2) Activator Protein); 0 (Liposomes); 0 (Lysophospholipids); 0 (Membrane Lipids); 0 (Monoglycerides); 0 (Sphingomyelins); 0 (bis(monoacylglyceryl)phosphate); 19600-01-2 (G(M2) Ganglioside); 97C5T2UQ7J (Cholesterol); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain)


  6 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:26020229
Author:Couceiro R; Fonseca A; Campos F
Title:Toddler with retinal defects. . .psychomotor regression. Sandhoff disease.
Source:J Pediatr Ophthalmol Strabismus; 52(3):138-9, 176, 2015 May-Jun.
ISSN:1938-2405
Country of publication:United States
Language:eng
Publication type:CASE REPORTS; JOURNAL ARTICLE
Name of substance:EC 3.2.1.52 (beta-Hexosaminidase alpha Chain); EC 3.2.1.52 (beta-Hexosaminidase beta Chain)


  7 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:25934542
Author:Feng D; Su RC; Zou L; Triggs-Raine B; Huang S; Xie J
Address:Department of Medical Genetics, Institute of Basic Medical Sciences, Chinese Academy of Medical Sciences & Peking Union Medical College Beijing 100005, China; Department of Physiology and Pathophysiology, Faculty of Medicine, University of Manitoba, Winnipeg MB R3E 0J9, Canada.
Title:Increase of a group of PTC(+) transcripts by curcumin through inhibition of the NMD pathway.
Source:Biochim Biophys Acta; 1849(8):1104-15, 2015 Aug.
ISSN:0006-3002
Country of publication:Netherlands
Language:eng
Abstract:Nonsense-mediated mRNA decay (NMD), an mRNA surveillance mechanism, eliminates premature termination codon-containing (PTC⁺) transcripts. For instance, it maintains the homeostasis of splicing factors and degrades aberrant transcripts of human genetic disease genes. Here we examine the inhibitory effect on the NMD pathway and consequent increase of PTC+ transcripts by the dietary compound curcumin. We have found that several PTC⁺ transcripts including that of serine/arginine-rich splicing factor 1 (SRSF1) were specifically increased in cells by curcumin. We also observed a similar curcumin effect on the PTC⁺ mutant transcript from a Tay-Sachs-causing HEXA allele or from a beta-globin reporter gene. The curcumin effect was accompanied by significantly reduced expression of the NMD factors UPF1, 2, 3A and 3B. Consistently, in chromatin immunoprecipitation assays, curcumin specifically reduced the occupancy of acetyl-histone H3 and RNA polymerase II at the promoter region (-376 to -247nt) of human UPF1, in a time- and dosage-dependent way. Importantly, knocking down UPF1 abolished or substantially reduced the difference of PTC(+) transcript levels between control and curcumin-treated cells. The disrupted curcumin effect was efficiently rescued by expression of exogenous Myc-UPF1 in the knockdown cells. Together, our data demonstrate that a group of PTC⁺ transcripts are stabilized by a dietary compound curcumin through the inhibition of UPF factor expression and the NMD pathway.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Codon, Nonsense); 0 (Nuclear Proteins); 0 (RNA, Messenger); 0 (RNA-Binding Proteins); 170974-22-8 (Serine-Arginine Splicing Factors); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain); IT942ZTH98 (Curcumin)


  8 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text
PMID:25860343
Author:Stendel C; Gallenmüller C; Peters K; Bürger F; Gramer G; Biskup S; Klopstock T
Address:Department of Neurology, Friedrich-Baur-Institute, Ludwig-Maximilians-University, 80336, Munich, Germany, claudia.stendel@med.uni-muenchen.de.
Title:Paranoid delusion as lead symptom in two siblings with late-onset Tay-Sachs disease and a novel mutation in the HEXA gene.
Source:J Neurol; 262(4):1072-3, 2015.
ISSN:1432-1459
Country of publication:Germany
Language:eng
Publication type:CASE REPORTS; LETTER
Name of substance:EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain)


  9 / 36 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
PubMed Central Full text
PMID:24518553
Author:Jamali S; Eskandari N; Aryani O; Salehpour S; Zaman T; Kamalidehghan B; Houshmand M
Address:Dept. of Genetics, Islamic Azad University, Ahar, Iran.
Title:Three novel mutations in Iranian patients with Tay-Sachs disease.
Source:Iran Biomed J; 18(2):114-9, 2014.
ISSN:2008-823X
Country of publication:Iran
Language:eng
Abstract:BACKGROUND: Tay-Sachs disease (TSD), or GM2 gangliosidosis, is a lethal autosomal recessive neurodegenerative disorder, which is caused by a deficiency of beta-hexosaminidase A (HEXA), resulting in lysosomal accumulation of GM2 ganglioside. The aim of this study was to identify the TSD-causing mutations in an Iranian population. METHODS: In this study, we examined 31 patients for TSD-causing mutations using PCR, followed by restriction enzyme digestion. RESULTS: Molecular genetics analysis of DNA from 23 patients of TSD revealed mutations that has been previously reported, including four-base duplications c.1274_1277dupTATC in exon 11 and IVS2+1G>A, deletion TTAGGCAAGGGC in exon 10 as well as a few novel mutations, including C331G, which altered Gln>Glu in HEXB, A>G, T>C, and p.R510X in exon 14, which predicted a termination codon or nonsense mutation. CONCLUSION: In conclusion, with the discovery of these novel mutations, the genotypic spectrum of Iranian patients with TSD disease has been extended and could facilitate definition of disease-related mutations.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (Protein Subunits); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (HEXB protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain); EC 3.2.1.52 (beta-Hexosaminidase beta Chain)


  10 / 36 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text
PMID:24389457
Author:Costanzi E; Urbanelli L; Bellezza I; Magini A; Emiliani C; Minelli A
Address:Dipartimento Medicina Sperimentale e Scienze Biochimiche, Università degli Studi di Perugia, 06124 Perugia, Italy. Electronic address: egidia.costanzi@unipg.it.
Title:Hypermethylation contributes to down-regulation of lysosomal ß-hexosaminidase α subunit in prostate cancer cells.
Source:Biochimie; 101:75-82, 2014 Jun.
ISSN:1638-6183
Country of publication:France
Language:eng
Abstract:ß-Hexosaminidase, involved in degradation of glycoproteins and glycosphingolipids, is altered in several tumours leading to enhanced migration capacity. To date, the expression of the ß-hexosaminidase isoenzymes in prostate cancer cells has not been elucidated. By using PC3, LNCaP, DUCaP, MDAPCa 2b, and hyperplasic prostate (BPH-1) cell lines, we analysed the ß-hexosaminidase activity in each cell line and determined ß-hexosaminidase α subunit gene expression in PC3, LNCaP, and BPH-1. We then investigated the methylation status of the gene promoter and determined the cellular responses of PC3 and LNCaP after transfection with ß-hexosaminidase α subunit. We found that each prostate cancer cell line had a decrease in total hexosaminidase activity and that the lack of hexosaminidase A activity, observed in PC3 and LNCaP cells, was associated with mRNA disappearance. The HEXA promoter region in LNCaP and PC3 cell lines had methylated CpG islands, as confirmed by 5'-Aza-2'-deoxycitidine treatment, in PC3 cells, used as cell cancer model. We also tested, the involvement of hexosaminidase A in the migration capacity by migration assay using Hex α subunit-transfected PC3. Finally, we found that, after Hex α subunit transfection, both PC3 and LNCaP were less susceptible to exogenous ceramide treatment. Results indicate a likely contribution of the lysosomal enzyme to the acquisition of cancerous features.
Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
Name of substance:0 (N-acetylsphingosine); EC 3.2.1.52 (HEXA protein, human); EC 3.2.1.52 (beta-Hexosaminidase alpha Chain); NGZ37HRE42 (Sphingosine)



page 1 of 4 go to page            
   


Refine the search
  Database : MEDLINE Advanced form   

    Search in field  
1  
2
3
 
           



Search engine: iAH v2.6 powered by WWWISIS

BIREME/PAHO/WHO - Latin American and Caribbean Center on Health Sciences Information