Figura, Kurt von

[["dc.bibliographiccitation.firstpage","710"],["dc.bibliographiccitation.issue","4"],["dc.bibliographiccitation.journal","Biochimica et Biophysica Acta (BBA) - Molecular Cell Research"],["dc.bibliographiccitation.lastpage","725"],["dc.bibliographiccitation.volume","1793"],["dc.contributor.author","Dierks, Thomas"],["dc.contributor.author","Schlotawa, Lars"],["dc.contributor.author","Frese, Marc-Andre"],["dc.contributor.author","Radhakrishnan, Karthikeyan"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Schmidt, Bernhard"],["dc.date.accessioned","2018-11-07T08:30:52Z"],["dc.date.available","2018-11-07T08:30:52Z"],["dc.date.issued","2009"],["dc.description.abstract","Multiple sulfatase deficiency (MSD), mucolipidosis (MIL) II/III and Niemann-Pick type C1 (NPC1) disease are rare but fatal lysosomal storage disorders caused by the genetic defect of non-lysosomal proteins. The NPC1 protein mainly localizes to late endosomes and is essential for cholesterol redistribution from endocytosed LDL to cellular membranes. NPC1 deficiency leads to lysosomal accumulation of a broad range of lipids. The precise functional mechanism of this membrane protein, however, remains puzzling. ML II, also termed I cell disease. and the less severe ML III result from deficiencies of the Golgi enzyme N-acetylglucosamine 1-phosphotransferase leading to a global defect of lysosome biogenesis. In patient cells, newly synthesized lysosomal proteins are not equipped with the critical lysosomal trafficking marker mannose 6-phosphate, thus escaping from lysosomal sorting at the trans Golgi network. MSD affects the entire sulfatase family, at least seven members of which are lysosomal enzymes that are specifically involved in the degradation of sulfated glycosaminoglycans, sulfolipids or other sulfated molecules. The combined deficiencies of all sulfatases result from a defective post-translational modification by the ER-localized formylglycine-generating enzyme (FGE), which oxidizes a specific cysteine residue to formylglycine, the catalytic residue enabling a unique mechanism of sulfate ester hydrolysis. This review gives an update on the molecular bases of these enigmatic diseases, which have been challenging researchers since many decades and so far led to a number of surprising findings that give deeper insight into both the cell biology and the pathobiochemistry underlying these complex disorders. In case of MSD, considerable progress has been made in recent years towards an understanding of disease-causing FGE mutations. First approaches to link molecular parameters with clinical manifestation have been described and even therapeutical options have been addressed. Further. the discovery of FGE as an essential sulfatase activating enzyme has considerable impact on enzyme replacement or gene therapy of lysosomal storage disorders caused by single sulfatase deficiencies. (C) 2008 Elsevier B.V. All rights reserved."],["dc.identifier.doi","10.1016/j.bbamcr.2008.11.015"],["dc.identifier.isi","000265369800011"],["dc.identifier.pmid","19124046"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/16996"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Bv"],["dc.relation.issn","0167-4889"],["dc.title","Molecular basis of multiple sulfatase deficiency, mucolipidosis II/III and Niemann-Pick C1 disease - Lysosomal storage disorders caused by defects of non-lysosomal proteins"],["dc.type","review"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Journal of Bone and Mineral Research"],["dc.bibliographiccitation.volume","16"],["dc.contributor.author","Everts, V."],["dc.contributor.author","Suter, A."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Beertsen, W."],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T08:42:46Z"],["dc.date.available","2018-11-07T08:42:46Z"],["dc.date.issued","2001"],["dc.format.extent","S451"],["dc.identifier.isi","000170709001316"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/19779"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Bone & Mineral Res"],["dc.publisher.place","Washington"],["dc.relation.issn","0884-0431"],["dc.title","Acid phosphatase deficiency leads to accumulation of osteopontin in the subosteoclastic resorption area."],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","5615"],["dc.bibliographiccitation.issue","15"],["dc.bibliographiccitation.journal","Molecular and Cellular Biology"],["dc.bibliographiccitation.lastpage","5620"],["dc.bibliographiccitation.volume","26"],["dc.contributor.author","Thiel, Christian"],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Matthijs, Gert"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Koerner, Christian"],["dc.date.accessioned","2018-11-07T09:30:01Z"],["dc.date.available","2018-11-07T09:30:01Z"],["dc.date.issued","2006"],["dc.description.abstract","Mutations in the cytosolic enzyme phosphomannomutase.2 (PMM2), which catalyzes the conversion of mannose-6-phosphate to mannose-l-phosphate, cause the most common form of congenital disorders of glycosylation, termed CDG-Ia. It is an inherited multisystemic disease with severe neurological impairment. To study the pathophysiology of CDG-Ia and to investigate possible therapeutic approaches, we generated a mouse model for CDG-Ia by targeted disruption of the Pmm2 gene. Heterozygous mutant mice appeared normal in development, gross anatomy, and fertility. In contrast, embryos homozygous for the Pmm2-null allele were recovered in embryonic development at days 2.5 to 3.5. These results indicate that Pmm2 is essential for early development of mice. Mating experiments of heterozygous mice with wild-type mice could further show that transmission of the female Pmm2-null allele is impaired."],["dc.identifier.doi","10.1128/MCB.02391-05"],["dc.identifier.isi","000239286600007"],["dc.identifier.pmid","16847317"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/31202"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Amer Soc Microbiology"],["dc.relation.issn","0270-7306"],["dc.title","Targeted disruption of the mouse phosphomannomutase 2 gene causes early embryonic lethality"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.journal","Acta Paediatrica"],["dc.bibliographiccitation.volume","96"],["dc.contributor.author","von Figura, Kurt"],["dc.date.accessioned","2018-11-07T11:03:18Z"],["dc.date.available","2018-11-07T11:03:18Z"],["dc.date.issued","2007"],["dc.format.extent","5"],["dc.identifier.doi","10.1111/j.1651-2227.2007.00197.x"],["dc.identifier.isi","000245177900002"],["dc.identifier.pmid","17391431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51586"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Blackwell Publishing"],["dc.relation.issn","0803-5253"],["dc.title","Structure-function relationship for lysosomal enzymes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dc.type.subtype","letter_note"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Neurobiology of Aging"],["dc.bibliographiccitation.volume","23"],["dc.contributor.author","Hartmann, Daniel"],["dc.contributor.author","De Strooper, B."],["dc.contributor.author","Serneels, L."],["dc.contributor.author","Craessaerts, K."],["dc.contributor.author","Herreman, A."],["dc.contributor.author","Annaert, W."],["dc.contributor.author","Brabant, V."],["dc.contributor.author","Luebke, Torben"],["dc.contributor.author","Illert, A. L."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T10:23:07Z"],["dc.date.available","2018-11-07T10:23:07Z"],["dc.date.issued","2002"],["dc.format.extent","S183"],["dc.identifier.isi","000177465300670"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/42396"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Elsevier Science Inc"],["dc.publisher.place","New york"],["dc.relation.issn","0197-4580"],["dc.title","Deficiency for the disintegrin metalloprotease ADAM10 causes disturbed alpha-secretase function and a notch deficiency-related phenotype in mice"],["dc.type","conference_abstract"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","681"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","686"],["dc.bibliographiccitation.volume","8"],["dc.contributor.author","Braulke, T."],["dc.contributor.author","Tippmer, S."],["dc.contributor.author","Neher, Erwin"],["dc.contributor.author","von Figura, K."],["dc.date.accessioned","2022-03-01T11:45:56Z"],["dc.date.available","2022-03-01T11:45:56Z"],["dc.date.issued","1989"],["dc.identifier.doi","10.1002/j.1460-2075.1989.tb03426.x"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103506"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.issn","0261-4189"],["dc.title","Regulation of the mannose 6-phosphate/IGF II receptor expression at the cell surface by mannose 6-phosphate, insulin like growth factors and epidermal growth factor."],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","472"],["dc.bibliographiccitation.issue","3"],["dc.bibliographiccitation.journal","The American Journal of Human Genetics"],["dc.bibliographiccitation.lastpage","481"],["dc.bibliographiccitation.volume","74"],["dc.contributor.author","Schwarz, M."],["dc.contributor.author","Thiel, C."],["dc.contributor.author","Lubbehusen, J."],["dc.contributor.author","Dorland, B."],["dc.contributor.author","de Koning, T."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Lehle, L."],["dc.contributor.author","Korner, C."],["dc.date.accessioned","2018-11-07T10:50:25Z"],["dc.date.available","2018-11-07T10:50:25Z"],["dc.date.issued","2004"],["dc.description.abstract","The molecular nature of a severe multisystemic disorder with a recurrent nonimmune hydrops fetalis was identified as deficiency of GDP-Man: GlcNAc(2)-PP-dolichol mannosyltransferase, the human orthologue of the yeast ALG1 gene (MIM 605907). The disease belongs to the group of congenital disorders of glycosylation (CDG) and is designated as subtype CDG-Ik. In patient-derived serum, the total amount of the glycoprotein transferrin was reduced. Moreover, a partial loss of N-glycan chains was observed, a characteristic feature of CDG type I forms. Metabolic labeling with [6-H-3] glucosamine revealed an accumulation of GlcNAc(2)-PP-dolichol and GlcNAc(1)-PP-dolichol in skin fibroblasts of the patient. Incubation of fibroblast extracts with [C-14] GlcNAc(2)-PP-dolichol and GDP-mannose indicated a severely reduced activity of the beta1,4- mannosyltransferase, elongating GlcNAc(2)-PP-dol-ichol to Man1 GlcNAc(2)-PP-dolichol at the cytosolic side of the endoplasmic reticulum. Genetic analysis of the patient's hALG1 gene identified a homozygous mutation leading to the exchange of a serine residue to leucine at position 258 in the hALG1 protein. The disease-causing nature of the hALG1 mutation for the glycosylation defect was verified by a retroviral complementation approach in patient-derived primary fibroblasts and was confirmed by the expression of wild-type and mutant hALG1 in the Saccharomyces cerevisiae alg1-1 strain."],["dc.identifier.doi","10.1086/382492"],["dc.identifier.isi","000220118500014"],["dc.identifier.pmid","14973778"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/48645"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Univ Chicago Press"],["dc.relation.issn","0002-9297"],["dc.title","Deficiency of GDP-Man : GlcNAc(2)-PP-dolichol mannosyltransferase causes congenital disorder of glycosylation type Ik"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","185"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Journal of Cell Science"],["dc.bibliographiccitation.lastpage","194"],["dc.bibliographiccitation.volume","115"],["dc.contributor.author","Obermuller, S."],["dc.contributor.author","Kiecke, Christina"],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Honing, S."],["dc.date.accessioned","2018-11-07T10:33:18Z"],["dc.date.available","2018-11-07T10:33:18Z"],["dc.date.issued","2002"],["dc.description.abstract","Lamp 1 and lysosomal acid phosphatase (LAP) are lysosomal membrane proteins that harbour a tyrosine-based sorting motif within their short cytoplasmic tails. Lamp 1 is delivered from the trans-Golgi network (TGN) via endosomes directly to lysosomes bypassing the plasma membrane, whereas LAP is indirectly transported to lysosomes and recycles between endosomes and the plasma membrane before being delivered to lysosomes. By analysing truncated forms of LAP and chimeras in which the cytoplasmic tail or part of the cytoplasmic tails of LAP and Lamp 1 were exchanged, we were able to show that the YRHV tyrosine motif of LAP is necessary and sufficient to mediate recycling between endosomes and the plasma membrane. When peptides corresponding to the cytoplasmic tails of LAP and Lamp 1 and chimeric or mutant forms of these tails were assayed for in vitro binding of AP1 and AP2, we found that AP2 bound to LAP- and Lamp-1-derived peptides, whereas AP1 bound only to peptides containing the YQTI tyrosine motif of Lamp 1. Residues +2 and +3 of the tyrosine motif were critical for the differential binding of adaptors. LAP in which these residues (-HV) were substituted for those of Lamp 1 (-TI) was transported directly to lysosomes, whereas a chimera carrying the Lamp 1 tail in which residues +2 and +3 were substituted for those of LAP (-HV) gained the ability to recycle. In conclusion, the residues +2 and +3 of the tyrosine motifs determine the sorting of Lamp 1 and LAP in endosomes, mediating either the direct or the indirect pathway to lysosomes."],["dc.identifier.isi","000173486200021"],["dc.identifier.pmid","11801736"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/44578"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Company Of Biologists Ltd"],["dc.relation.issn","0021-9533"],["dc.title","The tyrosine motifs of Lamp 1 and LAP determine their direct and indirect targetting to lysosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","60"],["dc.bibliographiccitation.issue","2"],["dc.bibliographiccitation.journal","Neuropediatrics"],["dc.bibliographiccitation.lastpage","62"],["dc.bibliographiccitation.volume","31"],["dc.contributor.author","Hanefeld, Folker"],["dc.contributor.author","Korner, C."],["dc.contributor.author","Holzbach-Eberle, U."],["dc.contributor.author","von Figura, Kurt"],["dc.date.accessioned","2018-11-07T11:24:18Z"],["dc.date.available","2018-11-07T11:24:18Z"],["dc.date.issued","2000"],["dc.description.abstract","The clinical phenotype and the molecular defect of a patient with a new subtype of congenital disorders of glycosylation (CDC-lc, formerly designated as CDGS type V) characterized by a deficiency of Dol-P-Glc:Man(9)GlcNAc(2)-PP-Dol glucosyltransferase is described. The clinical picture presents with several features similar to CDC-la (phosphomannomutase 2 deficiency) such as hypotonia and atactic-dystonic movements. In contrast to CDG-1a, the course of the disease appears milder. The head growth, the functioning of the peripheral nerves and the initial cerebellar development were normal. Sequencing of the patient's Dol-P-Clc:Man(9)GlcNAc(2)-PP-Dol glucosyltransferase cDNA revealed an in-frame deletion of three nucleotides leading to the loss of isoleucine 299."],["dc.identifier.doi","10.1055/s-2000-7486"],["dc.identifier.isi","000088299200002"],["dc.identifier.pmid","10832578"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/56370"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Georg Thieme Verlag"],["dc.relation.issn","0174-304X"],["dc.title","Congenital disorder of glycosylation-Ic: Case report and genetic defect"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","897"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","Cell Biology International"],["dc.bibliographiccitation.lastpage","902"],["dc.bibliographiccitation.volume","27"],["dc.contributor.author","Schellens, JPM"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Everts, V."],["dc.date.accessioned","2018-11-07T10:42:09Z"],["dc.date.available","2018-11-07T10:42:09Z"],["dc.date.issued","2003"],["dc.description.abstract","Transport of lysosomal enzymes is mediated by two mannose 6-phosphate receptors: a cation dependent (CD-MPR) and a cation independent receptor (CI-MPR). In the present study the effect of MPR-deficiency on the lysosomal system of neonatal mouse hepatocytes was studied by ultrastructural morphometric analyses. The volume density of the lysosomal system in hepatocytes of mice that lack both receptors was significantly increased in comparison with controls and with mice deficient for CI-MPR only. This higher volume density was due to a nine-fold increase of residual bodies. In CI-MPR-deficient mice the volume density of the lysosomal system was not different from controls and no increase of residual bodies was observed. It is concluded that in hepatocytes of MPR-deficient neonatal mice lysosomal storage occurs when both MPRs are lacking, whereas deficiency of CI-MPR only has no effect on the ultrastructure of the lysosomal system. (C) 2003 Elsevier Ltd. All rights reserved."],["dc.identifier.doi","10.1016/j.cellbi.2003.07.001"],["dc.identifier.isi","000186532600002"],["dc.identifier.pmid","14585283"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/46721"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Academic Press Ltd Elsevier Science Ltd"],["dc.relation.issn","1065-6995"],["dc.title","Deficiency of mannose 6-phosphate receptors and lysosomal storage: a morphometric analysis of hepatocytes of neonatal mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.status","published"],["dspace.entity.type","Publication"]]