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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1996-9-9
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pubmed:abstractText |
We developed a stable expression system for conformationally intact recombinant human PR3 (rPR3) using the human mast cell line HMC-1. Like in U937 cells, the rPR3 is processed from a 34 kDa precursor to the 29 kDa mature form, primarily as the result of oligosaccharide trimming. The rPR3 binds [3H]DFP and hydrolyzes the substrate N-methoxysuccinyl-Ala-Ala-Pro-Val-pNA. The enzymatic activity is inhibited by greater than 95% by alpha 1-PI. The rPR3 and the enzymatically inactive mutant rPR3-S176A are both packaged in granules. Thus, proteolytic autoprocessing is not required for PR3's targeting to granules. This rPR3 is the first to be recognized by most c-ANCA from WG patients and all anti-PR3 ANCA that were detected by standard anti-PR3 specific ELISA. This expression system for rPR3 represents a versatile tool for the analysis of its intracellular processing, structure-function relationships and interaction with autoantibodies.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
29
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pubmed:volume |
390
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
265-70
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8706874-Antibodies, Antineutrophil Cytoplasmic,
pubmed-meshheading:8706874-Autoantibodies,
pubmed-meshheading:8706874-Base Sequence,
pubmed-meshheading:8706874-Cell Line,
pubmed-meshheading:8706874-DNA Primers,
pubmed-meshheading:8706874-Enzyme-Linked Immunosorbent Assay,
pubmed-meshheading:8706874-Gene Expression,
pubmed-meshheading:8706874-Humans,
pubmed-meshheading:8706874-Hydrolysis,
pubmed-meshheading:8706874-Isoflurophate,
pubmed-meshheading:8706874-Mast Cells,
pubmed-meshheading:8706874-Microscopy, Fluorescence,
pubmed-meshheading:8706874-Microscopy, Phase-Contrast,
pubmed-meshheading:8706874-Molecular Sequence Data,
pubmed-meshheading:8706874-Myeloblastin,
pubmed-meshheading:8706874-Oligopeptides,
pubmed-meshheading:8706874-Phenotype,
pubmed-meshheading:8706874-Protein Processing, Post-Translational,
pubmed-meshheading:8706874-Recombinant Proteins,
pubmed-meshheading:8706874-Serine Endopeptidases,
pubmed-meshheading:8706874-Transfection,
pubmed-meshheading:8706874-Wegener Granulomatosis
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pubmed:year |
1996
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pubmed:articleTitle |
Recombinant human proteinase 3, the Wegener's autoantigen, expressed in HMC-1 cells is enzymatically active and recognized by c-ANCA.
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pubmed:affiliation |
Thoracic Diseases Research Unit, Mayo Clinic and Foundation, Rochester, MN 55905, USA. specks.ulrich@mayo.edu
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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