Recruitment of casein kinase 2 is involved in AbetaPP processing following cholinergic stimulation
The amyloid-beta protein precursor (AbetaPP) is an integral membrane protein subjected to constitutive and regulated proteolytic processing. We have previously demonstrated that protein kinase C epsilon (PKCepsilon) plays a key role in the regulation of AbetaPP metabolism via cholinergic receptors....
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Published in | Journal of Alzheimer's disease Vol. 20; no. 4; pp. 1133 - 1141 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Netherlands
2010
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Abstract | The amyloid-beta protein precursor (AbetaPP) is an integral membrane protein subjected to constitutive and regulated proteolytic processing. We have previously demonstrated that protein kinase C epsilon (PKCepsilon) plays a key role in the regulation of AbetaPP metabolism via cholinergic receptors. The purpose of the present work is to clarify whether other putative signaling systems are involved in the same pharmacological pathway. We focused particularly on casein kinase 2 (CK2), demonstrating a direct interaction between PKCepsilon and CK2 following cholinergic stimulation. Treatment of human neuroblastoma SH-SY5Y cells with a selective inhibitor of CK2 reduced the effect of carbachol on the release of sAbetaPPalpha. This treatment did not influence the activation and translocation of PKCepsilon suggesting that the latter is located upstream of CK2. On the basis of our results, we add another player to the complex cellular mechanisms regulating non-amyloidogenic processing of AbetaPP. |
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AbstractList | The amyloid-beta protein precursor (AbetaPP) is an integral membrane protein subjected to constitutive and regulated proteolytic processing. We have previously demonstrated that protein kinase C epsilon (PKCepsilon) plays a key role in the regulation of AbetaPP metabolism via cholinergic receptors. The purpose of the present work is to clarify whether other putative signaling systems are involved in the same pharmacological pathway. We focused particularly on casein kinase 2 (CK2), demonstrating a direct interaction between PKCepsilon and CK2 following cholinergic stimulation. Treatment of human neuroblastoma SH-SY5Y cells with a selective inhibitor of CK2 reduced the effect of carbachol on the release of sAbetaPPalpha. This treatment did not influence the activation and translocation of PKCepsilon suggesting that the latter is located upstream of CK2. On the basis of our results, we add another player to the complex cellular mechanisms regulating non-amyloidogenic processing of AbetaPP. |
Author | Govoni, Stefano De Leonardis, Fabio Stanga, Serena Lenzken, Silvia C Racchi, Marco Lanni, Cristina |
Author_xml | – sequence: 1 givenname: Silvia C surname: Lenzken fullname: Lenzken, Silvia C organization: Department of Experimental and Applied Pharmacology, Centre of Excellence in Applied Biology, University of Pavia, Pavia, Italy – sequence: 2 givenname: Serena surname: Stanga fullname: Stanga, Serena – sequence: 3 givenname: Cristina surname: Lanni fullname: Lanni, Cristina – sequence: 4 givenname: Fabio surname: De Leonardis fullname: De Leonardis, Fabio – sequence: 5 givenname: Stefano surname: Govoni fullname: Govoni, Stefano – sequence: 6 givenname: Marco surname: Racchi fullname: Racchi, Marco |
BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20413902$$D View this record in MEDLINE/PubMed |
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SubjectTerms | ADAM Proteins - metabolism ADAM10 Protein ADAM17 Protein Amyloid beta-Protein Precursor - metabolism Amyloid Precursor Protein Secretases - metabolism Blotting, Western Carbachol - pharmacology Casein Kinase II - physiology Cell Line Cholinergic Agonists - pharmacology Humans Immunohistochemistry Immunoprecipitation Membrane Proteins - metabolism Muscarinic Agonists - pharmacology Parasympathetic Nervous System - metabolism Protein Kinase C-epsilon - metabolism Protein Processing, Post-Translational - drug effects Tubulin - metabolism |
Title | Recruitment of casein kinase 2 is involved in AbetaPP processing following cholinergic stimulation |
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