Linked Life Data

9317128

Source:http://linkedlifedata.com/resource/pubmed/id/9317128

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1997-10-21
pubmed:abstractText
Human lymphotoxin-alpha (LT alpha) is found in a secreted form and on the surface of lymphocytes as a complex with a second related protein called lymphotoxin-beta (LT beta). Both secreted human LT alpha and TNF have similar biological activities mediated via the TNF receptors, whereas the cell surface LT alpha beta complex binds to a separate receptor called the LT beta receptor (LT beta R). The murine LT alpha and LT beta (mLT alpha and mLT beta) proteins have never been characterized. When recombinant mLT alpha was produced by either of several methods, the protein had a very low specific activity relative to that of human LT alpha in the conventional WEHI 164 cytotoxicity bioassay. The weak activity observed was inhibited by a soluble murine TNF-R55 Ig fusion protein (mTNF-R55-Ig), but not by mLT beta R-Ig. Coexpression of both mLT alpha and a soluble version of mLT beta in insect cells led to an LT alpha beta form that was cytotoxic in the WEHI 164 assay via the LT beta R. To determine whether natural mLT alpha-like forms with cytotoxic activity comparable to that of secreted human LT alpha were secreted from primary spleen cells, splenic lymphocytes were activated in various ways, and their supernatants were analyzed for cytotoxic activity. Using specific Abs to distinguish between mTNF and mLT, a TNF component was readily detected; however, there was no evidence for a secreted mLT alpha cytotoxic activity using this assay. Combined, these observations suggest that secreted mLT alpha may not play a role in the mouse via interactions with TNF-R55, and the ramifications of this hypothesis are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
159
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3299-310
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9317128-Amino Acid Sequence, pubmed-meshheading:9317128-Animals, pubmed-meshheading:9317128-Antibodies, Monoclonal, pubmed-meshheading:9317128-Cytotoxicity, Immunologic, pubmed-meshheading:9317128-Cytotoxicity Tests, Immunologic, pubmed-meshheading:9317128-Humans, pubmed-meshheading:9317128-Lymphocyte Activation, pubmed-meshheading:9317128-Lymphotoxin-alpha, pubmed-meshheading:9317128-Lymphotoxin-beta, pubmed-meshheading:9317128-Macromolecular Substances, pubmed-meshheading:9317128-Membrane Proteins, pubmed-meshheading:9317128-Mice, pubmed-meshheading:9317128-Mice, Inbred BALB C, pubmed-meshheading:9317128-Molecular Sequence Data, pubmed-meshheading:9317128-Receptors, Tumor Necrosis Factor, pubmed-meshheading:9317128-Recombinant Proteins, pubmed-meshheading:9317128-Solubility, pubmed-meshheading:9317128-T-Lymphocytes, Cytotoxic, pubmed-meshheading:9317128-Tumor Cells, Cultured, pubmed-meshheading:9317128-Tumor Necrosis Factor-alpha
pubmed:year
1997
pubmed:articleTitle
Cytotoxic activities of recombinant soluble murine lymphotoxin-alpha and lymphotoxin-alpha beta complexes.
pubmed:affiliation
Department of Immunology, Biogen, Cambridge, MA 02142, USA.
pubmed:publicationType
Journal Article, Comparative Study