A1 Vertaisarvioitu alkuperäisartikkeli tieteellisessä lehdessä
Molecular identification of PAL-E, a widely used endothelial-cell marker
Tekijät: Niemela H, Elima K, Henttinen T, Irjala H, Salmi M, Jalkanen S
Kustantaja: AMER SOC HEMATOLOGY
Julkaisuvuosi: 2005
Journal: Blood
Tietokannassa oleva lehden nimi: BLOOD
Lehden akronyymi: BLOOD
Vuosikerta: 106
Numero: 10
Aloitussivu: 3405
Lopetussivu: 3409
Sivujen määrä: 5
ISSN: 0006-4971
DOI: https://doi.org/10.1182/blood-2005-01-0254
Tiivistelmä
The pathologische anatomie Leiden-endothelium (PAL-E) antibody has been used for almost 20 years as a specific marker for vascular endothelial cells. Due to the fact that this antibody works only in very limited applications, the molecular identity of PAL-E has remained unknown. In this work, we demonstrate by double stainings, cross-immunoprecipitations, and transfectants that the PAL-E antigen is identical with a protein designated PV-1 (plasmalemmal vesicle 1) or FELS (fenestrated endothelial-linked structure protein) and is not vimentin, as reported earlier. As the expression of this molecule is by no means restricted to fenestrated endothelium, we suggest the use of the name PLVAP for this protein. Molecular identification of PLVAP should help in the production of new tools for the identification of vascular as opposed to lymphatic endothelium and to elucidate the function of this protein.
The pathologische anatomie Leiden-endothelium (PAL-E) antibody has been used for almost 20 years as a specific marker for vascular endothelial cells. Due to the fact that this antibody works only in very limited applications, the molecular identity of PAL-E has remained unknown. In this work, we demonstrate by double stainings, cross-immunoprecipitations, and transfectants that the PAL-E antigen is identical with a protein designated PV-1 (plasmalemmal vesicle 1) or FELS (fenestrated endothelial-linked structure protein) and is not vimentin, as reported earlier. As the expression of this molecule is by no means restricted to fenestrated endothelium, we suggest the use of the name PLVAP for this protein. Molecular identification of PLVAP should help in the production of new tools for the identification of vascular as opposed to lymphatic endothelium and to elucidate the function of this protein.