| Neurotrophic actions of PACAP-38 and LIF on human neuroblastoma SH-SY5Y cells. | |
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MedLine Citation:
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PMID: 18506635 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The neurotrophic actions of pituitary adenylate cyclase-activating polypeptide (PACAP)-38 and leukemia inhibitory factor (LIF) were investigated in human neuroblastoma SH-SY5Y cells. Effects on differentiation were assessed through monitoring morphological changes and Western blot analysis of the expression of neuronal marker proteins. In contrast to PACAP-38, which induced a 5.5-fold increase in the number of neurite-bearing cells, LIF had no significant effect on cell morphology compared to control cells over the 4-day time course. Cells co-treated with PACAP-38+LIF showed a similar increase in neurite-bearing cells compared to those treated with PACAP-38 alone. Cell morphology was similar for PACAP-38-treated and PACAP-38+LIF-co-treated cells, with the formation of bipolar neuron-like cells with long thin neurites, topped by growth cone-like structures and varicosities. SH-SY5Y cells express tyrosine hydroxylase (TH) but only low levels of the neuronal marker proteins: Bcl-2, GAP-43 and choline acetyltransferase (ChAT). Treatment of cells with PACAP-38 induced the expression of Bcl-2, GAP-43, and ChAT but did not appear to alter the expression of TH. LIF failed to induce the expression of GAP-43 and had little effect on the expression of TH, but did induce the expression of Bcl-2 and upregulated the expression of ChAT. Co-treatment with LIF had no effect on PACAP-38-induced expression of Bcl-2, GAP-43, and ChAT. Cells differentiated for 4 days with PACAP-38 or treated with LIF also displayed increased resistance to hypoxic conditions and to treatment with H2O2 and TNFalpha. The increased resistance to hypoxic conditions for PACAP-differentiated cells was blocked by the p38 MAP kinase inhibitor, SB203580, but not by the MEK1 inhibitor, PD98059. Additionally, cell proliferation assays show that LIF, but not PACAP-38, stimulates proliferation of SH-SY5Y cells, and this observed increase by LIF is not attenuated by co-treatment with PACAP. Further investigation of the intracellular signaling pathways mediating the neurotrophic effects of PACAP on SH-SY5Y cells indicate that neither phospholipase C activation nor Ca2+/calmodulin-dependent kinase II (CAMKII) are involved. |
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Authors:
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T K Monaghan; C Pou; C J MacKenzie; R Plevin; E M Lutz |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2008-05-28 |
Journal Detail:
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Title: Journal of molecular neuroscience : MN Volume: 36 ISSN: 0895-8696 ISO Abbreviation: J. Mol. Neurosci. Publication Date: 2008 Nov |
Date Detail:
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Created Date: 2008-11-26 Completed Date: 2009-02-17 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 9002991 Medline TA: J Mol Neurosci Country: United States |
Other Details:
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Languages: eng Pagination: 45-56 Citation Subset: IM |
Affiliation:
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Strathclyde Institute of Pharmacy and Biomedical Sciences, Royal College, 204 George Street, Glasgow, G1 1XW, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Biological Markers / metabolism Calcium-Calmodulin-Dependent Protein Kinase Type 2 / metabolism Cell Differentiation / drug effects Cell Line, Tumor Cell Proliferation / drug effects Cell Shape Humans Leukemia Inhibitory Factor / pharmacology* Nerve Growth Factors / pharmacology* Neuroblastoma Pituitary Adenylate Cyclase-Activating Polypeptide / pharmacology* Receptors, OSM-LIF / genetics, metabolism Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I / genetics, metabolism Type C Phospholipases / metabolism |
| Grant Support | |
ID/Acronym/Agency:
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//Wellcome Trust |
| Chemical | |
Reg. No./Substance:
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0/Biological Markers; 0/LIF protein, human; 0/Leukemia Inhibitory Factor; 0/Nerve Growth Factors; 0/Pituitary Adenylate Cyclase-Activating Polypeptide; 0/Receptors, OSM-LIF; 0/Receptors, Pituitary Adenylate Cyclase-Activating Polypeptide, Type I; EC 2.7.11.17/Calcium-Calmodulin-Dependent Protein Kinase Type 2; EC 3.1.4.-/Type C Phospholipases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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