Linked Life Data

15130945

Source:http://linkedlifedata.com/resource/pubmed/id/15130945

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-8-5
pubmed:abstractText
We analyzed herein whether members of the tetraspanin superfamily are involved in human immature dendritic cell (DC) functions such as foreign antigen internalization, phagocytosis, and cell migration. We show that CD63, CD9, CD81, CD82, and CD151 are present in immature DCs. Whereas CD9 and CD81 are mostly expressed at the cell surface, CD63 and CD82 are also located in intracellular organelles. Complexes of monoclonal antibody (Mab) FC-5.01-CD63 or Fab-5.01-CD63 were rapidly translocated "outside-in" and followed the endocytic pathway through early endosomes and lysosomes, reaching major histocompatibility complex (MHC) class II-enriched compartments (MIICs) in less than one hour. Internalization of CD63 was also observed during Saccharomyces cerevisiae phagocytosis. Moreover, an association of CD63 with the beta-glycan receptor dectin-1 was observed. Mabs against CD9, CD63, CD81, and CD82 enhanced by 50% the migration induced by the chemokines macrophage inflammatory protein-5 (MIP-5) and MIP-1alpha. Concomitantly, Mabs against CD63 and CD82 diminished the surface expression of CD29, CD11b, CD18, and alpha5 integrins. By immunoprecipitation experiments we found that CD63 associated with integrins CD11b and CD18. These results suggest that CD9, CD63, CD81, and CD82 could play a role in modulating the interactions between immature DCs and their environment, slowing their migratory ability. However, only CD63 would intervene in the internalization of complex antigens.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD63, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD81, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD82, http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD9, http://linkedlifedata.com/resource/pubmed/chemical/CD63 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CD81 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CD82 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/CD9 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Histocompatibility Antigens Class I, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Platelet Membrane Glycoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
104
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1183-90
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
CD63 tetraspanin slows down cell migration and translocates to the endosomal-lysosomal-MIICs route after extracellular stimuli in human immature dendritic cells.
pubmed:affiliation
Fundación Instituto Leloir, Av Patricias Argentinas 435, 1405 Capital Federal, Argentina.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't