Linked Life Data

1707136

Source:http://linkedlifedata.com/resource/pubmed/id/1707136

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
1991-5-8
pubmed:abstractText
The biochemical structure of CD69 early activation antigen has been characterized by means of two newly isolated mAb, namely C1.18 and E16.5. Upon analysis by SDS-PAGE, C1.18-reactive molecules immunoprecipitated from 125I-surface labeled PMA activated PBL consisted of a 32 + 32 kD dimer, a 32 + 26 kD dimer, a 26 + 26 kD dimer and a 21 + 21 kD dimer. E16.5-reactive molecules consisted of a 26 + 26 kD dimer and a 21 + 21 kD dimer. Cross absorption experiments showed that E16.5 mAb reacts with an epitope of the CD69 molecule distinct from the one recognized by C1.18 mAb and present only on a subpopulation of the CD69 molecular pool. The patterns of migration of C1.18- and E16.5-reactive molecules in two-dimensional gel-electrophoresis, under reducing conditions before and after treatment with Endoglycosidase F enzyme suggest that the two mAb recognize the same glycoprotein structure, but in two distinct glycosylation forms, both expressed on the cell surface membrane. Finally, p32, p26 and p21 of CD69 complex obtained from three distinct normal donors did not show appreciable structural polymorphism, by two-dimensional peptide mapping, not only among single subunits within the same individual, but also among homologous subunits in distinct individuals. Further, it was found that CD69 complex is expressed at the cell surface of resting PBL, although at a very reduced level in comparison to PMA activated cells. C1.18 and E16.5 mAb induced comparable cell proliferation and IL-2 production in PBL in the presence of PMA. C1.18 mAb increased intracellular free calcium concn in PMA activated PBL after cross-linking with goat anti mouse Ig, while the effect induced by E16.5 mAb after cross-linking was consistently lower. Finally, it was found that Sepharose-linked C1.18 mAb, in the presence of rIL-2 or PMA, did not induce TNF release from 6 NK cell clones.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
28
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
159-68
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:1707136-Antibodies, Monoclonal, pubmed-meshheading:1707136-Antigens, CD, pubmed-meshheading:1707136-Antigens, Differentiation, T-Lymphocyte, pubmed-meshheading:1707136-Calcium, pubmed-meshheading:1707136-Cell Membrane, pubmed-meshheading:1707136-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:1707136-Epitopes, pubmed-meshheading:1707136-Glycoproteins, pubmed-meshheading:1707136-Glycoside Hydrolases, pubmed-meshheading:1707136-Humans, pubmed-meshheading:1707136-Killer Cells, Natural, pubmed-meshheading:1707136-Lectins, C-Type, pubmed-meshheading:1707136-Lymphocyte Activation, pubmed-meshheading:1707136-Lymphocytes, pubmed-meshheading:1707136-Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase, pubmed-meshheading:1707136-Molecular Weight, pubmed-meshheading:1707136-Peptide Mapping, pubmed-meshheading:1707136-Protein Processing, Post-Translational
pubmed:articleTitle
Structural analysis of the CD69 early activation antigen by two monoclonal antibodies directed to different epitopes.
pubmed:affiliation
Istituto di Scienze Immunologiche, Università di Verona, Italy.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't