uu.seUppsala University Publications
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
The effect of IL-5 treatment on the stimulation-induced phosphorylation of proteins in blood eosinophils
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. (Inflammation)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. (Inflammation)
Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Sciences. (Inflammation)
2004 (English)In: Cytokine, ISSN 1043-4666, E-ISSN 1096-0023, Vol. 28, no 3, 137-148 p.Article in journal (Refereed) Published
Abstract [en]

Eosinophils are selectively primed and activated by the cytokine IL-5. The aim of this investigation was to study the effects of IL-5 treatment on stimulation-dependent protein phosphorylations, in human peripheral blood eosinophils. After IL-5 treatment, basal phosphorylation patterns showed increases in the phosphorylation of 67, 80 and 93 kDa proteins. Cell stimulations resulted in the following protein phosphorylation increases: 50, 60, 67, 80 and 93 kDa (PMA); 50, 67, 80 and 93 kDa (STZ); and 67, 80 and 93 kDa (IL-5). The phosphorylation of the 50 and 60 kDa proteins was shown to be MEK-independent and dependent on some PKC isoform/s, whereas that of the 67, 80 and 93 kDa proteins was both MEK- and PKC-alpha, beta, delta, gamma, tau and zeta-independent. A phosphoprotein of 50 kDa was identified as p47(phox) and another of 67 kDa protein as the tyrosine phosphatase SHPTP-1. Incubation with IL-5 followed by cell stimulation increased the total phosphorylation of p47(phox). Bidimensional (IEF-SDS/PAGE) analysis showed that the combination of IL-5 treatment followed by stimulation with either PMA or STZ induced the formation of an additional, hyperphosphorylated form of p47(phox). The presence of this form would explain the higher NADPH oxidase activity normally observed after IL-5 priming.

Place, publisher, year, edition, pages
2004. Vol. 28, no 3, 137-148 p.
Keyword [en]
Eosinophils/*drug effects/*metabolism, Female, Humans, Immunoprecipitation, Interleukin-5/*pharmacology, Intracellular Signaling Peptides and Proteins/pharmacology, Male, Molecular Weight, Phosphoproteins/chemistry/*metabolism, Phosphorylation/drug effects, Research Support; Non-U.S. Gov't
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:uu:diva-73022DOI: 10.1016/j.cyto.2004.08.001PubMedID: 15473955OAI: oai:DiVA.org:uu-73022DiVA: diva2:100933
Available from: 2005-09-13 Created: 2005-09-13 Last updated: 2017-12-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMedhttp://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed&cmd=Retrieve&list_uids=15473955&dopt=Citation

Authority records BETA

Woschnagg, CharlotteVenge, Per

Search in DiVA

By author/editor
Woschnagg, CharlotteVenge, Per
By organisation
Department of Medical Sciences
In the same journal
Cytokine
Medical and Health Sciences

Search outside of DiVA

GoogleGoogle Scholar

doi
pubmed
urn-nbn

Altmetric score

doi
pubmed
urn-nbn
Total: 503 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf