ArticleBritish journal of pharmacology1999
Roles of atypical protein kinase C in lysophosphatidic acid-induced type II adenylyl cyclase activation in RAW 264.7 macrophages.
Article in British journal of pharmacology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 24 citations in OpenAlex.
- Activation of macrophages by P2X7-induced microvesicles from myeloid cells is mediated by phospholipids and is partially dependent on TLR4.Journal of immunology (Baltimore, Md. : 1950) · 2010Article
- Lysophosphatidic acid signaling in airway epithelium: role in airway inflammation and remodeling.Cellular signalling · 2009Review
- Protein kinase C activation inhibits eosinophil degranulation through stimulation of intracellular cAMP production.British journal of pharmacology · 2004Article
- The cox-2-specific inhibitor celecoxib inhibits adenylyl cyclase.Inflammation · 2003Article
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3 authors at 1 institution in 1 country.
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Abstract
1 Lysophosphatidic acid (LPA) has been widely studied as a naturally occurring and multifunctional phospholipid messenger in diverse tissue and cell types and shown to inhibit adenylyl cyclase (AC) by a G protein-mediated mechanism. 2 In type II AC-expressing mouse RAW 264.7 macrophages, we showed that LPA at 3-50 microM increased cyclic AMP formation in a concentration-dependent manner, the effect being additive with that of forskolin or cholera toxin, and synergistic with that of prostaglandin E1 (PGE1) or isoproterenol. 3 The potentiation effect of LPA was unaffected by the removal of serum or pertussis toxin treatment. 4 Both colchicine and cytochalasin B potentiated the cyclic AMP response to PGE1, the effect being additive to that of LPA. 5 On studying the regulation of type II AC by protein kinase C (PKC), phorbol 12-myristate-13 acetate (PMA) potentiated the PGE1-elicited cyclic AMP response, this effect being non-additive to that of LPA, suggesting that PKC activation was the common mechanism involved in AC potentiation by LPA and PMA. 6 PKC inhibitor Ro 31-8220, but not Go 6976, significantly inhibited the LPA-induced cyclic AMP potentiation. 7 The potentiation effect of LPA was unaffected by long-term treatment with PMA, which resulted in the down-regulation of PKCalpha, betaI, betaII and PKCdelta, but not PKCepsilon, mu, lambda and zeta. 8 By in situ kinase assay, we found a marked increase in atypical PKC activity after LPA treatment. 9 Taken together, we conclude that LPA can elicit a unique signalling cascade in RAW 264.7 macrophages and increase type II AC activity via the activation of atypical PKC.
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