Source:http://linkedlifedata.com/resource/pubmed/id/17324376
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2007-4-30
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pubmed:abstractText |
Rat recombinant purple acid phosphatase (PAP) stably expressed in fibroblast-like CHO-K1 cells was purified and characterized with respect to post-translational modifications such as N-glycosylation and proteolytic processing in order to elucidate subcellular and molecular pathways for proteolytic activation. In these cells, proteolytically processed PAP was more abundant than the monomeric form. PAP-transfected CHO-K1 cells were expressing active cathepsin K intracellularly, which was partially co-localized with PAP. However, neither cathepsin K nor trypsin digestion of the purified monomeric PAP in vitro did result in a two-subunit form with kinetic and electrophoretic properties resembling the endogenous cellular two-subunit form. Treatment of PAP-transfected CHO-K1 cells with the cysteine proteinase inhibitor E-64 suggested that only a minor fraction of secreted PAP is processed intracellularly by cysteine proteinases. These data do not support a dominant or critical role for cathepsins or trypsin-like serine proteinases in the proteolytic activation of PAP in CHO-K1 cells, implicating yet unidentified proteinases in the proteolytic processing of both intracellular and secreted PAP in this cell line.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acid Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/purple acid phosphatase
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0003-9861
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
461
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-94
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pubmed:meshHeading |
pubmed-meshheading:17324376-Acid Phosphatase,
pubmed-meshheading:17324376-Animals,
pubmed-meshheading:17324376-CHO Cells,
pubmed-meshheading:17324376-Cricetinae,
pubmed-meshheading:17324376-Cricetulus,
pubmed-meshheading:17324376-Enzyme Stability,
pubmed-meshheading:17324376-Glycoproteins,
pubmed-meshheading:17324376-Hydrolysis,
pubmed-meshheading:17324376-Isoenzymes,
pubmed-meshheading:17324376-Peptide Hydrolases,
pubmed-meshheading:17324376-Protein Processing, Post-Translational,
pubmed-meshheading:17324376-Rats
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pubmed:year |
2007
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pubmed:articleTitle |
Expression and proteolytic processing of mammalian purple acid phosphatase in CHO-K1 cells.
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pubmed:affiliation |
Karolinska Institutet, Department of Laboratory Medicine, Division of Pathology, Karolinska University Hospital, S-141 86 Huddinge, Sweden.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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