Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-8-30
pubmed:abstractText
A recombinant form of human soluble CD23 (sCD23), the low affinity receptor for IgE (FcepsilonRII), was produced by PCR cloning the lectin-binding domain sequence into a bacterial expression vector. After renaturation and purification, the sCD23 bound IgE and divalent metal ions, indicating its activity. The recombinant human sCD23 exhibited similar proinflammatory properties as the native protein. Although interleukin-1beta, tumour necrosis factor-alpha, and nuclear factor-kappaB appeared not to be enhanced significantly in unstimulated RPMI 8866 B-lymphoblastoid and U937 promonocytic cell lines with 24 h incubation of recombinant sCD23, they were produced in both healthy and hyper-IgE-derived peripheral blood mononuclear cells, especially tumour necrosis factor-alpha. This study concludes that while recombinant and chimeric sCD23 may be useful in blocking IgE binding to immune cells and decreasing IgE synthesis by B-lymphocytes, the production of proinflammatory cytokines, particularly tumour necrosis factor-alpha will enhance immune responses in cases of asthma, allergy, and hyper-IgE syndrome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0008-8749
pubmed:author
pubmed:issnType
Print
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
146-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Production of biologically active recombinant human soluble CD23 and its effect on PBMCs isolated from hyper-IgE blood.
pubmed:affiliation
Department of Biochemistry and Microbiology, Nelson Mandela Metropolitan University, P.O. Box 77000, Port Elizabeth 6031, South Africa.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't