Coexpression of phospholipase A2 isoforms in rat striatal astrocytes
Section snippets
Acknowledgements
Part of this work was performed when S.S. was a recipient of an EMBO short term fellowship at INSERM U.109, Paris, France. The authors thank Dr. Piomelli for constructive criticism, Dr. R.M. Kramer (Eli Lilly, USA) and Dr. J. Ishizaki (Shionogi Research Laboratories, Japan) for providing PLA2 antibodies and sPLA2 cDNA.
References (15)
- et al.
Distinct roles in signal transduction for each of the phospholipase A2 enzymes present in P388D1 macrophages
J. Biol. Chem.
(1996) - et al.
Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
Anal. Biochem.
(1987) The growing phospholipase A2 superfamily of signal transduction enzymes
Trends Biochem. Sci.
(1997)- et al.
Phospholipase A2 enzymes: regulation and inhibition
Trends Pharmacol. Sci.
(1993) - et al.
cPLA2 is phosphorylated and activated by MAP kinase
Cell
(1993) - et al.
Inflammatory factors stimulate expression of group II phospholipase A2 in rat cultured astrocytes
J. Biol. Chem.
(1991) - et al.
Calcium-sensitive cytosolic phospholipase A2 is expressed in human brain astrocytes
Brain Res.
(1994)
Cited by (27)
Calcium-independent phospholipases A<inf>2</inf> and their roles in biological processes and diseases
2015, Journal of Lipid ResearchCitation Excerpt :PLA2s, including iPLA2β, are widely expressed in different regions of the brain (289–291), and iPLA2β immunoreactivity has been reported to be predominant in the cytosol and of less abundance in the nuclear fraction (292), suggesting a role for the enzyme and its products in nuclear signaling. iPLA2β has been purified from rat brain cytosol (293) and identified in dendrites and neurons, microglia, Purkinje cells, and astrocytes (290, 294–296), suggesting that it also participates in neuronal signaling. Advances in lipidomic analyses, coupled with kinetic studies in rodents and positron emission tomography protocols in humans, reveal that the turnover of AA in the brain is associated with cPLA2 and COX-2 activities, whereas that of DHA (22:6n-3) was related to iPLA2β and COX-1 activities (297).
Activation of cPLA<inf>2</inf> and sPLA<inf>2</inf> in astrocytes exposed to simulated ischemia in vitro
2007, Cell Biology InternationalCitation Excerpt :Astrocytes, being the most abundant glial cell type in the brain, are involved in numerous processes that affect neuronal survival during and after ischemic events (Gabryel and Trzeciak, 2001). The glial cells have been shown to contain all types of PLA2 (Zanassi et al., 1998). Evidence indicates that AA can exert several cytotoxic effects towards astrocytes, e.g. through inducing oxidative stress, activation of protein kinase C (PKC), protein kinase A (PKA), NADPH oxidase and GTPase-activating protein, and through the increase in [Ca2+]i (Saluja et al., 1997; Traystman et al., 1991).
Brain phospholipases A<inf>2</inf>: A perspective on the history
2004, Prostaglandins Leukotrienes and Essential Fatty AcidsRetinoic acid-mediated phospholipase A<inf>2</inf> signaling in the nucleus
2004, Brain Research Reviews