alexa Phosphorylation of connexin 43 acts as a stimuli for proteasome-dependent degradation of the protein in lens epithelial cells.
Ophthalmology

Ophthalmology

Journal of Clinical & Experimental Ophthalmology

Author(s): Giro H, Pereira P

Abstract Share this page

Abstract PURPOSE: The lens is an avascular organ in which gap junctions provide a pathway for intercellular communication, which is vital to maintain lens transparency. Connexin43 (Cx43) is the main gap-junctional protein in lens epithelial cells. Phosphorylation of connexins is implicated in the regulation of intercellular communication. The objective of this report is to determine whether phosphorylation of Cx43 in lens epithelial cells alters its resistance to degradation by a proteasome dependent mechanism. METHODS: Primary cultures of LEC were incubated with protein kinase activator (TPA) and allowed to recover either in the presence or absence of proteasome or lysosome inhibitors. The contribution of the proteasome for the degradation of the phosphorylated form of Cx43 was further investigated by metabolic labeling with 32P or [35S]-methionine. Subcellular distribution of Cx43 was evaluated by immunofluorescence using antibodies directed against Cx43. Gap junctional intercellular communication was evaluated by transfer of the dye Lucifer yellow. RESULTS: Inhibitors of proteasome and lysosome both stabilize Cx43, while proteasome inhibitors preferentially stabilize the phosphorylated form of the protein. Pulse chase experiments with 32P or [35S]-methionine show that while phosphorylation destabilizes Cx43, proteasome inhibitors stabilize the phosphorylated form of the protein. Intercellular communication is inhibited by TPA and can be restored by proteasome inhibitors, probably by preventing loss of Cx43 from the plasma membrane following treatment with TPA. CONCLUSIONS: Our observations support a model in which the combined action of phosphorylation and protein degradation by a proteasome dependent mechanism contribute to regulate Cx43 stability in plasma membrane and intercellular communication through gap junctions, thus adding a novel level of regulation to intercellular communication in lens epithelial cells.
This article was published in Mol Vis and referenced in Journal of Clinical & Experimental Ophthalmology

Relevant Expert PPTs

Relevant Speaker PPTs

Peer Reviewed Journals
 
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
 
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

Agri, Food, Aqua and Veterinary Science Journals

Dr. Krish

[email protected]

1-702-714-7001 Extn: 9040

Clinical and Biochemistry Journals

Datta A

[email protected]

1-702-714-7001Extn: 9037

Business & Management Journals

Ronald

[email protected]

1-702-714-7001Extn: 9042

Chemical Engineering and Chemistry Journals

Gabriel Shaw

[email protected]

1-702-714-7001 Extn: 9040

Earth & Environmental Sciences

Katie Wilson

[email protected]

1-702-714-7001Extn: 9042

Engineering Journals

James Franklin

[email protected]

1-702-714-7001Extn: 9042

General Science and Health care Journals

Andrea Jason

[email protected]

1-702-714-7001Extn: 9043

Genetics and Molecular Biology Journals

Anna Melissa

[email protected]

1-702-714-7001 Extn: 9006

Immunology & Microbiology Journals

David Gorantl

[email protected]

1-702-714-7001Extn: 9014

Informatics Journals

Stephanie Skinner

[email protected]

1-702-714-7001Extn: 9039

Material Sciences Journals

Rachle Green

[email protected]

1-702-714-7001Extn: 9039

Mathematics and Physics Journals

Jim Willison

[email protected]

1-702-714-7001 Extn: 9042

Medical Journals

Nimmi Anna

[email protected]

1-702-714-7001 Extn: 9038

Neuroscience & Psychology Journals

Nathan T

[email protected]

1-702-714-7001Extn: 9041

Pharmaceutical Sciences Journals

John Behannon

[email protected]

1-702-714-7001Extn: 9007

Social & Political Science Journals

Steve Harry

[email protected]

1-702-714-7001 Extn: 9042

 
© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version
adwords