Linked Life Data

19533738

Source:http://linkedlifedata.com/resource/pubmed/id/19533738

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2009-10-21
pubmed:abstractText
Inflammatory cytokines such as tumor necrosis factor (TNF)-alpha and interleukin (IL)-1beta stimulate glucuronosyltransferase genes (S and P) in endothelial cells (ECs) and up-regulate sulfoglucuronosyl paragloboside (SGPG) expression, which serves as a ligand for T cell adhesion. However, the mechanism of cytokine-mediated gene up-regulation has not been elucidated. To evaluate the precise mechanism of SGPG up-regulation, we have specifically inhibited the SGPG synthesis in the cerebromicrovascular EC line (SV-HCECs), a transformed brain ECs of human origin. SV-HCECs were transfected with small interfering RNA designed to mimic the human natural killer epitope-1 sulfotransferase (HNK-1ST), the ultimate enzyme that transfers the sulfate group to glucuronic acid for SGPG synthesis. An inhibition of SGPG expression along with a reduction of human CD4(+) cell adhesion was observed in siRNA HNK-1ST (siHNK-1)-transfected cells after TNFalpha stimulation. A thorough screening of the signaling system confirmed that TNFalpha/IL-1beta stimulation up-regulated nuclear factor kappaB (NFkappaB) signaling in SV-HCECs. siHNK-1 transfection interfered with the SGPG up-regulation after TNFalpha/IL-1beta stimulation in transfected cells and reduced the T cell adhesion. Hence, our study indicates that T cell-SGPG adhesion in SV-HCECs may proceed through NFkappaB activation. In addition, siHNK-1 transfection reduced the NFkappaB activity compared with cells that were transfected with scrambled siRNA, before and after TNFalpha/IL-1beta stimulation. This is the first report indicating that NFkappaB signaling is involved in SGPG gene expression in brain ECs by an unknown mechanism. Its down-regulation by inhibiting HNK-1ST expression may have a potential use in preventing the T cell invasion and consequently nerve damage during inflammation.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1097-4547
pubmed:author
pubmed:copyrightInfo
Copyright 2009 Wiley-Liss, Inc.
pubmed:issnType
Electronic
pubmed:volume
87
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3591-9
pubmed:meshHeading
pubmed-meshheading:19533738-Antigens, CD4, pubmed-meshheading:19533738-Brain, pubmed-meshheading:19533738-Cell Adhesion, pubmed-meshheading:19533738-Cell Line, pubmed-meshheading:19533738-Cells, Cultured, pubmed-meshheading:19533738-Endothelial Cells, pubmed-meshheading:19533738-Globosides, pubmed-meshheading:19533738-Humans, pubmed-meshheading:19533738-Immunohistochemistry, pubmed-meshheading:19533738-Interleukin-1beta, pubmed-meshheading:19533738-NF-kappa B, pubmed-meshheading:19533738-RNA, Small Interfering, pubmed-meshheading:19533738-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:19533738-Signal Transduction, pubmed-meshheading:19533738-Sulfotransferases, pubmed-meshheading:19533738-T-Lymphocytes, pubmed-meshheading:19533738-Transfection, pubmed-meshheading:19533738-Tumor Necrosis Factor-alpha, pubmed-meshheading:19533738-Up-Regulation
pubmed:year
2009
pubmed:articleTitle
Sulfoglucuronosyl paragloboside is a ligand for T cell adhesion: regulation of sulfoglucuronosyl paragloboside expression via nuclear factor kappaB signaling.
pubmed:affiliation
Institute of Molecular Medicine and Genetics, Medical College of Georgia, Augusta, Georgia 30912, USA.
pubmed:publicationType
Journal Article, Research Support, N.I.H., Extramural