PLD2 is enriched on exosomes and its activity is correlated to the release of exosomes.
Exosomes are small vesicles secreted by different immune cells and which display anti-tumoral properties. Stimulation of RBL-2H3 cells with ionomycin triggered phospholipase D2 (PLD2) translocation from plasma membrane to intracellular compartments and the release of exosomes. Although exosomes carry the two isoforms of PLD, PLD2 was enriched and specifically sorted on exosomes when overexpressed in cells. PLD activity present on exosomes was clearly increased following PLD2 overexpression. PLD2 activity in cells was correlated to the amount of exosome released, as measured by FACS. Therefore, the present work indicates that exosomes can vehicle signaling enzymes.
Département Lipoprotéines et Médiateurs Lipidiques, INSERM U563, CPTP, Bât C, CHU Purpan, Place Baylac, BP3028, 31024 Toulouse Cedex 3, France.
Karine
K
Laulagnier
David
D
Grand
Arnaud
A
Dujardin
Safouane
S
Hamdi
Hélène
H
Vincent-Schneider
Danielle
D
Lankar
Jean-Pierre
JP
Salles
Christian
C
Bonnerot
Bertrand
B
Perret
Michel
M
Record
D000818:Animals; D045744:Cell Line, Tumor; D002864:Chromogranins / Q000032:analysis; D022162:Cytoplasmic Vesicles / Q000648:ultrastructure*; D007700:Kinetics; D010739:Phospholipase D / Q000378:metabolism*; D051381:Rats
D002864:Chromogranins; C105606:phospholipase D2; D010739:Phospholipase D