Human lysosomal acid phosphatase: cloning, expression and chromosomal assignment
1988 | journal article. A publication with affiliation to the University of Göttingen.
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- Authors
- Pohlmann, Regina; Krentler, Christiane; Schmidt, Bernhard; Schröder, Wolfgang; Lorkowski, Gerhard; Culley, Jan; Mersmann, Guenther; Geier, Carola; Waheed, Abdul; Gottschalk, Stephen; Grzeschik, Karl-Heinz; Hasilik, Andrej; Figura, Kurt von
- 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.
- Issue Date
- 1988
- Publisher
- Nature Publishing Group
- Journal
- The EMBO Journal
- File Format
- application/pdf
- ISSN
- 0261-4189
- Language
- English