Linked Life Data

2801309

Source:http://linkedlifedata.com/resource/pubmed/id/2801309

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3-4
pubmed:dateCreated
1989-11-9
pubmed:abstractText
Three distinct N-terminal variants of rhIL-1 beta can be generated by expression of the IL-1 beta gene in E. coli; the naturally occurring Ala1 species, Met0-Ala1 and des-Ala1 proteins. Since most studies with rhIL-1 beta have used a mixture of two or more variants, we have evaluated their individual bioactivities. The variants were resolved by cation exchange HPLC. Bioactivity measurement on murine thymocytes gave a potency order of Ala1 greater than des-Ala1 greater than Met0-IL-1 beta. Analysis using human T-cells co-stimulated with PMA showed a potency order of Ala1 greater than des-Ala1 greater than Met0-IL-1 beta. Thus changes in the N-terminal amino acid of IL-1 beta changes the activity of the protein. Since murine and human T-cells respond similarly, the interactions between the N-terminus of rhIL-1 beta and their receptors probably occur through comparable mechanisms.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0065-4299
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
268-70
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Isolation and bioactivities of three IL-1 beta N-terminal variants.
pubmed:affiliation
Department of Hypersensitivity Diseases, Upjohn Company, Kalamazoo, MI 49001.
pubmed:publicationType
Journal Article, In Vitro