Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1993-2-11
pubmed:abstractText
We established a T-cell line, STO-2, by human T-cell lymphoma-leukemia virus-induced transformation of normal human T cells. Partial purification with isoelectric electrophoresis revealed that STO-2 liberated several eosinophil chemotactic factors (ECF) for eosinophils from healthy individuals with different isoelectric point of PI5, PI6, PI7, PI8, and PI9. Molecular weight of all the ECF was about 30,000 to 45,000. None of the ECF except ECF-PI5 was suppressed when they were incubated with monoclonal antibodies against IL-3, IL-5, and GM-CSF together, suggesting that ECF activity of ECF-PI5 is mainly comprised of IL-3, IL-5, and GM-CSF. ECF-PI5, PI6, and PI7 also exhibited enhancing activity on ex vivo eosinophil survival whereas ECF-PI8 and PI9 failed. Expression of Fc epsilon receptor II on eosinophils was potentiated by ECF-PI6 and ECF-PI7. In contrast, expression of Fc gamma receptor III was potentiated by ECF-PI7, ECF-PI8, and ECF-PI9. ECF-PI6 could also change an eosinophilic cell line, EOL-1, to eosinophilic granule-positive cells, whereas the rest of ECF failed. The above results suggested that eosinophils attracted by an ECF exhibit their biological functions, which differ from those of eosinophils attracted by other ECF. In further experiments, the chemotactic response of eosinophils from patients with eosinophilia was compared to that of eosinophils from healthy individuals.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1056-5477
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
331-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Establishment of a human T-cell line constitutively producing several eosinophil chemotactic lymphokines and their functional heterogeneity on eosinophils.
pubmed:affiliation
Department of Pathology, Kumamoto University Medical School, Japan.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't