Figura, Kurt von

[["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","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"]]

[["dc.bibliographiccitation.firstpage","4899"],["dc.bibliographiccitation.issue","23"],["dc.bibliographiccitation.journal","Development"],["dc.bibliographiccitation.lastpage","4910"],["dc.bibliographiccitation.volume","128"],["dc.contributor.author","Suter, A."],["dc.contributor.author","Everts, V."],["dc.contributor.author","Boyde, A."],["dc.contributor.author","Jones, S. J."],["dc.contributor.author","Lullmann-Rauch, R."],["dc.contributor.author","Hartmann, Daniel"],["dc.contributor.author","Hayman, A. R."],["dc.contributor.author","Cox, T. M."],["dc.contributor.author","Evans, M. J."],["dc.contributor.author","Meister, T."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.author","Saftig, P."],["dc.date.accessioned","2018-11-07T11:20:43Z"],["dc.date.available","2018-11-07T11:20:43Z"],["dc.date.issued","2001"],["dc.description.abstract","To date, two lysosomal acid phosphatases are known to be expressed in cells of the monocyte/phagocyte lineage: the ubiquitously expressed lysosomal acid phosphatase (LAP) and the tartrate-resistant acid phosphatase-type 5 (Acp5). Deficiency of either acid phosphatase results in relatively mild phenotypes, suggesting that these enzymes may be capable of mutual complementation. This prompted us to generate LAP/Acp5 doubly deficient mice. LAP/Acp5 doubly deficient mice are viable and fertile but display marked alterations in soft and mineralised tissues. They are characterised by a progressive hepatosplenomegaly, gait disturbances and exaggerated foreshortening of long bones. Histologically, these animals are distinguished by an excessive lysosomal storage in macrophages of the liver, spleen, bone marrow, kidney and by altered growth plates. Microscopic analyses showed an accumulation of osteopontin adjacent to actively resorbing osteoclasts of Acp5- and LAP/Acp5-deficient mice. In osteoclasts of phosphatase-deficient mice, vacuoles were frequently found which contained fine filamentous material. The vacuoles in Acp5- and LAP/Acp5 doubly-deficient osteoclasts also contained crystallite-Iike features, as well as osteopontin, suggesting that Acp5 is important for processing of this protein. This is further supported by biochemical analyses that demonstrate strongly reduced dephosphorylation of osteopontin incubated with LAP/Acp5-deficient bone extracts. Fibroblasts derived from LAP/Acp5 deficient embryos were still able to dephosphorylate mannose 6-phosphate residues of endocytosed arylsulfatase A. We conclude that for several substrates LAP and Acp5 can substitute for each other and that these acid phosphatases are essential for processing of non-collagenous proteins, including osteopontin, by osteoclasts."],["dc.identifier.isi","000172740900022"],["dc.identifier.pmid","11731469"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/55608"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.relation.issn","0950-1991"],["dc.title","Overlapping functions of lysosomal acid phosphatase (LAP) and tartrate-resistant acid phosphatase (Acp5) revealed by doubly deficient mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","293"],["dc.bibliographiccitation.lastpage","303"],["dc.bibliographiccitation.seriesnr","477"],["dc.contributor.author","Saftig, P."],["dc.contributor.author","Hunziker, Ernst B."],["dc.contributor.author","Everts, V."],["dc.contributor.author","Jones, Simon"],["dc.contributor.author","Boyde, A."],["dc.contributor.author","Wehmeyer, O."],["dc.contributor.author","Suter, A."],["dc.contributor.author","von Figura, Kurt"],["dc.contributor.editor","Langner, Jürgen"],["dc.contributor.editor","Ansorge, Siegfried"],["dc.date.accessioned","2018-11-07T11:02:03Z"],["dc.date.available","2018-11-07T11:02:03Z"],["dc.date.issued","2000"],["dc.description.abstract","Cathepsin K is a cysteine proteinase expressed predominantly in osteoclasts. Cathepsin K cleaves key bone matrix proteins and is believed to play an important role in degrading the organic phase of bone during bone resorption. Pycnodysostosis, an autosomal recessive osteosclerosing skeletal disorder has recently been shown to result from mutations in the cathepsin K gene. Cathepsin K deficient mice generated by targeted disruption of this proteinase phenocopy many aspects of pycnodysostosis. They display an osteopetrotic phenotype with excessive trabeculation of the bone-marrow space accompanied by an altered ultrastructural appearance of the cathepsin K deficient osteoclasts. These cells also demonstrate an impaired resorptive activity in vitro. In contrast to other forms of osteopetrosis, which are due to disrupted osteoclastogenesis, cathepsin K deficiency is associated with an inhibition of osteoclast activity. Taken together the phenotype of cathepsin K knockout mice underlines the importance of this proteinase in bone remodelling."],["dc.identifier.doi","10.1007/0-306-46826-3_32"],["dc.identifier.isi","000087923000032"],["dc.identifier.pmid","10849757"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/51290"],["dc.language.iso","en"],["dc.notes.status","zu prüfen"],["dc.notes.submitter","Najko"],["dc.publisher","Kluwer Academic / Plenum Publ"],["dc.publisher.place","New York"],["dc.relation.conference","International Conference on Cellular Peptidases in Immune Functions and Diseases II"],["dc.relation.crisseries","Advances in Experimental Medicine and Biology"],["dc.relation.doi","10.1007/0-306-46826-3"],["dc.relation.eventlocation","Magdeburg"],["dc.relation.eventstart","1999"],["dc.relation.isbn","0-306-46383-0"],["dc.relation.isbn","1-280-04290-7"],["dc.relation.ispartof","Cellular peptidases in immune functions and diseases 2"],["dc.relation.ispartofseries","Advances in experimental medicine and biology; 477"],["dc.relation.issn","0065-2598"],["dc.title","Functions of cathepsin K in bone resorption - Lessons from cathepsin K deficient mice"],["dc.type","conference_paper"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dspace.entity.type","Publication"]]