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Search on : Mucolipidoses [Words]
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[PMID]: 28449103
[Au] Autor:Li H; Pei W; Vergarajauregui S; Zerfas PM; Raben N; Burgess SM; Puertollano R
[Ad] Address:Cell Biology and Physiology Center, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD, USA.
[Ti] Title:Novel degenerative and developmental defects in a zebrafish model of mucolipidosis type IV.
[So] Source:Hum Mol Genet;26(14):2701-2718, 2017 07 15.
[Is] ISSN:1460-2083
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Mucolipidosis type IV (MLIV) is a lysosomal storage disease characterized by neurologic and ophthalmologic abnormalities. There is currently no effective treatment. MLIV is caused by mutations in MCOLN1, a lysosomal cation channel from the transient receptor potential (TRP) family. In this study, we used genome editing to knockout the two mcoln1 genes present in Danio rerio (zebrafish). Our model successfully reproduced the retinal and neuromuscular defects observed in MLIV patients, indicating that this model is suitable for studying the disease pathogenesis. Importantly, our model revealed novel insights into the origins and progression of the MLIV pathology, including the contribution of autophagosome accumulation to muscle dystrophy and the role of mcoln1 in embryonic development, hair cell viability and cellular maintenance. The generation of a MLIV model in zebrafish is particularly relevant given the suitability of this organism for large-scale in vivo drug screening, thus providing unprecedented opportunities for therapeutic discovery.
[Mh] MeSH terms primary: Mucolipidoses/genetics
Transient Receptor Potential Channels/genetics
Zebrafish Proteins/genetics
[Mh] MeSH terms secundary: Amino Acid Sequence
Animals
Autophagosomes/metabolism
Disease Models, Animal
Gene Knockout Techniques
Mucolipidoses/metabolism
Mucolipidoses/pathology
Mutation
Transient Receptor Potential Channels/metabolism
Zebrafish
Zebrafish Proteins/metabolism
[Pt] Publication type:JOURNAL ARTICLE; RESEARCH SUPPORT, N.I.H., INTRAMURAL
[Nm] Name of substance:0 (MCOLN1.1 protein, zebrafish); 0 (Transient Receptor Potential Channels); 0 (Zebrafish Proteins)
[Em] Entry month:1801
[Cu] Class update date: 180225
[Lr] Last revision date:180225
[Js] Journal subset:IM
[Da] Date of entry for processing:170428
[St] Status:MEDLINE
[do] DOI:10.1093/hmg/ddx158

  2 / 1020 MEDLINE  
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[PMID]: 29218369
[Au] Autor:Mulroy E; Chancellor AM; Pelosi L
[Ad] Address:Neurology Department, Auckland City Hospital, 2 Park Road, Grafton, Auckland, 1023, New Zealand. EoinM@adhb.govt.nz.
[Ti] Title:Peripheral nerve ultrasound findings in mucolipidosis type 3.
[So] Source:Neuroradiology;60(2):207-209, 2018 Feb.
[Is] ISSN:1432-1920
[Cp] Country of publication:Germany
[La] Language:eng
[Ab] Abstract:PURPOSE: The mucolipidoses are rare autosomal recessive lysosomal storage disorders. Neurologic involvement in these conditions is generally thought to be limited to cognitive delay and entrapment neuropathies (primarily carpal tunnel syndrome). We sought to evaluate peripheral nerves in this condition using nerve ultrasound. METHODS: We performed peripheral nerve ultrasound in two siblings with genetically confirmed mucolipidosis type 3 (alpha/beta). RESULTS: Peripheral nerves in mucolipidosis type 3 (alpha/beta) exhibit multifocal enlargement. CONCLUSION: The peripheral nerve ultrasound has a role in the evaluation of this, and possibly other lysosomal storage disorders.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180225
[Lr] Last revision date:180225
[St] Status:In-Process
[do] DOI:10.1007/s00234-017-1953-5

  3 / 1020 MEDLINE  
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[PMID]: 29289611
[Au] Autor:Kazemi N; Estiar MA; Fazilaty H; Sakhinia E
[Ad] Address:Immunology Research Center, Tabriz University of Medical Sciences, Tabriz, Iran; Division of Medical Genetics, Department of Clinical Biochemistry, Faculty of Medicine, Tabriz University of Medical Sciences, Tabriz, Iran.
[Ti] Title:Variants in GNPTAB, GNPTG and NAGPA genes are associated with stutterers.
[So] Source:Gene;647:93-100, 2018 Mar 20.
[Is] ISSN:1879-0038
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Non-syndromic stuttering is a neurodevelopmental disorder characterized by disruptions in normal flow of speech in the form of repetition, prolongation and involuntary halts. Previously, mutations with more severe effects on GNPTAB and GNPTG have been reported to cause Mucolipidosisll (ML-ll) and Mucolipidosislll (ML-lll), two lysosomal storage disorders with multiple pathologies. We used homozygosity mapping and Sanger sequencing to investigate variants of the three genes in 25 Iranian families with at least two first degree related non-syndromic stutterers. Bioinformatic evaluation and Segregation analysis of the found variants helped us define probable consequences. We also compared our findings with those related to Mucolipidosis. 14 variations were found in the three genes 3 of which, including a novel variant within intronic region of GNPTG and a heterozygous 2-bp deletion in coding region of GNPTAB, co-segregated with stuttering in the families they were found. Bioinformatics analysis predicted all three variants causing deleterious effects on gene functioning. Our findings support the role of these three variants in non-syndromic stuttering. This finding may challenge the current belief that variations causing stuttering are at different sites and have less severe consequences than genetic changes that cause ML-ll and ML-lll.
[Mh] MeSH terms primary: Genetic Predisposition to Disease/genetics
Mutation/genetics
Phosphoric Diester Hydrolases/genetics
Stuttering/genetics
Transferases (Other Substituted Phosphate Groups)/genetics
[Mh] MeSH terms secundary: Child
Child, Preschool
Female
Heterozygote
Homozygote
Humans
Introns/genetics
Male
Mucolipidoses/genetics
Phenotype
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:EC 2.7.8.- (Transferases (Other Substituted Phosphate Groups)); EC 2.7.8.15 (GNPTAB protein, human); EC 2.7.8.17 (GNPTG protein, human); EC 3.1.4.- (Phosphoric Diester Hydrolases); EC 3.1.4.45 (N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase)
[Em] Entry month:1802
[Cu] Class update date: 180209
[Lr] Last revision date:180209
[Js] Journal subset:IM
[Da] Date of entry for processing:180101
[St] Status:MEDLINE

  4 / 1020 MEDLINE  
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Acosta, Angelina Xavier
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[PMID]: 28918368
[Au] Autor:Ludwig NF; Velho RV; Sperb-Ludwig F; Acosta AX; Ribeiro EM; Kim CA; Gandelman Horovitz DD; Boy R; Rodovalho-Doriqui MJ; Lourenço CM; Santos ES; Braulke T; Pohl S; Schwartz IVD
[Ad] Address:Center of Gene Therapy, Hospital de Clínicas de Porto Alegre, Porto Alegre, Brazil; BRAIN Laboratory, Hospital de Clínicas de Porto Alegre, Porto Alegre, Brazil; Post Graduate Program in Genetics and Molecular Biology of Universidade Federal do Rio Grande do Sul, Porto Alegre, Brazil.
[Ti] Title:GNPTAB missense mutations cause loss of GlcNAc-1-phosphotransferase activity in mucolipidosis type II through distinct mechanisms.
[So] Source:Int J Biochem Cell Biol;92:90-94, 2017 Nov.
[Is] ISSN:1878-5875
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Mucolipidoses (ML) II and III alpha/beta are lysosomal storage diseases caused by pathogenic mutations in GNPTAB encoding the α/ß-subunit precursor of GlcNAc-1-phosphotransferase. To determine genotype-phenotype correlation and functional analysis of mutant GlcNAc-1-phosphotransferase, 13 Brazilian patients clinically and biochemical diagnosed for MLII or III alpha/beta were studied. By sequencing of genomic GNPTAB of the MLII and MLIII alpha/beta patients we identified six novel mutations: p.D76G, p.S385L, p.Q278Kfs*3, p.H588Qfs*27, p.N642Lfs*10 and p.Y1111*. Expression analysis by western blotting and immunofluorescence microscopy revealed that the mutant α/ß-subunit precursor p.D76G is retained in the endoplasmic reticulum whereas the mutant p.S385L is correctly transported to the cis-Golgi apparatus and proteolytically processed. Both mutations lead to complete loss of GlcNAc-1-phosphotransferase activity, consistent with the severe clinical MLII phenotype of the patients. Our study expands the genotypic spectrum of MLII and provides novel insights into structural requirements to ensure GlcNAc-1-phosphotransferase activity.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171107
[Lr] Last revision date:171107
[St] Status:In-Process

  5 / 1020 MEDLINE  
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[PMID]: 28442549
[Au] Autor:Pan X; De Aragão CBP; Velasco-Martin JP; Priestman DA; Wu HY; Takahashi K; Yamaguchi K; Sturiale L; Garozzo D; Platt FM; Lamarche-Vane N; Morales CR; Miyagi T; Pshezhetsky AV
[Ad] Address:Sainte-Justine University Hospital Research Center, University of Montreal, Montreal, Quebec, Canada.
[Ti] Title:Neuraminidases 3 and 4 regulate neuronal function by catabolizing brain gangliosides.
[So] Source:FASEB J;31(8):3467-3483, 2017 Aug.
[Is] ISSN:1530-6860
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Gangliosides (sialylated glycolipids) play an essential role in the CNS by regulating recognition and signaling in neurons. Metabolic blocks in processing and catabolism of gangliosides result in the development of severe neurologic disorders, including gangliosidoses manifesting with neurodegeneration and neuroinflammation. We demonstrate that 2 mammalian enzymes, neuraminidases 3 and 4, play important roles in catabolic processing of brain gangliosides by cleaving terminal sialic acid residues in their glycan chains. In neuraminidase 3 and 4 double-knockout mice, G ganglioside is stored in microglia, vascular pericytes, and neurons, causing micro- and astrogliosis, neuroinflammation, accumulation of lipofuscin bodies, and memory loss, whereas their cortical and hippocampal neurons have lower rate of neuritogenesis Double-knockout mice also have reduced levels of G ganglioside and myelin in neuronal axons. Furthermore, neuraminidase 3 deficiency drastically increased storage of G in the brain tissues of an asymptomatic mouse model of Tay-Sachs disease, a severe human gangliosidosis, indicating that this enzyme is responsible for the metabolic bypass of ß-hexosaminidase A deficiency. Together, our results provide the first evidence that neuraminidases 3 and 4 have important roles in CNS function by catabolizing gangliosides and preventing their storage in lipofuscin bodies.-Pan, X., De Britto Pará De Aragão, C., Velasco-Martin, J. P., Priestman, D. A., Wu, H. Y., Takahashi, K., Yamaguchi, K., Sturiale, L., Garozzo, D., Platt, F. M., Lamarche-Vane, N., Morales, C. R., Miyagi, T., Pshezhetsky, A. V. Neuraminidases 3 and 4 regulate neuronal function by catabolizing brain gangliosides.
[Mh] MeSH terms primary: Brain/metabolism
Gangliosides/metabolism
Neuraminidase/metabolism
Neurons/physiology
[Mh] MeSH terms secundary: Animals
Brain/pathology
Cells, Cultured
Embryo, Mammalian
Gene Expression Regulation, Enzymologic
Mice
Mice, Knockout
Motor Activity/physiology
Mucolipidoses/metabolism
Neuraminidase/genetics
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Gangliosides); EC 3.2.1.18 (Neu3 protein, mouse); EC 3.2.1.18 (Neu4 protein, mouse); EC 3.2.1.18 (Neuraminidase)
[Em] Entry month:1710
[Cu] Class update date: 171010
[Lr] Last revision date:171010
[Js] Journal subset:IM
[Da] Date of entry for processing:170427
[St] Status:MEDLINE
[do] DOI:10.1096/fj.201601299R

  6 / 1020 MEDLINE  
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[PMID]: 28392473
[Au] Autor:Segal P; Pode-Shakked B; Raas-Rothschild A
[Ad] Address:Department of Psychology, Hebrew University, Jerusalem, Israel.
[Ti] Title:Elucidating the behavioral phenotype of patients affected with mucolipidosis IV: What can we learn from the parents?
[So] Source:Eur J Med Genet;60(6):340-344, 2017 Jun.
[Is] ISSN:1878-0849
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:BACKGROUND: Mucolipidosis type IV (ML-IV) is a rare autosomal recessive lysosomal storage disorder which presents with nonspecific developmental delay. Nowadays with the use of new tools such as next generation sequencing, more ML-IV affected patients are diagnosed. Still, identifying the behavioral phenotype might be of help for early diagnosis and anticipatory guidance, as well as for counseling of the families. OBJECTIVE: Identification of the behavioral characteristics of 12 ML-IV patients, aged from 2.5 to 34 years, based on their caregivers' observations. METHODS: The information was gathered from the patients' parents using an extensive semi-structured interview especially designed for this study. Each interview lasted approximately three hours. RESULTS: Patients were uniformly described as friendly and show explicit pleasure from both social interactions and music. They all presented delays in psychomotor development, while their general health was reported as good. Parents reported that the patients present deterioration of motor and communication skills over the years. Episodes of ocular pain, with ipsilateral flushing of the face and tearing were frequently reported, as was shortening of the Achilles tendon. Since the identification of the ML-IV gene, diagnosis is made earlier in life. CONCLUSION: We suggest that ML-IV be considered in the differential diagnosis of patients with developmental delay, who present the behavioral phenotype reported here. This pattern could also be useful for the ancitipatory guidance in the care of ML-IV affected patients. Further clinical research is warranted to confirm these preliminary findings.
[Mh] MeSH terms primary: Child Behavior
Mucolipidoses/diagnosis
Phenotype
[Mh] MeSH terms secundary: Adolescent
Adult
Child
Child, Preschool
Diagnosis, Differential
Female
Humans
Male
Motor Skills
Mucolipidoses/genetics
Parents
Social Behavior
Transient Receptor Potential Channels/genetics
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (MCOLN1 protein, human); 0 (Transient Receptor Potential Channels)
[Em] Entry month:1708
[Cu] Class update date: 170807
[Lr] Last revision date:170807
[Js] Journal subset:IM
[Da] Date of entry for processing:170411
[St] Status:MEDLINE

  7 / 1020 MEDLINE  
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[PMID]: 28112729
[Au] Autor:Li M; Zhang WK; Benvin NM; Zhou X; Su D; Li H; Wang S; Michailidis IE; Tong L; Li X; Yang J
[Ad] Address:Department of Biological Sciences, Columbia University, New York, New York, USA.
[Ti] Title:Structural basis of dual Ca /pH regulation of the endolysosomal TRPML1 channel.
[So] Source:Nat Struct Mol Biol;24(3):205-213, 2017 Mar.
[Is] ISSN:1545-9985
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The activities of organellar ion channels are often regulated by Ca and H , which are present in high concentrations in many organelles. Here we report a structural element critical for dual Ca /pH regulation of TRPML1, a Ca -release channel crucial for endolysosomal function. TRPML1 mutations cause mucolipidosis type IV (MLIV), a severe lysosomal storage disorder characterized by neurodegeneration, mental retardation and blindness. We obtained crystal structures of the 213-residue luminal domain of human TRPML1 containing three missense MLIV-causing mutations. This domain forms a tetramer with a highly electronegative central pore formed by a novel luminal pore loop. Cysteine cross-linking and cryo-EM analyses confirmed that this architecture occurs in the full-length channel. Structure-function studies demonstrated that Ca and H interact with the luminal pore and exert physiologically important regulation. The MLIV-causing mutations disrupt the luminal-domain structure and cause TRPML1 mislocalization. Our study reveals the structural underpinnings of TRPML1's regulation, assembly and pathogenesis.
[Mh] MeSH terms primary: Calcium/metabolism
Endosomes/metabolism
Lysosomes/metabolism
TRPM Cation Channels/chemistry
TRPM Cation Channels/metabolism
[Mh] MeSH terms secundary: Amino Acids/chemistry
Crystallography, X-Ray
HEK293 Cells
Humans
Hydrogen-Ion Concentration
Models, Molecular
Mucolipidoses/genetics
Mutation, Missense
Protein Binding
Protein Multimerization
Protein Subunits/metabolism
Reproducibility of Results
Static Electricity
Structure-Activity Relationship
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Amino Acids); 0 (Protein Subunits); 0 (TRPM Cation Channels); 0 (TRPM1 protein, human); SY7Q814VUP (Calcium)
[Em] Entry month:1706
[Cu] Class update date: 171030
[Lr] Last revision date:171030
[Js] Journal subset:IM
[Da] Date of entry for processing:170124
[St] Status:MEDLINE
[do] DOI:10.1038/nsmb.3362

  8 / 1020 MEDLINE  
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[PMID]: 28065440
[Au] Autor:Kubaski F; Suzuki Y; Orii K; Giugliani R; Church HJ; Mason RW; Dung VC; Ngoc CT; Yamaguchi S; Kobayashi H; Girisha KM; Fukao T; Orii T; Tomatsu S
[Ad] Address:Nemours/Alfred I. duPont Hospital for Children, Wilmington, DE, United States; Department of Biological Sciences, University of Delaware, Newark, DE, United States; INAGEMP, Porto Alegre, Brazil.
[Ti] Title:Glycosaminoglycan levels in dried blood spots of patients with mucopolysaccharidoses and mucolipidoses.
[So] Source:Mol Genet Metab;120(3):247-254, 2017 Mar.
[Is] ISSN:1096-7206
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Mucopolysaccharidoses (MPSs) and mucolipidoses (ML) are groups of lysosomal storage disorders in which lysosomal hydrolases are deficient leading to accumulation of undegraded glycosaminoglycans (GAGs), throughout the body, subsequently resulting in progressive damage to multiple tissues and organs. Assays using tandem mass spectrometry (MS/MS) have been established to measure GAGs in serum or plasma from MPS and ML patients, but few studies were performed to determine whether these assays are sufficiently robust to measure GAG levels in dried blood spots (DBS) of patients with MPS and ML. MATERIAL AND METHODS: In this study, we evaluated GAG levels in DBS samples from 124 MPS and ML patients (MPS I=16; MPS II=21; MPS III=40; MPS IV=32; MPS VI=10; MPS VII=1; ML=4), and compared them with 115 age-matched controls. Disaccharides were produced from polymer GAGs by digestion with chondroitinase B, heparitinase, and keratanase II. Subsequently, dermatan sulfate (DS), heparan sulfate (HS-0S, HS-NS), and keratan sulfate (mono-sulfated KS, di-sulfated KS, and ratio of di-sulfated KS in total KS) were measured by MS/MS. RESULTS: Untreated patients with MPS I, II, VI, and ML had higher levels of DS compared to control samples. Untreated patients with MPS I, II, III, VI, and ML had higher levels of HS-0S; and untreated patients with MPS II, III and VI and ML had higher levels of HS-NS. Levels of KS were age dependent, so although levels of both mono-sulfated KS and di-sulfated KS were generally higher in patients, particularly for MPS II and MPS IV, age group numbers were not sufficient to determine significance of such changes. However, the ratio of di-sulfated KS in total KS was significantly higher in all MPS patients younger than 5years old, compared to age-matched controls. MPS I and VI patients treated with HSCT had normal levels of DS, and MPS I, VI, and VII treated with ERT or HSCT had normal levels of HS-0S and HS-NS, indicating that both treatments are effective in decreasing blood GAG levels. CONCLUSION: Measurement of GAG levels in DBS is useful for diagnosis and potentially for monitoring the therapeutic efficacy in MPS.
[Mh] MeSH terms primary: Dried Blood Spot Testing/methods
Glycosaminoglycans/blood
Mucolipidoses/diagnosis
Mucopolysaccharidoses/diagnosis
[Mh] MeSH terms secundary: Adolescent
Adult
Age Factors
Child
Child, Preschool
Chromatography, Liquid
Dermatan Sulfate/blood
Female
Heparitin Sulfate/blood
Humans
Infant
Infant, Newborn
Keratan Sulfate/blood
Male
Mucolipidoses/metabolism
Mucopolysaccharidoses/metabolism
Sensitivity and Specificity
Tandem Mass Spectrometry
Young Adult
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Glycosaminoglycans); 24967-94-0 (Dermatan Sulfate); 9050-30-0 (Heparitin Sulfate); 9056-36-4 (Keratan Sulfate)
[Em] Entry month:1708
[Cu] Class update date: 170829
[Lr] Last revision date:170829
[Js] Journal subset:IM
[Da] Date of entry for processing:170110
[St] Status:MEDLINE

  9 / 1020 MEDLINE  
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[PMID]: 28062798
[Au] Autor:Markmann S; Krambeck S; Hughes CJ; Mirzaian M; Aerts JM; Saftig P; Schweizer M; Vissers JP; Braulke T; Damme M
[Ad] Address:From the ‡Department of Biochemistry, Children's Hospital, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.
[Ti] Title:Quantitative Proteome Analysis of Mouse Liver Lysosomes Provides Evidence for Mannose 6-phosphate-independent Targeting Mechanisms of Acid Hydrolases in Mucolipidosis II.
[So] Source:Mol Cell Proteomics;16(3):438-450, 2017 Mar.
[Is] ISSN:1535-9484
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The efficient receptor-mediated targeting of soluble lysosomal proteins to lysosomes requires the modification with mannose 6-phosphate (M6P) residues. Although the absence of M6P results in misrouting and hypersecretion of lysosomal enzymes in many cells, normal levels of lysosomal enzymes have been reported in liver of patients lacking the M6P-generating phosphotransferase (PT). The identity of lysosomal proteins depending on M6P has not yet been comprehensively analyzed. In this study we purified lysosomes from liver of PT-defective mice and 67 known soluble lysosomal proteins were identified that illustrated quantitative changes using an ion mobility-assisted data-independent label-free LC-MS approach. After validation of various differentially expressed lysosomal components by Western blotting and enzyme activity assays, the data revealed a small number of lysosomal proteins depending on M6P, including neuraminidase 1, cathepsin F, Npc2, and cathepsin L, whereas the majority reach lysosomes by alternative pathways. These data were compared with findings on cultured hepatocytes and liver sinusoid endothelial cells isolated from the liver of wild-type and PT-defective mice. Our findings show that the relative expression, targeting efficiency and lysosomal localization of lysosomal proteins tested in cultured hepatic cells resemble their proportion in isolated liver lysosomes. Hypersecretion of newly synthesized nonphosphorylated lysosomal proteins suggest that secretion-recapture mechanisms contribute to maintain major lysosomal functions in liver.
[Mh] MeSH terms primary: Hydrolases/metabolism
Lysosomes/metabolism
Mannosephosphates/metabolism
Mucolipidoses/enzymology
Proteome/analysis
[Mh] MeSH terms secundary: Animals
Cells, Cultured
Chromatography, Liquid
Disease Models, Animal
Gene Expression Regulation
Liver/metabolism
Mass Spectrometry
Mice
Mucolipidoses/genetics
Phosphotransferases/deficiency
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Mannosephosphates); 0 (Proteome); 3672-15-9 (mannose-6-phosphate); EC 2.7.- (Phosphotransferases); EC 3.- (Hydrolases)
[Em] Entry month:1707
[Cu] Class update date: 170719
[Lr] Last revision date:170719
[Js] Journal subset:IM
[Da] Date of entry for processing:170108
[St] Status:MEDLINE
[do] DOI:10.1074/mcp.M116.063636

  10 / 1020 MEDLINE  
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[PMID]: 27797444
[Au] Autor:Ferreira CR; Devaney JM; Hofherr SE; Pollard LM; Cusmano-Ozog K
[Ad] Address:National Human Genome Research Institute, National Institutes of Health, Bethesda, Maryland.
[Ti] Title:Hereditary fructose intolerance mimicking a biochemical phenotype of mucolipidosis: A review of the literature of secondary causes of lysosomal enzyme activity elevation in serum.
[So] Source:Am J Med Genet A;173(2):501-509, 2017 Feb.
[Is] ISSN:1552-4833
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:We describe a patient with failure to thrive, hepatomegaly, liver dysfunction, and elevation of multiple plasma lysosomal enzyme activities mimicking mucolipidosis II or III, in whom a diagnosis of hereditary fructose intolerance (HFI) was ultimately obtained. She presented before introduction of solid foods, given her consumption of a fructose-containing infant formula. We present the most extensive panel of lysosomal enzyme activities reported to date in a patient with HFI, and propose that multiple enzyme elevations in plasma, especially when in conjunction with a normal plasma α-mannosidase activity, should elicit a differential diagnosis of HFI. We also performed a review of the literature on the different etiologies of elevated lysosomal enzyme activities in serum or plasma. © 2016 Wiley Periodicals, Inc.
[Mh] MeSH terms primary: Fructose Intolerance/diagnosis
Mucolipidoses/diagnosis
[Mh] MeSH terms secundary: Biomarkers/blood
Diagnosis, Differential
Enzyme Activation
Female
Fructose Intolerance/blood
Fructose Intolerance/genetics
Humans
Infant
Leukocytes/enzymology
Lysosomes/enzymology
Mucolipidoses/blood
Mucolipidoses/genetics
Phenotype
[Pt] Publication type:CASE REPORTS; JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:0 (Biomarkers)
[Em] Entry month:1710
[Cu] Class update date: 171024
[Lr] Last revision date:171024
[Js] Journal subset:IM
[Da] Date of entry for processing:161101
[St] Status:MEDLINE
[do] DOI:10.1002/ajmg.a.38023


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