Source:http://linkedlifedata.com/resource/pubmed/id/12164923
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
2002-8-7
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pubmed:abstractText |
Keratinocytes are an integral component of the skin immune system and function as nonprofessional antigen-presenting cells in pathophysiologic conditions when they express major histocompatibility complex class II molecules, e.g., in psoriasis. In order to analyze further this function we investigated the activity of cathepsin S in comparison with cathepsins B and L. These enzymes were suggested to be involved in antigen presentation. Specific catalytic activities of these cathepsins were determined fluorometrically by hydrolysis of a synthetic substrate (Z-Phe-Arg-7-amido-4-methylcoumarin) in subcellular fractions of human keratinocytes. It was found that the human keratinocyte cell line HaCaT exhibits activities of all three cathepsins investigated. Endosomal/lysosomal compartments show highest cathepsin activities. Normal human keratinocytes in primary culture show a comparable pattern of cathepsin activities. In contrast to this, in syngeneic Epstein-Barr virus-transformed B cells the level of cathepsin B activity was found to be 10% of that in the corresponding keratinocytes, whereas the activities for cathepsins L and S were in a similar range. Interferon-gamma stimulation of primary keratinocytes and HaCaT cells resulted in a selective upregulation of the cathepsin S activity, the extent of which was very similar. The mechanism of this upregulation was demonstrated as induction at the mRNA and protein levels. This report documents that cathepsin S in human keratinocytes is selectively upregulated, in parallel to major histocompatibility complex class II molecules, in response to a pro-inflammatory cytokine. Our observations support the concept of keratinocytes functioning as nonprofessional antigen-presenting cells in states of inflammation.
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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/Antineoplastic Agents,
http://linkedlifedata.com/resource/pubmed/chemical/CTSL1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin B,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsin L,
http://linkedlifedata.com/resource/pubmed/chemical/Cathepsins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Interferon-gamma,
http://linkedlifedata.com/resource/pubmed/chemical/cathepsin S
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0022-202X
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pubmed:author |
pubmed-author:BoehnckeWolf-HenningWH,
pubmed-author:BraunManuelaM,
pubmed-author:BursterTimoT,
pubmed-author:DresselDanielaD,
pubmed-author:FladThomasT,
pubmed-author:KalbacherHubertH,
pubmed-author:SchmidHeideH,
pubmed-author:SchröterChristian JCJ,
pubmed-author:SchwarzGeroldG,
pubmed-author:WeberEkkehardE
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pubmed:issnType |
Print
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pubmed:volume |
119
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
44-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12164923-Antigen Presentation,
pubmed-meshheading:12164923-Antineoplastic Agents,
pubmed-meshheading:12164923-B-Lymphocytes,
pubmed-meshheading:12164923-Cathepsin B,
pubmed-meshheading:12164923-Cathepsin L,
pubmed-meshheading:12164923-Cathepsins,
pubmed-meshheading:12164923-Cell Line, Transformed,
pubmed-meshheading:12164923-Cysteine Endopeptidases,
pubmed-meshheading:12164923-Enzyme Activation,
pubmed-meshheading:12164923-Flow Cytometry,
pubmed-meshheading:12164923-Humans,
pubmed-meshheading:12164923-Interferon-gamma,
pubmed-meshheading:12164923-Keratinocytes,
pubmed-meshheading:12164923-Lysosomes,
pubmed-meshheading:12164923-Psoriasis,
pubmed-meshheading:12164923-Up-Regulation
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pubmed:year |
2002
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pubmed:articleTitle |
Cathepsin S activity is detectable in human keratinocytes and is selectively upregulated upon stimulation with interferon-gamma.
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pubmed:affiliation |
Medical and Natural Sciences Research Center, University of Tübingen, Ob dem Himmelreich 7, D-72074 Tübingen, Germany.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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