Tsutsumi_2009_Prostaglandins.Other.Lipid.Mediat_88_1

Reference

Title : Ecto-lysophospholipase C controls lysophospholipid uptake and metabolism in porcine kidney epithelial cell line LLC-PK1 - Tsutsumi_2009_Prostaglandins.Other.Lipid.Mediat_88_1
Author(s) : Tsutsumi T , Adachi M , Yoshioka Y , Tokumura A
Ref : Prostaglandins Other Lipid Mediat , 88 :1 , 2009
Abstract :

Lysophosphatidylcholine (LPC) has diverse biological activities through different mechanisms including its conversion into other types of lipid mediators such as lysophosphatidic acid and 2-arachidonoylglycerol. Previously, we found that a large portion of the fluorescent analog of alkyl type LPC (Bodipy-lysoPAF) on porcine kidney epithelial cells (LLC-PK1) was degraded to monoalkylglycerol by lysophospholipase C-like activity and then quickly internalized into the cells. In this study, we investigated whether exogenous fluorescently labeled LPC (NBD-LPC) itself was also metabolized and internalized by a similar mechanism. LLC-PK1 cells converted NBD-LPC to either NBD-MG, possibly due to lysophospholipase C-like activity of ecto-nucleotide pyrophosphatase/phosphodiesterase-6, or to free fatty acid (FA), due to lysophospholipase activity in the culture medium at both sites. The resultant NBD-MG was further degraded to NBD-FA by lipase activity before or after its uptake into the cells, and a portion of NBD-FA was finally released into the culture medium on the opposite side.

PubMedSearch : Tsutsumi_2009_Prostaglandins.Other.Lipid.Mediat_88_1
PubMedID: 18786648

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Citations formats

Tsutsumi T, Adachi M, Yoshioka Y, Tokumura A (2009)
Ecto-lysophospholipase C controls lysophospholipid uptake and metabolism in porcine kidney epithelial cell line LLC-PK1
Prostaglandins Other Lipid Mediat 88 :1

Tsutsumi T, Adachi M, Yoshioka Y, Tokumura A (2009)
Prostaglandins Other Lipid Mediat 88 :1