Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain

Research output: Contribution to journalJournal articleResearchpeer-review

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Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain. / Kolko, Miriam; Christoffersen, Nanna Rønbjerg; Barreiro, S.G.; Miller, M.L.; Pizza, A.J.; Bazan, N.G.

In: Journal of Neuroscience Research, Vol. 83, No. 5, 2006, p. 874-882.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kolko, M, Christoffersen, NR, Barreiro, SG, Miller, ML, Pizza, AJ & Bazan, NG 2006, 'Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain', Journal of Neuroscience Research, vol. 83, no. 5, pp. 874-882. https://doi.org/10.1002/jnr.20773

APA

Kolko, M., Christoffersen, N. R., Barreiro, S. G., Miller, M. L., Pizza, A. J., & Bazan, N. G. (2006). Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain. Journal of Neuroscience Research, 83(5), 874-882. https://doi.org/10.1002/jnr.20773

Vancouver

Kolko M, Christoffersen NR, Barreiro SG, Miller ML, Pizza AJ, Bazan NG. Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain. Journal of Neuroscience Research. 2006;83(5):874-882. https://doi.org/10.1002/jnr.20773

Author

Kolko, Miriam ; Christoffersen, Nanna Rønbjerg ; Barreiro, S.G. ; Miller, M.L. ; Pizza, A.J. ; Bazan, N.G. / Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain. In: Journal of Neuroscience Research. 2006 ; Vol. 83, No. 5. pp. 874-882.

Bibtex

@article{f5dae0a070eb11dcbee902004c4f4f50,
title = "Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain",
abstract = "Secretory phospholipases A2 (sPLA2) form a diverse family of enzymes involved in a variety of physiologic and pathologic processes. Common among all sPLA2 is the ability to cleave the second position of phospholipids, thereby releasing fatty acid and a lysophospholipid. Several sPLA2 have been cloned and characterized in various tissues and receptors have been identified. In the nervous system, sPLA2 groups IB, IIA, IIE, IIF, V, and XII have been identified, and binding sites for sPLA2 have been found. Here, we report sPLA2-IIE and sPLA2-X in rat brain as well as in neurons in primary culture. We furthermore confirm the presence of sPLA2-V in rat brain and demonstrate the presence of sPLA2-V in primary neuronal cultures. The distribution of sPLA2-IIE, V, and -X seems to be mainly neuronal, with the highest abundance occurring in the cerebral cortex and hippocampus. We also find that sPLA2-IIE, -V, and -X are differentially induced by kainic acid. This study supports the concept that sPLA2 heterogeneity in brain is functionally relevant and responsive to seizures. ",
keywords = "Animals, Brain, Cells, Cultured, Embryo, Mammalian, Group II Phospholipases A2, Immunohistochemistry, In Situ Hybridization, Neurons, Phospholipases A, Phospholipases A2, Rats, Reverse Transcriptase Polymerase Chain Reaction",
author = "Miriam Kolko and Christoffersen, {Nanna R{\o}nbjerg} and S.G. Barreiro and M.L. Miller and A.J. Pizza and N.G. Bazan",
year = "2006",
doi = "10.1002/jnr.20773",
language = "English",
volume = "83",
pages = "874--882",
journal = "Journal of Neuroscience Research",
issn = "0360-4012",
publisher = "JohnWiley & Sons, Inc.",
number = "5",

}

RIS

TY - JOUR

T1 - Characterization and location of secretory phospholipase A2 groups IIE, V, and X in the rat brain

AU - Kolko, Miriam

AU - Christoffersen, Nanna Rønbjerg

AU - Barreiro, S.G.

AU - Miller, M.L.

AU - Pizza, A.J.

AU - Bazan, N.G.

PY - 2006

Y1 - 2006

N2 - Secretory phospholipases A2 (sPLA2) form a diverse family of enzymes involved in a variety of physiologic and pathologic processes. Common among all sPLA2 is the ability to cleave the second position of phospholipids, thereby releasing fatty acid and a lysophospholipid. Several sPLA2 have been cloned and characterized in various tissues and receptors have been identified. In the nervous system, sPLA2 groups IB, IIA, IIE, IIF, V, and XII have been identified, and binding sites for sPLA2 have been found. Here, we report sPLA2-IIE and sPLA2-X in rat brain as well as in neurons in primary culture. We furthermore confirm the presence of sPLA2-V in rat brain and demonstrate the presence of sPLA2-V in primary neuronal cultures. The distribution of sPLA2-IIE, V, and -X seems to be mainly neuronal, with the highest abundance occurring in the cerebral cortex and hippocampus. We also find that sPLA2-IIE, -V, and -X are differentially induced by kainic acid. This study supports the concept that sPLA2 heterogeneity in brain is functionally relevant and responsive to seizures.

AB - Secretory phospholipases A2 (sPLA2) form a diverse family of enzymes involved in a variety of physiologic and pathologic processes. Common among all sPLA2 is the ability to cleave the second position of phospholipids, thereby releasing fatty acid and a lysophospholipid. Several sPLA2 have been cloned and characterized in various tissues and receptors have been identified. In the nervous system, sPLA2 groups IB, IIA, IIE, IIF, V, and XII have been identified, and binding sites for sPLA2 have been found. Here, we report sPLA2-IIE and sPLA2-X in rat brain as well as in neurons in primary culture. We furthermore confirm the presence of sPLA2-V in rat brain and demonstrate the presence of sPLA2-V in primary neuronal cultures. The distribution of sPLA2-IIE, V, and -X seems to be mainly neuronal, with the highest abundance occurring in the cerebral cortex and hippocampus. We also find that sPLA2-IIE, -V, and -X are differentially induced by kainic acid. This study supports the concept that sPLA2 heterogeneity in brain is functionally relevant and responsive to seizures.

KW - Animals

KW - Brain

KW - Cells, Cultured

KW - Embryo, Mammalian

KW - Group II Phospholipases A2

KW - Immunohistochemistry

KW - In Situ Hybridization

KW - Neurons

KW - Phospholipases A

KW - Phospholipases A2

KW - Rats

KW - Reverse Transcriptase Polymerase Chain Reaction

U2 - 10.1002/jnr.20773

DO - 10.1002/jnr.20773

M3 - Journal article

C2 - 16511882

VL - 83

SP - 874

EP - 882

JO - Journal of Neuroscience Research

JF - Journal of Neuroscience Research

SN - 0360-4012

IS - 5

ER -

ID: 1203153