Please use this identifier to cite or link to this item:
https://hdl.handle.net/2440/7439
Citations | ||
Scopus | Web of ScienceĀ® | Altmetric |
---|---|---|
?
|
?
|
Type: | Journal article |
Title: | Activation of mitogen- activated protein kinase by arachidonic acid in rat liver epithelial WB cells by a protein kinase C-dependent mechanism |
Author: | Hii, C. Ferrante, A. Edwards, Y. Huang, Z. Hartfield, P. Rathjen, D. Poulos, A. Murray, A. |
Citation: | Journal of Biological Chemistry, 1995; 270(9):4201-4204 |
Publisher: | American Society of Biological Chemists |
Issue Date: | 1995 |
ISSN: | 0021-9258 1083-351X |
Statement of Responsibility: | Charles S. T. Hii, Antonio Ferrante, Yasmin S. Edwards, Zhi H. Huang, Perry J. Hartfield, Deborah A. Rathjen, Alf Poulos, and Andrew W. Murray |
Abstract: | Arachidonic acid (20:4(n-6)), which is released by cells responding to a wide range of stimuli, may play an important role in intracellular signaling. We now report that incubation of WB cells with 20:4(n-6) resulted in the appearance of several tyrosine-phosphorylated cytosolic proteins. Two of the phosphotyrosine-containing proteins, migrating in SDS-polyacrylamide gels of approximately 43 and 45 kDa, corresponded in mobility to phosphorylated species of the 42- and 44-kDa mitogen-activated protein kinase (MAPK) isoforms. Immunoblots of soluble fractions from unstimulated WB cells with anti-MAPK antibodies revealed the presence of the 42- and 44-kDa isoforms of MAPK. Upon incubation with 20:4(n-6), the mobility of both isoforms was retarded, consistent with their activation by phosphorylation. Chromatography of soluble fractions from these cells on Mono Q columns revealed early and late eluting peaks of myelin basic protein kinase activity, which contained the 42- and 44-kDa MAPK isoforms, respectively. Activation of MAPK was transient, peaking at 5 min, and was detectable at 5 microM 20:4(n-6). Further studies into the mechanisms by which MAPK was activated by 20:4(n-6) strongly suggested the involvement of protein kinase C (PKC). Not only did incubation of WB cells with 20:4(n-6) result in the translocation of PKC alpha, delta, and epsilon to a particulate fraction, it was found that the fatty acid failed to activate MAPK in cells pretreated for 26 h with phorbol 12-myristate 13-acetate, which depleted WB cells of PKC alpha, delta and epsilon. In addition, fatty acids of the n-3 series were effective activators of MAPK. The present study, to our knowledge, is the first to report that polyunsaturated fatty acids can cause the activation of MAPK. |
Keywords: | Liver Epithelium Cells, Cultured Epithelial Cells Animals Rats Tetradecanoylphorbol Acetate Mitogen-Activated Protein Kinases Mitogen-Activated Protein Kinase 1 Mitogen-Activated Protein Kinase 3 Protein Kinase C Fatty Acids, Unsaturated Arachidonic Acid Enzyme Activation Protein-Tyrosine Kinases Calcium-Calmodulin-Dependent Protein Kinases |
DOI: | 10.1074/jbc.270.9.4201 |
Published version: | http://dx.doi.org/10.1074/jbc.270.9.4201 |
Appears in Collections: | Aurora harvest Paediatrics publications |
Files in This Item:
There are no files associated with this item.
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.