Source:http://linkedlifedata.com/resource/pubmed/id/14617626
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
|
pubmed:dateCreated |
2004-2-2
|
pubmed:abstractText |
Apoptotic elimination of T cells at sites of inflammation or infiltration into tumors limits an effective immune response. T cell apoptosis can be initiated by a variety of triggers, including galectin-1, a soluble, secreted lectin that binds to oligosaccharide ligands on cell surface glycoproteins, or to oligosaccharide ligands on extracellular matrix glycoproteins in tissue stroma. Although galectin-1 has no transmembrane domain and is secreted from cells that make it, it is not clear if galectin-1 functions as a soluble death trigger in vivo. We examined the ability of stromal cells secreting galectin-1 to kill T cells. Although the stromal cells synthesized abundant galectin-1, the majority of the galectin-1 remained bound to the cell surface, and stromal cell-associated galectin-1 killed bound T cells. In contrast, insufficient amounts of functional galectin-1 were released from the stromal cells into the media to kill T cells in the absence of contact with stromal cells. However, when stromal cells were grown on Matrigel, a mixture of extracellular matrix proteins, or on permeable membranes above Matrigel, secreted galectin-1 bound to Matrigel and killed T cells without stromal cell contact. Ten-fold less galectin-1 on Matrigel was sufficient to kill adherent T cells compared with soluble galectin-1. These results demonstrate that galectin-1 in extracellular matrix is able to directly kill susceptible T cells. Because increased galectin-1 deposition in tumor stroma occurs with tumor progression in various types of cancer, galectin-1 in stroma may act locally in the apoptotic elimination of infiltrating T cells during an immune response.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0021-9258
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
6
|
pubmed:volume |
279
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
4705-12
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:14617626-Animals,
pubmed-meshheading:14617626-Apoptosis,
pubmed-meshheading:14617626-CHO Cells,
pubmed-meshheading:14617626-Cell Adhesion,
pubmed-meshheading:14617626-Cell Communication,
pubmed-meshheading:14617626-Cell Division,
pubmed-meshheading:14617626-Cell Line,
pubmed-meshheading:14617626-Cricetinae,
pubmed-meshheading:14617626-Extracellular Matrix,
pubmed-meshheading:14617626-Galectin 1,
pubmed-meshheading:14617626-Humans,
pubmed-meshheading:14617626-Lymphocytes, Tumor-Infiltrating,
pubmed-meshheading:14617626-Recombinant Proteins,
pubmed-meshheading:14617626-Solubility,
pubmed-meshheading:14617626-Stromal Cells,
pubmed-meshheading:14617626-T-Lymphocytes
|
pubmed:year |
2004
|
pubmed:articleTitle |
Presentation of galectin-1 by extracellular matrix triggers T cell death.
|
pubmed:affiliation |
Department of Pathology, UCLA School of Medicine, Los Angeles, California 90095, USA.
|
pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
|