rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
1
|
pubmed:dateCreated |
2011-1-26
|
pubmed:abstractText |
Endocytosis plays an important role in cell function and the activation and propagation of signaling pathways. Signaling occurs on endocytic pathways and signaling endosomes, and endocytosis is subjected to high-order regulation by cellular signaling mechanisms. Marginal cells showed active endocytosis of microperoxidase (MPO) via the clathrin-independent pathway. We examined the signaling pathway that regulates MPO endocytosis in marginal cells using specific inhibitors and activators of signaling molecules. The results showed that pertussis toxin - which inhibits the ribosylation of G-protein-coupled receptor - did not affect MPO endocytosis, but Clostridium botulinum C3 toxin - which induces RhoA inactivation resulting in extracellular-signal-related kinase inactivation - inhibited MPO endocytosis. The main endocytotic pathway of MPO did not depend on the Rho-associated protein kinase molecular switch or actin/myosin motor system, but was mainly regulated by the RhoA signaling cascade.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADP Ribose Transferases,
http://linkedlifedata.com/resource/pubmed/chemical/Botulinum Toxins,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Kinase,
http://linkedlifedata.com/resource/pubmed/chemical/Myosin-Light-Chain Phosphatase,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidases,
http://linkedlifedata.com/resource/pubmed/chemical/Pertussis Toxin,
http://linkedlifedata.com/resource/pubmed/chemical/exoenzyme C3, Clostridium botulinum,
http://linkedlifedata.com/resource/pubmed/chemical/microperoxidase,
http://linkedlifedata.com/resource/pubmed/chemical/rho-Associated Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/rhoA GTP-Binding Protein
|
pubmed:status |
MEDLINE
|
pubmed:issn |
1423-0275
|
pubmed:author |
|
pubmed:copyrightInfo |
Copyright © 2010 S. Karger AG, Basel.
|
pubmed:issnType |
Electronic
|
pubmed:volume |
73
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
1-8
|
pubmed:meshHeading |
pubmed-meshheading:20975313-ADP Ribose Transferases,
pubmed-meshheading:20975313-Animals,
pubmed-meshheading:20975313-Botulinum Toxins,
pubmed-meshheading:20975313-Cell Membrane,
pubmed-meshheading:20975313-Cochlear Duct,
pubmed-meshheading:20975313-Endocytosis,
pubmed-meshheading:20975313-Endolymph,
pubmed-meshheading:20975313-Guinea Pigs,
pubmed-meshheading:20975313-Myosin-Light-Chain Kinase,
pubmed-meshheading:20975313-Myosin-Light-Chain Phosphatase,
pubmed-meshheading:20975313-Peroxidases,
pubmed-meshheading:20975313-Pertussis Toxin,
pubmed-meshheading:20975313-Signal Transduction,
pubmed-meshheading:20975313-rho-Associated Kinases,
pubmed-meshheading:20975313-rhoA GTP-Binding Protein
|
pubmed:year |
2011
|
pubmed:articleTitle |
Endocytosis of microperoxidase in marginal cells is mainly regulated by RhoA signaling cascade, but not by Rho-associated protein kinase, myosin light-chain kinase and myosin phosphatase.
|
pubmed:affiliation |
Department of Otolaryngology, Faculty of Medicine, University of Tokyo, Tokyo, Japan. kakigi-tky@umin.ac.jp
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|