Schmidt, Bernhard

[["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","3497"],["dc.bibliographiccitation.issue","11"],["dc.bibliographiccitation.journal","The EMBO Journal"],["dc.bibliographiccitation.lastpage","3506"],["dc.bibliographiccitation.volume","9"],["dc.contributor.author","Peters, Christoph"],["dc.contributor.author","Braun, Martin"],["dc.contributor.author","Weber, Birgit"],["dc.contributor.author","Wendland, Martin"],["dc.contributor.author","Schmidt, Bernhard"],["dc.contributor.author","Pohlmann, Regina"],["dc.contributor.author","Waheed, Abdul"],["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","1990"],["dc.description.abstract","Lysosomal acid phosphatase (LAP) is synthesized as a transmembrane protein with a short carboxy-terminal cytoplasmic tail of 19 amino acids, and processed to a soluble protein after transport to lysosomes. Deletion of the membrane spanning domain and the cytoplasmic tail converts LAP to a secretory protein, while deletion of the cytoplasmic tail as well as substitution of tyrosine 413 within the cytoplasmic tail against phenylalanine causes accumulation at the cell surface. A chimeric polypeptide, in which the cytoplasmic tail of LAP was fused to the ectoplasmic and transmembrane domain of hemagglutinin is rapidly internalized and tyrosine 413 of the LAP tail is essential for internalization of the fusion protein. A chimeric polypeptide, in which the membrane spanning domain and cytoplasmic tail of LAP are fused to the ectoplasmic domain of the Mr 46 kd mannose 6-phosphate receptor, is rapidly transported to lysosomes, whereas wild type receptor is not transported to lysosomes. We conclude that a tyrosine containing endocytosis signal in the cytoplasmic tail of LAP is necessary and sufficient for targeting to lysosomes."],["dc.format.mimetype","application/pdf"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?goescholar/3435"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/61024"],["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","endocytosis signal;intemalization; lysosomes; targeting"],["dc.subject.ddc","610"],["dc.title","Targeting of a lysosomal membrane protein: a tyrosine-containing endocytosis signal in the cytoplasmic tail of lysosomal acid phosphatase is necessary and sufficient for targeting to lysosomes"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]