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A peptide fragment of ependymin neurotrophic factor uses protein kinase C and the mitogen-activated protein kinase pathway to activate c-Jun N-terminal kinase and a functional AP-1 containing c-Jun and c-Fos proteins in mouse NB2a cells.
J Neurosci Res. 2003 May 01; 72(3):405-16.JN

Abstract

Ependymin (EPN) is a goldfish brain neurotrophic factor previously shown to function in a variety of cellular events related to long-term memory formation and neuronal regeneration. CMX-8933, an 8-amino-acid synthetic peptide fragment of EPN, was designed for aiding an investigation of the biological properties of this glycoprotein. We reported from previous studies that treatment of mouse neuroblastoma (NB2a) cultures with CMX-8933 promotes activation of transcription factor AP-1, a characteristic previously associated with the following full-length neurotrophic factors: nerve growth factor, neurotropin-3, and brain-derived neurotrophic factor. The CMX-8933-activated AP-1 specifically bound an AP-1 consensus probe and appeared to contain c-Jun and c-Fos protein components in antibody supershift experiments. Because AP-1 influences a variety of positive and negative cellular processes, determined in part by its exact protein composition and mechanism of activation, we extended these initial AP-1 observations in the current study to confirm the identity of the CMX-8933-activated c-Jun and c-Fos components. CMX-8933 increases the enzymatic activity of c-Jun N-terminal kinase (JNK), increases the phosphorylation of JNK and c-Jun proteins, and increases the cellular titers of c-Jun and c-Fos mRNAs. Furthermore, the AP-1 activated by CMX-8933 is functional, insofar as it transactivates both synthetic and natural AP-1-dependent reporter plasmids. Inhibition studies indicate that activation of the 8933-induced AP-1 occurs via the mitogen-activated protein kinase pathway. These data are in agreement with the recently proposed model for the conversion of short- to long-term synaptic plasticity and memory, in which a JNK-activated transcription factor AP-1, containing c-Jun and c-Fos components, functions at the top of a hierarchy of transcription factors known to regulate long-term neural plasticity.

Authors+Show Affiliations

Department of Biology/Biotechnology, Worcester Polytechnic Institute, Worcester, Massachusetts 01609, USA. dadams@wpi.eduNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12692907

Citation

Adams, David S., et al. "A Peptide Fragment of Ependymin Neurotrophic Factor Uses Protein Kinase C and the Mitogen-activated Protein Kinase Pathway to Activate c-Jun N-terminal Kinase and a Functional AP-1 Containing c-Jun and c-Fos Proteins in Mouse NB2a Cells." Journal of Neuroscience Research, vol. 72, no. 3, 2003, pp. 405-16.
Adams DS, Hasson B, Boyer-Boiteau A, et al. A peptide fragment of ependymin neurotrophic factor uses protein kinase C and the mitogen-activated protein kinase pathway to activate c-Jun N-terminal kinase and a functional AP-1 containing c-Jun and c-Fos proteins in mouse NB2a cells. J Neurosci Res. 2003;72(3):405-16.
Adams, D. S., Hasson, B., Boyer-Boiteau, A., El-Khishin, A., & Shashoua, V. E. (2003). A peptide fragment of ependymin neurotrophic factor uses protein kinase C and the mitogen-activated protein kinase pathway to activate c-Jun N-terminal kinase and a functional AP-1 containing c-Jun and c-Fos proteins in mouse NB2a cells. Journal of Neuroscience Research, 72(3), 405-16.
Adams DS, et al. A Peptide Fragment of Ependymin Neurotrophic Factor Uses Protein Kinase C and the Mitogen-activated Protein Kinase Pathway to Activate c-Jun N-terminal Kinase and a Functional AP-1 Containing c-Jun and c-Fos Proteins in Mouse NB2a Cells. J Neurosci Res. 2003 May 1;72(3):405-16. PubMed PMID: 12692907.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - A peptide fragment of ependymin neurotrophic factor uses protein kinase C and the mitogen-activated protein kinase pathway to activate c-Jun N-terminal kinase and a functional AP-1 containing c-Jun and c-Fos proteins in mouse NB2a cells. AU - Adams,David S, AU - Hasson,Brendan, AU - Boyer-Boiteau,Anne, AU - El-Khishin,Adam, AU - Shashoua,Victor E, PY - 2003/4/15/pubmed PY - 2003/5/24/medline PY - 2003/4/15/entrez SP - 405 EP - 16 JF - Journal of neuroscience research JO - J Neurosci Res VL - 72 IS - 3 N2 - Ependymin (EPN) is a goldfish brain neurotrophic factor previously shown to function in a variety of cellular events related to long-term memory formation and neuronal regeneration. CMX-8933, an 8-amino-acid synthetic peptide fragment of EPN, was designed for aiding an investigation of the biological properties of this glycoprotein. We reported from previous studies that treatment of mouse neuroblastoma (NB2a) cultures with CMX-8933 promotes activation of transcription factor AP-1, a characteristic previously associated with the following full-length neurotrophic factors: nerve growth factor, neurotropin-3, and brain-derived neurotrophic factor. The CMX-8933-activated AP-1 specifically bound an AP-1 consensus probe and appeared to contain c-Jun and c-Fos protein components in antibody supershift experiments. Because AP-1 influences a variety of positive and negative cellular processes, determined in part by its exact protein composition and mechanism of activation, we extended these initial AP-1 observations in the current study to confirm the identity of the CMX-8933-activated c-Jun and c-Fos components. CMX-8933 increases the enzymatic activity of c-Jun N-terminal kinase (JNK), increases the phosphorylation of JNK and c-Jun proteins, and increases the cellular titers of c-Jun and c-Fos mRNAs. Furthermore, the AP-1 activated by CMX-8933 is functional, insofar as it transactivates both synthetic and natural AP-1-dependent reporter plasmids. Inhibition studies indicate that activation of the 8933-induced AP-1 occurs via the mitogen-activated protein kinase pathway. These data are in agreement with the recently proposed model for the conversion of short- to long-term synaptic plasticity and memory, in which a JNK-activated transcription factor AP-1, containing c-Jun and c-Fos components, functions at the top of a hierarchy of transcription factors known to regulate long-term neural plasticity. SN - 0360-4012 UR - https://www.unboundmedicine.com/medline/citation/12692907/A_peptide_fragment_of_ependymin_neurotrophic_factor_uses_protein_kinase_C_and_the_mitogen_activated_protein_kinase_pathway_to_activate_c_Jun_N_terminal_kinase_and_a_functional_AP_1_containing_c_Jun_and_c_Fos_proteins_in_mouse_NB2a_cells_ L2 - https://doi.org/10.1002/jnr.10590 DB - PRIME DP - Unbound Medicine ER -