Figura, Kurt von

[["dc.bibliographiccitation.firstpage","2343"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2350"],["dc.bibliographiccitation.volume","7"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Krentler, Christiane"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Schröder, Wolfgang"],["dc.contributor.author","Lorkowski, Gerhard"],["dc.contributor.author","Culley, Jan"],["dc.contributor.author","Mersmann, Guenther"],["dc.contributor.author","Geier, Carola"],["dc.contributor.author","Waheed, Abdul"],["dc.contributor.author","Gottschalk, Stephen"],["dc.contributor.author","Grzeschik, Karl-Heinz"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:44Z"],["dc.date.available","2019-07-10T08:12:44Z"],["dc.date.issued","1988"],["dc.description.abstract","A 2112-bp cDNA clone (λCT29) encoding the entire sequence of the human lysosomal acid phosphatase (EC 3.1.3.2) was isolated from a λgt11 human placenta cDNA library. The cDNA hybridized with a 2.3-kb mRNA from human liver and HL-60 promyelocytes. The gene for lysosomal acid phosphatase was localized to human chromosome 11. The cDNA includes a 12-bp 5' noncoding region, an open reading frame of 1269 bp and an 831-bp 3' non-coding region with a putative polyadenylation signal 25 bp upstream of a 3' poly(A) tract. The deduced amino acid sequence reveals a putative signal sequence of 30 amino acids followed by a sequence of 393 amino acids that contains eight potential glycosylation sites and a hydrophobic region, which could function as a transmembrane domain. A 60% homology between the known 23 N-terminal amino acid residues of human prostatic acid phosphatase and the N-terminal sequence of lysosomal acid phosphatase suggests an evolutionary link between these two phosphatases. Insertion of the cDNA into the expression vector pSVL yielded a construct that encoded enzymatically active acid phosphatase in transfected monkey COS cells."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3431"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61020"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","lysosomal acid hydrolyase; human chromosome 11"],["dc.subject.ddc","610"],["dc.title","Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","167"],["dc.bibliographiccitation.journal","Annual Review of Biochemistry"],["dc.bibliographiccitation.lastpage","193"],["dc.bibliographiccitation.volume","55"],["dc.contributor.author","Figura, Kurt von"],["dc.contributor.author","Hasilik, Andrej"],["dc.date.accessioned","2019-07-10T08:12:43Z"],["dc.date.available","2019-07-10T08:12:43Z"],["dc.date.issued","1986"],["dc.description.abstract","This review is limited to discussion of synthesis and transport of lysosomal enzymes in mammalian tissues. We focus on the processing of the oligosaccharides in lysosomal enzymes, on the mannose 6-phosphate-specific receptor (MPR), and on its role in the transport of lysosomal enzymes. The transport of lysosomal enzymes and the function of mannose 6-phosphate-specific receptors have been the subject of recent reviews (3-5)."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3428"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61017"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Annual Reviews"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","Lysosomal enzymes"],["dc.subject.ddc","610"],["dc.title","Lysosomal enzymes and their receptors"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2677"],["dc.bibliographiccitation.issue","9"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","2681"],["dc.bibliographiccitation.volume","6"],["dc.contributor.author","Stein, Martin"],["dc.contributor.author","Zijderhand-Bleekemolen, Jos E."],["dc.contributor.author","Geuze, Hans"],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:43Z"],["dc.date.available","2019-07-10T08:12:43Z"],["dc.date.issued","1987"],["dc.description.abstract","Antibodies that block the ligand binding site of the cationdependent mannose 6-phosphate specific receptor (Mr 46 000 MIPR) were used to probe the function of the receptor in transport of lysosomal enzymes. Addition of the antibodies to the medium of Morris hepatoma 7777 cells, which express only the Mr 46 000 MPR, resulted in a decreased intracellular retention and increased secretion of newly synthesized lysosomal enzymes. In fibroblasts and HepG2 cells that express the cation-independent mannose 6-phosphate specific receptor (Mr 215 000 MPR) in addition to the Mr 46 000 MPR, antibodies against the Mr 46 000 MPR inhibited the intracellular retention of newly synthesized lysosomal enzymes only when added to the medium together with antibodies against the Mr 215 000 MPR. Morris hepatoma (M.H.) 7777 did not endocytose lysosomal enzymes, while U937 monocytes, which express both types of MPR, internalized lysosomal enzymes. The uptake was inhibited by antibodies against the Mr 215 000 MPR, but not by antibodies against the Mr 46 000 MPR. These observations suggest that Mr 46 000 MPR mediates transport of endogenous but not endocytosis of exogenous lysosomal enzymes. Internalization of receptor antibodies indicated that the failure to mediate endocytosis of lysosomal enzymes is due to an inability of surface Mr 46 000 MPR to bind ligands rather than its exclusion from the plasma membrane or from internalization."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3429"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61018"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","Nature Publishing Group"],["dc.relation.issn","0261-4189"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","mannose 6-phosphate; specific receptor; lysosomal"],["dc.subject.ddc","610"],["dc.title","Mr 46 000 mannose 6-phosphate specific receptor: its role in targeting of lysosomal enzymes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2253"],["dc.bibliographiccitation.journal","Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","2262"],["dc.bibliographiccitation.volume","101"],["dc.contributor.author","Geuze, Hans J."],["dc.contributor.author","Slot, Jan W."],["dc.contributor.author","Strous, Ger J. A. M."],["dc.contributor.author","Hasilik, Andrej"],["dc.contributor.author","Figura, Kurt von"],["dc.date.accessioned","2019-07-10T08:12:43Z"],["dc.date.available","2019-07-10T08:12:43Z"],["dc.date.issued","1985"],["dc.description.abstract","Immunogold double-labeling and ultrathin cryosections were used to compare the subcellular distribution of albumin, mannose 6-phosphate receptor (MPR), galactosyltransferase, and the lysosomal enzymes cathepsin D, beta-hexosaminidase, and alpha-glucosidase in Hep Gz cells. MPR and lysosomal enzymes were found throughout the stack of Golgi cisternae and in a trans-Golgi reticulum (TGR) of smooth-surfaced tubules with coated buds and vesicles. The trans-Golgi orientation of TGR was ascertained by the co-localization with galactosyltransferase. MPR was particularly abundant in TGR and CURL, the compartment of uncoupling receptors and ligands. Both TGR and CURL also contained lysosomal enzymes, but endogenous albumin was detected in TGR only. The coated buds on TGR tubules contained MPR, lysosomal enzymes, as well as albumin. MPR and lysosomal enzymes were also found in coated pits of the plasma membrane. CURL tubules seemed to give rise to smooth vesicles, often of the multivesicular body type. In CURL, the enzymes were found in the lumina of the smooth vesicles while MPR prevailed in the tubules. These observations suggest a role of CURL in transport of lysosomal enzymes to lysosomes. When the cells were treated with the lysosomotropic amine primaquine, binding of anti- MPR to the cells in culture was reduced by half. Immunocytochemistry showed that MPR accumulated in TGR, especially in coated buds. Since these buds contain endogenous albumin and lysosomal enzymes also, these data suggest that coated vesicles originating from TGR provide for a secretory route in Hep G2 cells and that this pathway is followed by the MPR system as well."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3427"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61016"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.publisher","RU Press"],["dc.relation.issn","0021-9525"],["dc.rights","Goescholar"],["dc.rights.access","openAccess"],["dc.rights.uri","https://goescholar.uni-goettingen.de/licenses"],["dc.subject","pathways; lysosomal enzyme delivery"],["dc.subject.ddc","610"],["dc.title","Possible Pathways for Lysosomal Enzyme Delivery"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]