RGD Reference Report - Distinct arachidonate-releasing functions of mammalian secreted phospholipase A2s in human embryonic kidney 293 and rat mastocytoma RBL-2H3 cells through heparan sulfate shuttling and external plasma membrane mechanisms. - Rat Genome Database

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Distinct arachidonate-releasing functions of mammalian secreted phospholipase A2s in human embryonic kidney 293 and rat mastocytoma RBL-2H3 cells through heparan sulfate shuttling and external plasma membrane mechanisms.

Authors: Murakami, M  Koduri, RS  Enomoto, A  Shimbara, S  Seki, M  Yoshihara, K  Singer, A  Valentin, E  Ghomashchi, F  Lambeau, G  Gelb, MH  Kudo, I 
Citation: Murakami M, etal., J Biol Chem. 2001 Mar 30;276(13):10083-96. Epub 2000 Dec 5.
RGD ID: 2303037
Pubmed: PMID:11106649   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M007877200   (Journal Full-text)

We analyzed the ability of a diverse set of mammalian secreted phospholipase A(2) (sPLA(2)) to release arachidonate for lipid mediator generation in two transfected cell lines. In human embryonic kidney 293 cells, the heparin-binding enzymes sPLA(2)-IIA, -IID, and -V promote stimulus-dependent arachidonic acid release and prostaglandin E(2) production in a manner dependent on the heparan sulfate proteoglycan glypican. In contrast, sPLA(2)-IB, -IIC, and -IIE, which bind weakly or not at all to heparanoids, fail to elicit arachidonate release, and addition of a heparin binding site to sPLA(2)-IIC allows it to release arachidonate. Heparin nonbinding sPLA(2)-X liberates arachidonic acid most likely from the phosphatidylcholine-rich outer plasma membrane in a glypican-independent manner. In rat mastocytoma RBL-2H3 cells that lack glypican, sPLA(2)-V and -X, which are unique among sPLA(2)s in being able to hydrolyze phosphatidylcholine-rich membranes, act most likely on the extracellular face of the plasma membrane to markedly augment IgE-dependent immediate production of leukotriene C(4) and platelet-activating factor. sPLA(2)-IB, -IIA, -IIC, -IID, and -IIE exert minimal effects in RBL-2H3 cells. These results are also supported by studies with sPLA(2) mutants and immunocytostaining and reveal that sPLA(2)-dependent lipid mediator generation occur by distinct (heparanoid-dependent and -independent) mechanisms in HEK293 and RBL-2H3 cells.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Pla2g5Ratarachidonic acid secretion  IDA  RGD 
Pla2g5Ratleukotriene biosynthetic process  IDA  RGD 
Pla2g5Ratplatelet activating factor biosynthetic process  IDA  RGD 

Objects Annotated

Genes (Rattus norvegicus)
Pla2g5  (phospholipase A2, group V)


Additional Information