Database : MEDLINE
Search on : Oculocerebrorenal and Syndrome [Words]
References found : 391 [refine]
Displaying: 1 .. 10   in format [Detailed]

page 1 of 40 go to page                         

  1 / 391 MEDLINE  
              next record last record
select
to print
Photocopy
Full text

[PMID]: 29226564
[Au] Autor:Abdalla E; El-Beheiry A; Dieterich K; Thevenon J; Fauré J; Rendu J
[Ad] Address:Department of Human Genetics, Medical Research Institute, Alexandria University, Alexandria, Egypt.
[Ti] Title:"Lowe syndrome: A particularly severe phenotype without clinical kidney involvement".
[So] Source:Am J Med Genet A;176(2):460-464, 2018 Feb.
[Is] ISSN:1552-4833
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Lowe syndrome (LS) is a very rare disorder of phosphatidylinositol metabolism, which manifests with a complex phenotype comprising a clinical triad encompassing major abnormalities of the eyes, the kidneys, and the central nervous system. We are reporting a 23-year-old Egyptian male with a severe phenotype of LS with a minimal kidney disease. Direct sequencing of the OCRL gene detected a p.His375Arg mutation in the catalytic domain of the protein. The patient suffered from bilateral congenital cataracts and glaucoma, striking growth deficiency, severe psychomotor disability, a severe osteopathy, and seizures, but only minimal renal dysfunction. Although the biological mechanisms underlying the pathophysiology of LS manifestations is yet unclear, it has been proposed that growth delay and osteopathy are linked to a renal dysfunction. This report, however, argues this association and suggests that kidney dysfunction may partially explain the growth deficiency and bone abnormalities, but other still undefined factors might have a potential impact.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1712
[Cu] Class update date: 180115
[Lr] Last revision date:180115
[St] Status:In-Data-Review
[do] DOI:10.1002/ajmg.a.38572

  2 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 29028801
[Au] Autor:Del Signore SJ; Biber SA; Lehmann KS; Heimler SR; Rosenfeld BH; Eskin TL; Sweeney ST; Rodal AA
[Ad] Address:Rosenstiel Basic Medical Sciences Research Center, Department of Biology, Brandeis University, Waltham, Massachusetts, United States of America.
[Ti] Title:dOCRL maintains immune cell quiescence by regulating endosomal traffic.
[So] Source:PLoS Genet;13(10):e1007052, 2017 Oct.
[Is] ISSN:1553-7404
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Lowe Syndrome is a developmental disorder characterized by eye, kidney, and neurological pathologies, and is caused by mutations in the phosphatidylinositol-5-phosphatase OCRL. OCRL plays diverse roles in endocytic and endolysosomal trafficking, cytokinesis, and ciliogenesis, but it is unclear which of these cellular functions underlie specific patient symptoms. Here, we show that mutation of Drosophila OCRL causes cell-autonomous activation of hemocytes, which are macrophage-like cells of the innate immune system. Among many cell biological defects that we identified in docrl mutant hemocytes, we pinpointed the cause of innate immune cell activation to reduced Rab11-dependent recycling traffic and concomitantly increased Rab7-dependent late endosome traffic. Loss of docrl amplifies multiple immune-relevant signals, including Toll, Jun kinase, and STAT, and leads to Rab11-sensitive mis-sorting and excessive secretion of the Toll ligand Spåtzle. Thus, docrl regulation of endosomal traffic maintains hemocytes in a poised, but quiescent state, suggesting mechanisms by which endosomal misregulation of signaling may contribute to symptoms of Lowe syndrome.
[Mh] MeSH terms primary: Cytokinesis/genetics
Immunity, Innate/genetics
Oculocerebrorenal Syndrome/genetics
Phosphoric Monoester Hydrolases/genetics
[Mh] MeSH terms secundary: Animals
Drosophila
Endosomes/genetics
Endosomes/pathology
Hemocytes/metabolism
Hemocytes/pathology
Humans
Mutation
Oculocerebrorenal Syndrome/pathology
Protein Binding
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (OCRL protein, human)
[Em] Entry month:1711
[Cu] Class update date: 171111
[Lr] Last revision date:171111
[Js] Journal subset:IM
[Da] Date of entry for processing:171014
[St] Status:MEDLINE
[do] DOI:10.1371/journal.pgen.1007052

  3 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28923975
[Au] Autor:Daste F; Walrant A; Holst MR; Gadsby JR; Mason J; Lee JE; Brook D; Mettlen M; Larsson E; Lee SF; Lundmark R; Gallop JL
[Ad] Address:Wellcome Trust/Cancer Research UK Gurdon Institute and Department of Biochemistry, University of Cambridge, Cambridge, England, UK.
[Ti] Title:Control of actin polymerization via the coincidence of phosphoinositides and high membrane curvature.
[So] Source:J Cell Biol;216(11):3745-3765, 2017 Nov 06.
[Is] ISSN:1540-8140
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:The conditional use of actin during clathrin-mediated endocytosis in mammalian cells suggests that the cell controls whether and how actin is used. Using a combination of biochemical reconstitution and mammalian cell culture, we elucidate a mechanism by which the coincidence of PI(4,5)P and PI(3)P in a curved vesicle triggers actin polymerization. At clathrin-coated pits, PI(3)P is produced by the INPP4A hydrolysis of PI(3,4)P , and this is necessary for actin-driven endocytosis. Both Cdc42â‹…guanosine triphosphate and SNX9 activate N-WASP-WIP- and Arp2/3-mediated actin nucleation. Membrane curvature, PI(4,5)P , and PI(3)P signals are needed for SNX9 assembly via its PX-BAR domain, whereas signaling through Cdc42 is activated by PI(4,5)P alone. INPP4A activity is stimulated by high membrane curvature and synergizes with SNX9 BAR domain binding in a process we call curvature cascade amplification. We show that the SNX9-driven actin comets that arise on human disease-associated oculocerebrorenal syndrome of Lowe (OCRL) deficiencies are reduced by inhibiting PI(3)P production, suggesting PI(3)P kinase inhibitors as a therapeutic strategy in Lowe syndrome.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171110
[Lr] Last revision date:171110
[St] Status:In-Process
[do] DOI:10.1083/jcb.201704061

  4 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28871046
[Au] Autor:Prosseda PP; Luo N; Wang B; Alvarado JA; Hu Y; Sun Y
[Ad] Address:Stanford University, Department of Ophthalmology, 1651 Page Mill Road, Rm 2220, Palo Alto, CA 94304, USA.
[Ti] Title:Loss of OCRL increases ciliary PI(4,5)P in Lowe oculocerebrorenal syndrome.
[So] Source:J Cell Sci;130(20):3447-3454, 2017 Oct 15.
[Is] ISSN:1477-9137
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Lowe syndrome is a rare X-linked disorder characterized by bilateral congenital cataracts and glaucoma, mental retardation, and proximal renal tubular dysfunction. Mutations in OCRL, an inositol polyphosphate 5-phosphatase that dephosphorylates PI(4,5)P , cause Lowe syndrome. Previously we showed that OCRL localizes to the primary cilium, which has a distinct membrane phospholipid composition, but disruption of phosphoinositides in the ciliary membrane is poorly understood. Here, we demonstrate that cilia from Lowe syndrome patient fibroblasts exhibit increased levels of PI(4,5)P and decreased levels of PI4P. In particular, subcellular distribution of PI(4,5)P build-up was observed at the transition zone. Accumulation of ciliary PI(4,5)P was pronounced in mouse embryonic fibroblasts (MEFs) derived from Lowe syndrome mouse model as well as in -null MEFs, which was reversed by reintroduction of OCRL. Similarly, expression of wild-type OCRL reversed the elevated PI(4,5)P in Lowe patient cells. Accumulation of sonic hedgehog protein in response to hedgehog agonist was decreased in MEFs derived from a Lowe syndrome mouse model. Together, our findings show for the first time an abnormality in ciliary phosphoinositides of both human and mouse cell models of Lowe syndrome.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1709
[Cu] Class update date: 171016
[Lr] Last revision date:171016
[St] Status:In-Process
[do] DOI:10.1242/jcs.200857

  5 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28803024
[Au] Autor:Nakanishi K; Nozu K; Hiramoto R; Minamikawa S; Yamamura T; Fujimura J; Horinouchi T; Ninchoji T; Kaito H; Morisada N; Ishimori S; Nakanishi K; Morioka I; Awano H; Matsuo M; Iijima K
[Ad] Address:Department of Pediatrics, Kobe University Graduate School of Medicine, Kobe, Japan.
[Ti] Title:A comparison of splicing assays to detect an intronic variant of the OCRL gene in Lowe syndrome.
[So] Source:Eur J Med Genet;60(12):631-634, 2017 Dec.
[Is] ISSN:1878-0849
[Cp] Country of publication:Netherlands
[La] Language:eng
[Ab] Abstract:Lowe syndrome is an X-linked inherited disorder diagnosed by congenital cataracts, intellectual impairment, and renal tubular dysfunction. It is caused by pathogenic variants of the oculocerebrorenal syndrome of Lowe gene (OCRL), of which more than 250 have been reported so far. Around 30 of these variants are intronic nucleotide changes; however, to show the pathogenicity of these variants is usually laborious. In this report, we conducted genetic testing of a patient clinically diagnosed with Lowe syndrome to detect the presence of OCRL variants. We analyzed variant transcript expression in peripheral blood leukocytes and using a minigene construct in addition to in silico analysis. We detected a 9 base pair intronic insertion between OCRL exon 10 and exon 11 derived from the alteration of the splicing acceptor site in intron 10 caused by the intronic splicing variant NM_000276.3: c.940-11G>A (p.Lys313_Val314insAsnSer*). The findings obtained from transcript analysis of peripheral blood leukocytes and the minigene construct assay were identical to those of in silico analysis. All assays detected the same transcript abnormality and were reliable in revealing the pathogenicity of the intronic variant. The in vitro assay can also be used to clarify the complicated splicing mechanisms in inherited kidney diseases.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1708
[Cu] Class update date: 171120
[Lr] Last revision date:171120
[St] Status:In-Process

  6 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28739877
[Au] Autor:Sun HM; Chen XL; Chen XJ; Liu J; Ma L; Wu HY; Huang QH; Xi XD; Yin T; Zhu J; Chen Z; Chen SJ
[Ad] Address:State Key Laboratory of Medical Genomics, Shanghai Institute of Hematology, RuiJin Hospital Affiliated to Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China.
[Ti] Title:PALLD Regulates Phagocytosis by Enabling Timely Actin Polymerization and Depolymerization.
[So] Source:J Immunol;199(5):1817-1826, 2017 Sep 01.
[Is] ISSN:1550-6606
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:PALLD is an actin cross-linker supporting cellular mechanical tension. However, its involvement in the regulation of phagocytosis, a cellular activity essential for innate immunity and physiological tissue turnover, is unclear. We report that is highly induced along with all- -retinoic acid-induced maturation of myeloid leukemia cells, to promote Ig- or complement-opsonized phagocytosis. PALLD mechanistically facilitates phagocytic receptor clustering by regulating actin polymerization and c-Src dynamic activation during particle binding and early phagosome formation. PALLD is also required at the nascent phagosome to recruit phosphatase oculocerebrorenal syndrome of Lowe, which regulates phosphatidylinositol-4,5-bisphosphate hydrolysis and actin depolymerization to complete phagosome closure. Collectively, our results show a new function for PALLD as a crucial regulator of the early phase of phagocytosis by elaborating dynamic actin polymerization and depolymerization.
[Mh] MeSH terms primary: Actins/metabolism
Cytoskeletal Proteins/metabolism
Dendritic Cells/immunology
Leukemia, Myeloid, Acute/immunology
Neoplastic Stem Cells/physiology
Oculocerebrorenal Syndrome/immunology
Phagocytosis
Phosphoproteins/metabolism
[Mh] MeSH terms secundary: Animals
Cell Differentiation
Cell Line, Tumor
Cell Self Renewal
Cytoskeletal Proteins/genetics
Humans
Immunity, Innate
Mice
Mice, Inbred C57BL
Phagosomes/metabolism
Phosphoproteins/genetics
Phosphoric Monoester Hydrolases/metabolism
Polymerization
Receptor Aggregation
Tretinoin/metabolism
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:0 (Actins); 0 (Cytoskeletal Proteins); 0 (Phosphoproteins); 0 (palladin protein, human); 5688UTC01R (Tretinoin); EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (phosphoinositide 5-phosphatase)
[Em] Entry month:1709
[Cu] Class update date: 170929
[Lr] Last revision date:170929
[Js] Journal subset:AIM; IM
[Da] Date of entry for processing:170726
[St] Status:MEDLINE
[do] DOI:10.4049/jimmunol.1602018

  7 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28669993
[Au] Autor:De Matteis MA; Staiano L; Emma F; Devuyst O
[Ad] Address:Telethon Institute of Genetics and Medicine, Via Campi Flegrei 34, 80078, Pozzuoli, Italy.
[Ti] Title:The 5-phosphatase OCRL in Lowe syndrome and Dent disease 2.
[So] Source:Nat Rev Nephrol;13(8):455-470, 2017 Aug.
[Is] ISSN:1759-507X
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Lowe syndrome is an X-linked disease that is characterized by congenital cataracts, central hypotonia, intellectual disability and renal Fanconi syndrome. The disease is caused by mutations in OCRL, which encodes an inositol polyphosphate 5-phosphatase (OCRL) that acts on phosphoinositides - quantitatively minor constituents of cell membranes that are nonetheless pivotal regulators of intracellular trafficking. In this Review we summarize the considerable progress made over the past decade in understanding the cellular roles of OCRL in regulating phosphoinositide balance along the endolysosomal pathway, a fundamental system for the reabsorption of proteins and solutes by proximal tubular cells. We discuss how studies of OCRL have led to important discoveries about the basic mechanisms of membrane trafficking and describe the key features and limitations of the currently available animal models of Lowe syndrome. Mutations in OCRL can also give rise to a milder pathology, Dent disease 2, which is characterized by renal Fanconi syndrome in the absence of extrarenal pathologies. Understanding how mutations in OCRL give rise to two clinical entities with differing extrarenal manifestations represents an opportunity to identify molecular pathways that could be targeted to develop treatments for these conditions.
[Mh] MeSH terms primary: Genetic Diseases, X-Linked/genetics
Mutation
Nephrolithiasis/genetics
Oculocerebrorenal Syndrome/genetics
Phosphoric Monoester Hydrolases/genetics
[Mh] MeSH terms secundary: Animals
Clathrin-Coated Vesicles
Disease Models, Animal
Endocytosis
Humans
Inositol Polyphosphate 5-Phosphatases/genetics
Kidney Tubules, Proximal/cytology
[Pt] Publication type:JOURNAL ARTICLE; REVIEW
[Nm] Name of substance:EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (OCRL protein, human); EC 3.1.3.56 (Inositol Polyphosphate 5-Phosphatases)
[Em] Entry month:1708
[Cu] Class update date: 170817
[Lr] Last revision date:170817
[Js] Journal subset:IM
[Da] Date of entry for processing:170704
[St] Status:MEDLINE
[do] DOI:10.1038/nrneph.2017.83

  8 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28473699
[Au] Autor:Song E; Luo N; Alvarado JA; Lim M; Walnuss C; Neely D; Spandau D; Ghaffarieh A; Sun Y
[Ad] Address:Department of Ophthalmology, Indiana University, Indianapolis, IN, USA.
[Ti] Title:Ocular Pathology of Oculocerebrorenal Syndrome of Lowe: Novel Mutations and Genotype-Phenotype Analysis.
[So] Source:Sci Rep;7(1):1442, 2017 May 04.
[Is] ISSN:2045-2322
[Cp] Country of publication:England
[La] Language:eng
[Ab] Abstract:Mutations in the OCRL1 gene result in the oculocerebrorenal syndrome of Lowe, with symptoms including congenital bilateral cataracts, glaucoma, renal failure, and neurological impairments. OCRL1 encodes an inositol polyphosphate 5-phosphatase which preferentially dephosphorylates phosphatidylinositide 4,5 bisphosphate (PI(4,5)P ). We have identified two novel mutations in two unrelated Lowe syndrome patients with congenital glaucoma. Novel deletion mutations are detected at c.739-742delAAAG in Lowe patient 1 and c.1595-1631del in Lowe patient 2. End stage glaucoma in patient 2 resulted in the enucleation of the eye, which on histology demonstrated corneal keloid, fibrous infiltration of the angle, ectropion uvea, retinal gliosis, and retinal ganglion cell loss. We measured OCRL protein levels in patient keratinocytes and found that Lowe 1 patient cells had significantly reduced OCRL protein as compared to the control keratinocytes. Genotype-phenotype correlation of OCRL1 mutations associated with congenital glaucoma revealed clustering of missense and deletion mutations in the 5-phosphatase domain and the RhoGAP-like domain. In conclusion, we report novel OCRL1 mutations in Lowe syndrome patients and the corresponding histopathologic analysis of one patient's ocular pathology.
[Pt] Publication type:JOURNAL ARTICLE
[Em] Entry month:1705
[Cu] Class update date: 170714
[Lr] Last revision date:170714
[St] Status:In-Data-Review
[do] DOI:10.1038/s41598-017-01447-3

  9 / 391 MEDLINE  
              first record previous record next record last record
select
to print
Photocopy
Full text

[PMID]: 28397227
[Au] Autor:Zhu X; Li J; Ru T; Zhu R; Dai C; Wang W; Hu Y
[Ad] Address:Prenatal Diagnosis Center of Jiangsu Province, Drum Tower Hospital Affiliated to Nanjing University Medical School, Nanjing, Jiangsu 210008, China. glyyhuyali@163.com.
[Ti] Title:[Prenatal diagnosis and follow-up of a case with Lowe syndrome caused by interstitial deletion of Xq25-26].
[So] Source:Zhonghua Yi Xue Yi Chuan Xue Za Zhi;34(2):236-239, 2017 Apr 10.
[Is] ISSN:1003-9406
[Cp] Country of publication:China
[La] Language:chi
[Ab] Abstract:OBJECTIVE: To report on a sporadic case of Lowe syndrome diagnosed prenatally with ultrasound examination and genetic testing. METHODS: Detailed sonographic fetal screening was performed by an experienced sonographer at 32 weeks of gestation. Fetal cranial magnetic resonance imaging (MRI) was applied to detect potential brain abnormality. Chromosomal microarray analysis (CMA) was conducted on amniotic fluid sample from the fetus and peripheral blood sample from the mother. RESULTS: Congenital cataract and enlarged posterior fossa were detected by fetal ultrasound screening. Fetal cranial MRI found hypoplasia of the gyrus. CMA revealed that the fetus has carried a 633 kb deletion at Xq25-26.1 which encompassed the OCRL gene. The mother was a carrier of the same deletion. Clinical examination after birth confirmed that the neonate was affected with Lowe syndrome in addition with an atrial septal defect. CONCLUSION: Prenatal diagnosis of Lowe syndrome without a family history largely depends on fetal imaging. Should cataract be found by ultrasound screening, fetal MRI may be considered to rule out central nervous system anomalies. CMA assay should also be considered to facilitate the diagnosis.
[Mh] MeSH terms primary: Fetal Diseases/genetics
Oculocerebrorenal Syndrome/genetics
[Mh] MeSH terms secundary: Adult
Child
Child, Preschool
Chromosome Deletion
Chromosomes, Human, X/genetics
Female
Fetal Diseases/diagnosis
Humans
Infant
Male
Microarray Analysis
Oculocerebrorenal Syndrome/diagnosis
Oculocerebrorenal Syndrome/embryology
Phosphoric Monoester Hydrolases/genetics
Pregnancy
Prenatal Diagnosis
Ultrasonography, Prenatal
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (OCRL protein, human)
[Em] Entry month:1709
[Cu] Class update date: 170914
[Lr] Last revision date:170914
[Js] Journal subset:IM
[Da] Date of entry for processing:170412
[St] Status:MEDLINE
[do] DOI:10.3760/cma.j.issn.1003-9406.2017.02.019

  10 / 391 MEDLINE  
              first record previous record
select
to print
Photocopy
Full text

[PMID]: 27895154
[Au] Autor:Inoue K; Balkin DM; Liu L; Nandez R; Wu Y; Tian X; Wang T; Nussbaum R; De Camilli P; Ishibe S
[Ad] Address:Departments of Internal Medicine.
[Ti] Title:Kidney Tubular Ablation of / Phenocopies Lowe Syndrome Tubulopathy.
[So] Source:J Am Soc Nephrol;28(5):1399-1407, 2017 May.
[Is] ISSN:1533-3450
[Cp] Country of publication:United States
[La] Language:eng
[Ab] Abstract:Lowe syndrome and Dent disease are two conditions that result from mutations of the inositol 5-phosphatase oculocerebrorenal syndrome of Lowe (OCRL) and share the feature of impaired kidney proximal tubule function. Genetic ablation of in mice failed to recapitulate the human phenotypes, possibly because of the redundant functions of OCRL and its paralog type 2 inositol polyphosphate-5-phosphatase (INPP5B). Germline knockout of both paralogs in mice results in early embryonic lethality. We report that kidney tubule-specific inactivation of on a global -knockout mouse background resulted in low molecular weight proteinuria, phosphaturia, and acidemia. At the cellular level, we observed a striking impairment of clathrin-dependent and -independent endocytosis in proximal tubules, phenocopying what has been reported for Dent disease caused by mutations in the gene encoding endosomal proton-chloride exchange transporter 5. These results suggest that the functions of OCRL/INPP5B and proton-chloride exchange transporter 5 converge on shared mechanisms, the impairment of which has a dramatic effect on proximal tubule endocytosis.
[Mh] MeSH terms primary: Kidney Tubules, Proximal
Mutation
Oculocerebrorenal Syndrome/genetics
Phenotype
Phosphoric Monoester Hydrolases/genetics
[Mh] MeSH terms secundary: Animals
Humans
Mice
Mice, Knockout
[Pt] Publication type:JOURNAL ARTICLE
[Nm] Name of substance:EC 3.1.3.2 (Phosphoric Monoester Hydrolases); EC 3.1.3.36 (Ocrl protein, mouse); EC 3.1.3.36 (phosphoinositide 5-phosphatase)
[Em] Entry month:1705
[Cu] Class update date: 170531
[Lr] Last revision date:170531
[Js] Journal subset:IM
[Da] Date of entry for processing:161130
[St] Status:MEDLINE
[do] DOI:10.1681/ASN.2016080913


page 1 of 40 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