Skip to main content

Lysophosphatidic acid: A bioactive phospholipid with growth factor-like properties

  • Chapter
  • First Online:
Reviews of Physiology, Biochemistry and Pharmacology, 119

Part of the book series: Reviews of Physiology, Biochemistry and Pharmacology ((REVIEWS,volume 119))

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Akiyama T, Ishida J, Nakagawa S, Ogawara H, Watanabe S, Itoh N, Shibuya M, Ukami Y (1987) Genistein, a specific inhibitor of tyrosine-specific protein kinases. J Biol Chem 262:5592–5595

    Google Scholar 

  • Benovic JL, Bouvier M, Caron HG, Lefkowitz RJ (1988) Regulation of adenylate cyclase-coupled β-adrenergic receptors. Ann Rev Cell Biol 4:405–428

    Google Scholar 

  • Benton AM, Gerrard JM, Michiel T, Kindom SE (1982) Are lysophosphatidic acids involved in stimulus activation coupling in platelets. Blood 60:642–649

    Google Scholar 

  • Berridge MJ (1987) Inositol trisphosphate and diacylglycerol: two interacting second messangers. Ann Rev Biochem 56:159–193

    Google Scholar 

  • Betsholtz C, Johnsson A, Heldin C-H, Westermar B (1986) Efficient reversion of simion sarcoma virus-transformation by suramin. Proc Natl Acid Sci USA 83:6440–6444

    Google Scholar 

  • Billah MM, Anthes JC (1990) The regulation and cellular functions of phosphatidylcholine hydrolysis. Biochem J 269:281–291

    Google Scholar 

  • Billah MM, Lapetina EG, Cuatrecasa P (1981) Phospholipase A2 activity specific for phosphatidic acid. J Biol Chem 256:5399–5403

    Google Scholar 

  • Bishop WR, Bell RM (1988) Assembly of phospholipids into cellular membranes: biosynthesis, transmembrane movement and intracellular translocation. Ann Rev Cell Biol 4:579–610

    Google Scholar 

  • Bocckino SB, Blackmore PF, Wilson PB, Exton JH (1987) Phosphatidate accumulation in hormone-treated hepatocytes via a phospholipase D mechanism. J Biol Chem 262:15309–15315

    Google Scholar 

  • Carpenter G, Cohen S (1990) Epidermal growth factor. J Biol Chem 265:7709–7712

    Google Scholar 

  • Chinkers M, McKanna JA, Cohen S (1981) Rapid rounding of human A431 cells induced by epidermal growth factor. J Cell Biol 88:422–429

    Google Scholar 

  • Coffey RL, Leof EB, Shipley GD, Moses HL (1987) Suramin inhibition of growth factor receptor binding and mitogenicity in AKR-2B cells. J Cell Physiol 132:143–148

    Google Scholar 

  • Davitz MA, Hom J, Schenkman S (1989) Purification of a glycosyl-phosphatidylinositol-specific phospholipase D from human plasma. J Biol Chem 264:13760–13764

    Google Scholar 

  • Downes CP, Macphee CH (1990) Myo-inositol metabolites as cellular signals. Eur J Biochem 193:1–118

    Google Scholar 

  • Exton JH (1990) Signaling through phosphatidylcholine hydrolysis. J Biol Chem 265:1–4

    Google Scholar 

  • Fantus IG, Kadota S, Deragon G, Foster B, Posner BI (1989) Pervanadate mimics insulin action in rat adipocytes via activation of the insulin receptor tyrosine kinase. Biochemistry 28:8864–8871

    Google Scholar 

  • Fortes PAG, Ellory JC, Lew VL (1973) Suramin: a potent ATPase inhibitor which acts on the inside surface of the sodium pump. Biochim Biophys Acta 318:262–272

    Google Scholar 

  • Gerrard JM, Robinson P (1989) Identification of the molecular species of lysophosphatidic acid produced when platelets are stimulated by thrombin. Biochim Biophys Acta 1001:282–285

    Google Scholar 

  • Heldin NE, Paulsson Y, Forsberg K, Heldin C-H, Westermark B (1989) Induction of cAMP synthesis by forskolin is followed by inhibition of thymidine incorporation in human fibroblasts. J Cell Physiol 138:17–23

    Google Scholar 

  • Hosang M (1985) Suramin binds to platelet-derived growth factor and inhibits its biological activity. J Cell Biochem 29:265–273

    Google Scholar 

  • Imagawa W, Bandyophadhyay GK, Wallace D, Nandi S (1989) Phospholipids contain polyunsaturated fatty acyl groups are mitogenic for normal mouse mammary epithelial cells in serum-free primary cell culture. Proc Natl Acad Sci USA 86:4122–4126

    Google Scholar 

  • Jalink K, Van Corven EJ, Moolenaar WH (1990) Lysophosphatidic acid, but not phosphatidic acid, is a potent Ca2+-mobilizing stimulus for fibroblasts. J Biol Chem 265:12232–12239

    Google Scholar 

  • Jove R, Hanafusa H (1987) Cell transformation by the viral src oncogene. Annu Rev Cell Biol 3:31–56

    Google Scholar 

  • Kanoh H, Yamada K, Sakane F (1990) Diacylglycerol kinase: a key modulator of signal transduction? Trends Biochem Sci 15:47–50

    Google Scholar 

  • Kawase T, Suzuki A (1988) Phosphatidic acid-induced calcium mobilization in osteoblasts. J Biochem (Tokyo) 103:581–582

    Google Scholar 

  • Krabak MJ, Hui S-W (1991) The mitogenic activities of phosphatidate are acyl-chain-length dependent and calcium independent in C3H/10T1/2 cells. Cell Regulation 2:57–64

    Google Scholar 

  • Lamb NJC, Fernandez A, Watsin A, Labbé J-C, Cavadore J-C (1990) Microinjection of cdc2 kinase induces marked changes in cell shape, cytoskeletal organization, and chromatin structure in mammalian fibroblasts. Cell 60:151–165

    Google Scholar 

  • Lapetina EG, Billah MM, Cuatrecasas P (1981) Lysophosphatidic acid potentiates the thrombin-induced production of arachidonate metabolites in platelets. J Biol Chem 256:11904–11909

    Google Scholar 

  • Low MG, Prasad ARS (1988) A phospholipase D specific for the phosphatitylinositol anchor of cell-surface proteins is abundant in plasma. Proc Natl Acad Sci USA 85:980–984

    Google Scholar 

  • Moolenaar WH (1991) G-protein-coupled receptors, phosphoinositide hydrolysis and cell proliferation. Cell growth and differentiation 2:350–364

    Google Scholar 

  • Moolenaar WH, Kruijer W, Tilly BC, Verlaan I, Bierman AJ, De Laat SW (1986) Growth factor-like action of phosphatidic acid. Nature 323:171–173

    Google Scholar 

  • Müller W, Wolpert W (1976) Spectroscopic studies on the complex formation of suramin with bovine and human serum albumin. Biochim Biophys Acta 427:465–480

    Google Scholar 

  • Murayama T, Ui M (1987) Phosphatidic acid may stimulate membrane receptors mediating adenylate cyclase inhibition and phospholipid breakdown in 3T3 fibroblasts. J Biol Chem 5522–5529

    Google Scholar 

  • Nishizuka Y (1986) Studies and perspectives of protein kinase C. Science 233:305–312

    Google Scholar 

  • Pagano RE, Longmuir KJ (1985) Phosphorylation, transbilayer movement, and facilitated intracellular transport of diacylglycerol are involved in the uptake of a fluorescent analog of phosphatidic acid by cultured fibroblasts. J Biol Chem 260:1909–1916

    Google Scholar 

  • Pollak M, Richard M (1990) Suramin blockade of insulin-like growth factor I-stimulated proliferation of human osteosarcoma cells. J Natl Cancer Inst 82:1349–1352

    Google Scholar 

  • Pollard TD, Cooper JA (1986) Actin and actin-binding proteins — A critical evaluation of mechanisms and functions. Annu Rev Biochem 55:987–1035

    Google Scholar 

  • Proll MA, Clark RB, Butcher RW (1985) Phosphatidate and monooleoylphosphatidate inhibition of fibroblast adenylate cyclase is mediated by the inhibitory coupling protein, Ni. Mol Pharmacol 28:331–337

    Google Scholar 

  • Rozengurt E (1986) Early signals in the mitogenic response. Science 234:161–166

    Google Scholar 

  • Rüegg UT, Burgess GM (1989) Staurosporine, K-252 and UCN-01: potent but non-specific inhibitors of protein kinases. Trends Pharmacol Sci 10:218–220

    Google Scholar 

  • Salmon DM, Honeyman TW (1980) Proposed mechanism of cholinergic action in smooth muscle. Nature 284:344–345

    Google Scholar 

  • Seuwen K, Magnaldo I, Pouysségur J (1988) Serotonin stimulates DNA synthesis in fibroblasts acting through 5-HT1-β receptors coupled to a Gi protein. Nature 335:254–256

    Google Scholar 

  • Siegmann D (1987) Stimulation of quiescent 3T3 cells by phosphatidic acid-containing liposomes. Biochem Biophys Res Commun 145:228–233

    Google Scholar 

  • Stossel TP (1989) From signal to pseudopod. How cells control cytoplasmic actin assembly. J Biol Chem 264:18261–18264

    Google Scholar 

  • Tokumura A, Fukuzawa K, Yamada S, Tsukatani H (1980) Stimulatory effects of lysophosphatidic acids on uterine smooth muscles of non-pregnant rats. Arch Int Pharmacodyn Ther 245:74–83

    Google Scholar 

  • Ullrich A, Schlessinger J (1990) Signal transduction by receptors with tyrosine kinase activity. Cell 61:203–212

    Google Scholar 

  • Van Corven EJ, Groenink A, Jalink K, Eichholtz T, Moolenaar WH (1989) Lysophosphatidate-induced cell proliferation: identification and dissection of signaling pathways mediated by G proteins. Cell 59:45–54

    Google Scholar 

  • Van Corven EJ, Van Rijswijk A, Jalink K, Van der Bend R, Van Blitterswijk W, Moolenaar W (1992) Mitogenic action of (lyso)phosphatidic acid on fibroblasts: Correlation with acyl chain length and inhibition by suramin. Biochem J 201:163–169

    Google Scholar 

  • Watson LP, McConnell RT, Lapetina EG (1985) Decanoyl lysophosphatidic acid induces platelet aggregation through an extracellular action. Biochem J 232:61–66

    Google Scholar 

  • Whitman M, Cantley L (1988) Phosphoinositide metabolism and the control of cell proliferation. Biochim Biophys Acta 984:327–344

    Google Scholar 

  • Williams LT (1989) Signal transduction by the platelet-derived growth factor receptor. Science 243:1564–1590

    Google Scholar 

  • Yu C-L, Tsai M-H, Stacey DW (1988) Cellular ras activity and phospholipid metabolism. Cell 52:63–71

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

Copyright information

© 1992 Springer-Verlag

About this chapter

Cite this chapter

Moolenaar, W.H., Jalink, K., van Corven, E.J. (1992). Lysophosphatidic acid: A bioactive phospholipid with growth factor-like properties. In: Reviews of Physiology, Biochemistry and Pharmacology, 119. Reviews of Physiology, Biochemistry and Pharmacology, vol 119. Springer, Berlin, Heidelberg. https://doi.org/10.1007/3540551921_3

Download citation

  • DOI: https://doi.org/10.1007/3540551921_3

  • Published:

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-55192-8

  • Online ISBN: 978-3-540-46770-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics