Incorporation of leucocyte GPI-anchored proteins and protein tyrosine kinases into lipid-rich membrane domains of COS-7 cells
Jazyk angličtina Země Spojené státy americké Médium print
Typ dokumentu časopisecké články, práce podpořená grantem
PubMed
9500981
DOI
10.1006/bbrc.1998.8149
PII: S0006291X98981499
Knihovny.cz E-zdroje
- MeSH
- acylace MeSH
- antigeny CD2 genetika metabolismus MeSH
- antigeny CD59 genetika metabolismus MeSH
- buněčná membrána metabolismus MeSH
- COS buňky MeSH
- exprese genu MeSH
- glykosylfosfatidylinositoly metabolismus MeSH
- leukocyty chemie MeSH
- lidé MeSH
- membránové lipidy metabolismus MeSH
- membránové proteiny genetika metabolismus MeSH
- protein-tyrosinkináza ZAP-70 MeSH
- receptory interleukinu-2 genetika metabolismus MeSH
- rekombinantní proteiny metabolismus MeSH
- transfekce MeSH
- tyrosinkinasa p56(lck), specifická pro lymfocyty genetika metabolismus MeSH
- tyrosinkinasy genetika metabolismus MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- Názvy látek
- antigeny CD2 MeSH
- antigeny CD59 MeSH
- glykosylfosfatidylinositoly MeSH
- membránové lipidy MeSH
- membránové proteiny MeSH
- protein-tyrosinkináza ZAP-70 MeSH
- receptory interleukinu-2 MeSH
- rekombinantní proteiny MeSH
- tyrosinkinasa p56(lck), specifická pro lymfocyty MeSH
- tyrosinkinasy MeSH
- ZAP70 protein, human MeSH Prohlížeč
Several human leucocyte surface glycoproteins and two lymphoid protein kinases were transiently expressed in monkey COS-7 fibroblastoid cells. All glycosylphospha-tidylinositol (GPI)-anchored proteins (CD14, CD16B, CD48, CD59, CD87 and GPI-anchored versions of CD2 and CD25) and protein tyrosine kinase (PTK) Lck but not transmembrane proteins (CD2, CD4, CD5, CD6, CD8) and PTK ZAP-70 were in part localized in buoyant, lipid-rich, detergent-resistant membrane GPI-microdomains of the COS cells. Endogenous GPI-microdomains of COS cells appear to be, in contrast to those present in leucocytes, essentially devoid of associated PTKs. Our results indicate that GPI-anchor is sufficient to target proteins to these membrane specializations even if expressed ectopically. Moreover, the N-terminal double acylation of the PTK Lck appears to be functional also in COS cells and targets the enzyme to the membrane GPI-microdomains implicated in receptor signalling.
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