Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
|
pubmed:dateCreated |
1993-10-5
|
pubmed:abstractText |
Full-length (membrane bound) and truncated (secreted) forms of the beta 2 integrin heterodimer, CD11b/CD18 (Mac-1), were expressed in a human kidney cell line (293) that normally does not express leukocyte adhesion molecules (Leu-CAMs). The biosynthesis of recombinant Mac-1 in 293 cells differed from that reported for leukocytes in that heterodimer formation was not required for CD11b to be exported to the cell surface. A stable cell line was constructed that constitutively secreted the recombinant, truncated Mac-1 heterodimer into growth conditioned cell culture medium. A novel monoclonal antibody that enabled an immunoaffinity method for the selective purification of recombinant Mac-1 heterodimers was identified. Sufficient protein was purified to allow the first measurement of the 50% inhibitory concentration (IC50) for CD11b/CD18 and for the direct comparison of the inhibitory activity of recombinant soluble Mac-1 with that of various CD18 and CD11b specific monoclonal antibodies. Purified recombinant soluble Mac-1 inhibited the binding of neutrophils, activated by opsonized zymosan or fMet-Leu-Phe peptide, to human umbilical vein endothelial cells. Similarly, the recombinant integrin was effective in inhibiting the binding of unactivated neutrophils to tumor necrosis factor (TNF-alpha) activated endothelial cells. The availability of an abundant source of purified, biologically active Mac-1 will enable direct physical and chemical investigations into the relationship between the structure and function of this leukocyte adhesion molecule.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0730-2312
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
52
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
183-95
|
pubmed:dateRevised |
2004-11-17
|
pubmed:meshHeading |
pubmed-meshheading:8366136-Carbohydrates,
pubmed-meshheading:8366136-Cell Membrane,
pubmed-meshheading:8366136-Cloning, Molecular,
pubmed-meshheading:8366136-Humans,
pubmed-meshheading:8366136-Kidney,
pubmed-meshheading:8366136-Kinetics,
pubmed-meshheading:8366136-Macrophage-1 Antigen,
pubmed-meshheading:8366136-Neutrophils,
pubmed-meshheading:8366136-Precipitin Tests,
pubmed-meshheading:8366136-Recombinant Proteins,
pubmed-meshheading:8366136-Tumor Cells, Cultured
|
pubmed:year |
1993
|
pubmed:articleTitle |
Biosynthesis and function of membrane bound and secreted forms of recombinant CD11b/CD18 (Mac-1).
|
pubmed:affiliation |
Department of Immunology, Genentech, Inc., South San Francisco, California 94080.
|
pubmed:publicationType |
Journal Article
|