Involvement of Phospholipase D2 in Lysophosphatidate-induced Transactivation of Platelet-derived Growth Factor Receptor-β in Human Bronchial Epithelial Cells

Wang, Lixin; Cummings, Rhett; Zhao, Yutong; Kazlauskas, Andrius; K.S., Sham, James; Morris, Andrew J.; Georas, Steve N.; Brindley, David N.; Natarajan, Viswanathan

doi:10.1074/jbc.m302896200

Cited by 63 publications

(89 citation statements)

References 63 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We have previously shown transactivation of RTKs, such as PDGF-Rβ and EGF-R, by LPARs in HBEpCs [19,20]. Here we examined the cross-talk between LPA-Rs and c-Met in HBEpCs.…”

Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

“…Our previous studies showed that PKC δ plays a critical role in LPA-induced IL-8 expression [16] and EGF-R transactivation [20]. Here we examined the role of PKC δ in cross-talk between LPA-Rs and c-Met in HBEpCs.…”

Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

“…We previously identified the transactivation of PDGF-Rβ and EGF-R by LPA ligation to Gprotein-coupled LPA-Rs and determined that the transactivation of RTKs regulates LPAmediated cellular responses, such as phosphorylation of Erk and IL-8 gene expression and secretion in HBEpCs [20,21] c-Met is the prototype member of RTKs and the high-affinity receptor for HGF [22,23]. Ligation of HGF to the extracellular domain of c-Met results in receptor dimerization, phosphorylation of multiple tyrosine residues at the intracellular region, and binding and activation of signal transducers such as PI-3-Kinase, PLC, STATs, and Erk1/2 [22,[25][26][27].…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, LPA induced IL-13 receptor alpha2 (IL-13Rα2) expression and secretion and attenuated IL-13-induced signaling in HBEpCs [19]. In addition, ligation of LPA to LPA-Rs transactivated RTKs, such as Platelet-Derived Growth Factor Receptor beta (PDGF-Rβ) [20] and Epidermal Growth Factor Receptor (EGF-R) [21]. EGF-R transactivation by LPA contributed to LPAinduced IL-8 secretion [21], while PDGF-Rβ transactivation was involved in LPA-induced phosphorylation of extracelluar signal-regulated kinase (Erk) [20].…”

Section: Introductionmentioning

confidence: 99%

“…In addition, ligation of LPA to LPA-Rs transactivated RTKs, such as Platelet-Derived Growth Factor Receptor beta (PDGF-Rβ) [20] and Epidermal Growth Factor Receptor (EGF-R) [21]. EGF-R transactivation by LPA contributed to LPAinduced IL-8 secretion [21], while PDGF-Rβ transactivation was involved in LPA-induced phosphorylation of extracelluar signal-regulated kinase (Erk) [20]. LPA also induced PDGF-Rβ transactivation through phospholipase D 2 (PLD2) [19] and EGF-R transactivation through PKC δ-mediated activation of lyn kinase, matrix metallopreinases, and heparin-binding EGF (HB-EGF) shedding in HBEpCs [21].…”

Section: Introductionmentioning

confidence: 99%

See 4 more Smart Citations

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

Self Cite

View full text Add to dashboard Cite

Previously we demonstrated that ligation of lysophosphatidic acid (LPA) to G protein-coupled LPA receptors induces transactivation of receptor tyrosine kinases (RTKs), such as platelet-derived growth factor receptor beta (PDGF-Rβ) and epidermal growth factor receptor (EGF-R), in primary cultures of human bronchial epithelial cells (HBEpCs). Here we examined the role of LPA on c-Met redistribution and modulation of hepatocyte growth factor ( These results demonstrate that LPA regulates c-Met function through PKC δ-and E-cadherin in HBEpCs, suggesting an alternate function of the cross-talk between G-protein coupled receptors (GPCRs) and RTKs in HBEpCs.

show abstract

“…We have previously shown transactivation of RTKs, such as PDGF-Rβ and EGF-R, by LPARs in HBEpCs [19,20]. Here we examined the cross-talk between LPA-Rs and c-Met in HBEpCs.…”

Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

Section: Lpa Induces Serine Phosphorylation Of C-met Via G I and Pkc mentioning

confidence: 90%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Zhao¹,

He²,

Stern³

et al. 2007

Cellular Signalling

Self Cite

View full text Add to dashboard Cite

show abstract

Lipid phosphate phosphatases and related proteins: Signaling functions in development, cell division, and cancer

Brindley

2004

J of Cellular Biochemistry

Self Cite

227

199

View full text Add to dashboard Cite

Lipid phosphates initiate key signaling cascades in cell activation. Lysophosphatidate (LPA) and sphingosine 1-phosphate (S1P) are produced by activated platelets. LPA is also formed from circulating lysophosphatidylcholine by autotaxin, a protein involved tumor progression and metastasis. Extracellular LPA and S1P stimulate families of G-protein coupled receptors that elicit diverse responses. LPA is involved in wound repair and tumor growth. Exogenous S1P is a potent stimulator of angiogenesis, a process vital in development, tissue repair and the growth of aggressive tumors. Inside the cell, phosphatidate (PA), ceramide 1-phosphate (C1P), LPA, and S1P act as signaling molecules with distinct functions including the stimulation of cell division, cytoskeletal rearrangement, Ca(2+) transients, and membrane movement. These observations imply that phosphatases that degrade lipid phosphates on the cell surface, or inside the cell, regulate cell signaling under physiological and pathological conditions. This occurs through attenuation of signaling by the lipid phosphates and by the production of bioactive products (diacylglycerol, ceramide, and sphingosine). Three lipid phosphate phosphatases (LPPs) and a splice variant dephosphorylate LPA, PA, CIP, and S1P. Two S1P phosphatases (SPPs) act specifically on S1P. In addition, there is family of four LPP-related proteins (LPRs, or plasticity-related genes, PRGs). PRG-1 expression in neurons has been reported to increase extracellular LPA breakdown and attenuate LPA-induced axonal retraction. It is unclear whether the LRPs dephosphorylate LPA directly, stimulate LPP activity, or bind LPA and S1P. Also, the importance of extra- versus intra-cellular actions of the LPPs and SPPs, and the individual roles of different isoforms is not firmly established. Understanding the functions and regulation of the LPPs, SPPs and related proteins will hopefully contribute to interventions to correct dysfunctions in conditions such as wound repair, inflammation, angiogenesis, tumor growth, and metastasis.

show abstract

Lipid Mediators and Modulators of Neural Function: Lysophosphatidate and Lysolipids

Brindley¹,

Bräuer²

2009

Handbook of Neurochemistry and Molecular Neurobiology

View full text Add to dashboard Cite

Involvement of Phospholipase D2 in Lysophosphatidate-induced Transactivation of Platelet-derived Growth Factor Receptor-β in Human Bronchial Epithelial Cells

Cited by 63 publications

References 63 publications

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Lysophosphatidic acid modulates c-Met redistribution and hepatocyte growth factor/c-Met signaling in human bronchial epithelial cells through PKC δ and E-cadherin

Lipid phosphate phosphatases and related proteins: Signaling functions in development, cell division, and cancer

Lipid Mediators and Modulators of Neural Function: Lysophosphatidate and Lysolipids

Contact Info

Product

Resources

About