Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1987-3-30
|
| pubmed:abstractText |
Recently, we and others reported on the expression of a serine proteinase in long-term cultured murine T lymphocyte cell lines. In an attempt to explore the distribution and possible regulation of this enzyme in T lymphocyte subsets, we performed the presented detailed study. We found that the proteinase is not expressed by thymocytes and resting T cells but can be induced by lectin or antigen in combination with lymphokine sources in vitro in macrophage-depleted unselected T cells as well as in both T cell subsets (Lyt-2+,L3T4- and Lyt-2-,L3T4+) separated by flow cytofluorometry. Furthermore, it appears that cell-associated proteinase activity is increasing with prolonged culture period of sensitized T lymphocytes and that it is higher in antigen-activated as compared to lectin-activated T cells. When tested for substrate specificity the T cell-associated proteinase was shown to preferentially cleave model peptide substrates carrying L-arginine at position P1 in combination with nonpolar amino acids at position P2 and P3. As concluded from its sensitivity to proteinase inhibitors the enzyme can be classified as a serine proteinase and by molecular sieving at high ionic strength it was shown to have a mol. mass of approximately 50-60 kDa. Analysis of in vivo activated T cells revealed that this particular proteinase was expressed in flow cytofluorometry sorted lymphocytic choriomeningitis virus-specific Lyt-2+,L3T4- cytolytic T lymphocytes but not in Lyt-2-,L3T4+ T cells presensitized with either Listeria monocytogenes or I-A alloantigens. The data demonstrate that the two T cell subsets (Lyt-2+,L3T4-; Lyt-2-,L3T4+) have distinct in vitro induction requirements for the expression of proteinase and that after activation of T cells in vivo the enzyme is preferentially associated with Lyt-2+,L3T4- effector cells.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Differentiation...,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface,
http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases,
http://linkedlifedata.com/resource/pubmed/chemical/Isoflurophate,
http://linkedlifedata.com/resource/pubmed/chemical/Lectins,
http://linkedlifedata.com/resource/pubmed/chemical/Lymphokines,
http://linkedlifedata.com/resource/pubmed/chemical/Protease Inhibitors,
http://linkedlifedata.com/resource/pubmed/chemical/Serine Endopeptidases
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Dec
|
| pubmed:issn |
0014-2980
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
16
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
1559-68
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:3102247-Animals,
pubmed-meshheading:3102247-Antigens, Differentiation, T-Lymphocyte,
pubmed-meshheading:3102247-Antigens, Surface,
pubmed-meshheading:3102247-Chromatography, Gel,
pubmed-meshheading:3102247-Clone Cells,
pubmed-meshheading:3102247-Cytotoxicity, Immunologic,
pubmed-meshheading:3102247-Endopeptidases,
pubmed-meshheading:3102247-Enzyme Induction,
pubmed-meshheading:3102247-Flow Cytometry,
pubmed-meshheading:3102247-Isoflurophate,
pubmed-meshheading:3102247-Lectins,
pubmed-meshheading:3102247-Lymphocyte Activation,
pubmed-meshheading:3102247-Lymphokines,
pubmed-meshheading:3102247-Mice,
pubmed-meshheading:3102247-Mice, Inbred C57BL,
pubmed-meshheading:3102247-Protease Inhibitors,
pubmed-meshheading:3102247-Serine Endopeptidases,
pubmed-meshheading:3102247-Substrate Specificity,
pubmed-meshheading:3102247-T-Lymphocytes
|
| pubmed:year |
1986
|
| pubmed:articleTitle |
A specific serine proteinase is inducible in Lyt-2+,L3T4- and Lyt-2-,L3T4+ T cells in vitro but is mainly associated with Lyt-2+,L3T4- effector cells in vivo.
|
| pubmed:publicationType |
Journal Article
|