| First Author | Jaworowski A | Year | 1994 |
| Journal | Biochem Biophys Res Commun | Volume | 201 |
| Issue | 2 | Pages | 733-9 |
| PubMed ID | 8003009 | Mgi Jnum | J:18658 |
| Mgi Id | MGI:66914 | Doi | 10.1006/bbrc.1994.1762 |
| Citation | Jaworowski A, et al. (1994) Phospholipase D is activated by phorbol ester but not CSF-1 in murine bone marrow-derived macrophages. Biochem Biophys Res Commun 201(2):733-9 |
| abstractText | Phospholipase D activity was measured in murine bone marrow-derived macrophages (BMM) treated with either colony stimulating factor-1 (CSF-1) or phorbol myristyl acetate (PMA) by measuring formation of phosphatidylbutanol (PtBut) in cells preloaded with n-butanol. Addition of 10(-7) M PMA for 15 min stimulated the amount of PtBut formed in growth arrested cells by 3-4 fold whereas no stimulation was observed with 5000 units mL-1 CSF-1 for 0.5, 2 or 15 min. Protein kinase C activity was determined in growth-arrested BMM by phosphorylation of Myristoylated Alanine-Rich C Kinase Substrate (MARCKS). PMA stimulation for 5 min increased protein kinase C activity 5-6 fold whereas CSF-1 treatment for 5 min or 15 min did not. Contrary to earlier reports, CSF-1 did not stimulate diradyl glycerol formation in BMM. These results show that stimulation of protein kinase C and the activation of phospholipase D are not involved in the early events of CSF-1-stimulated signal transduction pathways in BMM. |
