Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-12-3
pubmed:abstractText
Phagocytosis by macrophages is most important in the initial stages of an immune response. Although RhoA regulates cell adhesion, its roles in the integrin-related association of particles with macrophages and in phagocytosis are not clearly understood. We introduced C3 exoenzyme, a specific inhibitor of Rho, into J774A.1 macrophage cells fused with the 9 amino acid (49-57) transduction domain (RKKRRQRRR) of HIV-1 Tat. The presence of this Tat-C3 vector altered RhoA mobility on non-denaturing gels, indicating that Tat-C3 modified RhoA by ADP-ribosylation. Uptake of (FITC)-conjugated serum-opsonized zymosan particles and adhesion to fibrinogen-coated plates were reduced as was the association of serum-opsonized zymosan particles, and complement C3 and C3bi with the transfected cells. These results suggest that Rho regulates the activity of integrins that are involved in the association of particles with macrophages, phagocytosis, adhesion, and binding of complement C3 and C3bi.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1016-8478
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
16
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
216-23
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Exoenzyme Tat-C3 inhibits association of zymosan particles, phagocytosis, adhesion, and complement binding in macrophage cells.
pubmed:affiliation
Department of Genetic Engineering, Division of Life Sciences, Hallym University, Chunchon 200-702, Korea. jbpark@hallym.ac.kr
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't