Secretion of a lysophospholipase D activity by adipocytes: involvement in lysophosphatidic acid synthesis

Autor: Stephane Gesta, Astrid Rey, Marie-Françoise Simon, David Sibrac, Max Lafontan, Philippe Valet, Jean Sébastien Saulnier-Blache, Alexia Girard
Přispěvatelé: Saulnier-Blache, Jean Sébastien, Biologie de l'adipocyte, physiologie du tissu adipeux et obésités, Université Toulouse III - Paul Sabatier (UT3), Université Fédérale Toulouse Midi-Pyrénées-Université Fédérale Toulouse Midi-Pyrénées-Institut Louis Bugnard-Institut National de la Santé et de la Recherche Médicale (INSERM)
Předmět:
Hot Temperature
Adipose tissue
MESH: Research Support
Non-U.S. Gov't
MESH: Lysophosphatidylcholines
Biochemistry
chemistry.chemical_compound
Endocrinology
Adipocyte
Lysophosphatidic acid
Adipocytes
MESH: Phenanthrolines
phospholipase D
MESH: Animals
Cells
Cultured
chemistry.chemical_classification
MESH: Culture Media
Conditioned
adipose tissue
Lysophosphatidylcholine
lipids (amino acids
peptides
and proteins)
Female
biological phenomena
cell phenomena
and immunity
MESH: Cells
Cultured
Phenanthrolines
MESH: Edetic Acid
3T3F442A preadipocytes
MESH: Heat
[SDV.BC]Life Sciences [q-bio]/Cellular Biology
QD415-436
Biology
Article
Divalent
MESH: Lysophospholipids
Extracellular
Animals
Humans
Secretion
human
[SDV.BC] Life Sciences [q-bio]/Cellular Biology
MESH: Adipocytes
mouse
Edetic Acid
MESH: Humans
Phosphoric Diester Hydrolases
Lysophosphatidylcholines
Cell Biology
Metabolic pathway
chemistry
Culture Media
Conditioned
phospholipase A2
Lysophospholipids
MESH: Phosphoric Diester Hydrolases
MESH: Female
Zdroj: Europe PubMed Central
Scopus-Elsevier
Journal of Lipid Research, Vol 43, Iss 6, Pp 904-910 (2002)
J Lipid Res
J Lipid Res, 2002, 43 (6), pp.904-10
Popis: The aim of the present work was to depict the metabolic pathways involved in extracellular production of lysophosphatidic acid (LPA) by adipocytes. LPA was followed by quantifying the accumulation of LPA in the incubation medium (conditioned medium, CM) of 3T3F442A adipocytes or human adipose tissue explants using a radioenzymatic assay. Surprisingly, after separation from the cells, the amount of LPA present in CM could be significantly increased by further incubation at 37 degrees C. This suggested the presence of a LPA-synthesizing activity (LPA-SA) in CM. LPA-SA appeared as a soluble activity which was inhibited by divalent ion chelators EDTA and phenanthrolin. The effect of EDTA was preferentially reverted by CoCl2, as described for a lysophospholipase D (lyso-PLD) activity previously identified in rat plasma. LPA concentration could also be increased by treatment with a bacterial PLD, demonstrating the presence of PLD-sensitive LPA precursors (mainly lysophosphatidylcholine) in adipocyte CM. LPA-SA could be increased by the addition of exogenous lysophosphatidylcholine, lysophosphatidylglycerol, or lyso-platelet activating factor, demonstrating that LPA-SA resulted from the action of a lyso-PLD. LPA-SA was not inhibited, but rather activated, by primary alcohol (ethanol and 1-butanol), suggesting that adipocyte lyso-PLD was not a classical PLD. Finally, LPA-SA was found to be weaker in CM of undifferentiated adipocyte (preadipocytes) compared with CM of differentiated adipocytes. In conclusion, our results reveal the existence of a secreted lyso-PLD activity regulated during adipocyte-differentiation and involved in extra cellular production of synthesis of LPA by adipocytes.
Databáze: OpenAIRE
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