Linked Life Data

12531283

Source:http://linkedlifedata.com/resource/pubmed/id/12531283

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2003-1-17
pubmed:abstractText
Our previous study showed that recombinant canine IL-13 (rcaIL-13) stimulated production of allergen-specific IgE in vitro by peripheral blood mononuclear cells (PBMC) from flea allergen-sensitized dogs. This has also been demonstrated using human IL-13 (huIL-13) and PBMC isolated from human allergy patients. The stimulatory activity of rcaIL-13 was specifically inhibited by a fusion protein of the extracellular domain of canine IL-13Ralpha2 and the Fc fragment of canine IgG heavy chain (rcaIL-13Ralpha2-Fc). In this communication, we report the construction and expression of a non-fused recombinant extracellular domain of canine IL-13Ralpha2 (rcaIL-13Ralpha2) in an E. coli expression system. The E. coli expressed rcaIL-13Ralpha2 was isolated in inclusion bodies, then solubilized in buffer containing denaturants and reducing agents. After refolding and purification, the biological activity of rcaIL-13Ralpha2 was found in the monomer fraction resulting from gel filtration and ion exchange chromatographies. Biological activity of purified rcaIL-13Ralpha2 was demonstrated by the specific inhibition of rcaIL-13 activity in a TF-1 cell proliferation assay. Additionally, rcaIL-13Ralpha2 was found to be active in neutralizing rcaIL-13 induced upregulation of IgE mRNA levels in PBMCs of "high IgE" dogs, which have been bred to exhibit a predisposition for high IgE production and are used as a model for allergic asthma. The data confirm our previous report that the regulatory effects of IL-13 on IgE production in canine PBMCs are similar to those reported in humans. Thus, allergic dogs, such as the "high IgE" producing dogs, may be excellent models for research on IgE-mediated diseases in humans.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0161-5890
pubmed:author
pubmed:issnType
Print
pubmed:volume
39
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
719-27
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12531283-Allergens, pubmed-meshheading:12531283-Animals, pubmed-meshheading:12531283-Asthma, pubmed-meshheading:12531283-Base Sequence, pubmed-meshheading:12531283-Cell Line, pubmed-meshheading:12531283-DNA, Complementary, pubmed-meshheading:12531283-Dogs, pubmed-meshheading:12531283-Escherichia coli, pubmed-meshheading:12531283-Gene Expression, pubmed-meshheading:12531283-Humans, pubmed-meshheading:12531283-Immunoglobulin E, pubmed-meshheading:12531283-Interleukin-13, pubmed-meshheading:12531283-Interleukin-13 Receptor alpha1 Subunit, pubmed-meshheading:12531283-Leukocytes, Mononuclear, pubmed-meshheading:12531283-Protein Folding, pubmed-meshheading:12531283-RNA, Messenger, pubmed-meshheading:12531283-Receptors, Interleukin, pubmed-meshheading:12531283-Receptors, Interleukin-13, pubmed-meshheading:12531283-Recombinant Proteins
pubmed:year
2003
pubmed:articleTitle
Expression and characterization of recombinant canine IL-13 receptor alpha2 protein and its biological activity in vitro.
pubmed:affiliation
Heska Corporation, 1613 Prospect Parkway, Fort Collins, CO 80525, USA.
pubmed:publicationType
Journal Article, In Vitro