The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Protein Kinase C Regulates the Phosphorylation and Cellular Localization of Occludin
Open accessAbstract
Occludin is an integral membrane phosphoprotein specifically associated with tight junctions, contributing to the structure and function of this intercellular seal. Occludin function is thought to be regulated by phosphorylation, but no information is available on the molecular pathways involved. In the present study, the involvement of the protein kinase C pathway in the regulation of the phosphorylation and cellular distribution of occludin has been investigated. Phorbol 12-myristate 13-acetate and 1,2-dioctanoylglycerol induced the rapid phosphorylation of occludin in Madin-Darby canine kidney cells cultured in low extracellular calcium medium with a concomitant translocation of occludin to the regions of cell-cell contact. The extent of occludin phosphorylation as well as its incorporation into tight junctions induced by protein kinase C activators or calcium switch were markedly decreased by the protein kinase C inhibitor GF-109203X. In addition, in vitro experiments showed that the recombinant COOH-terminal domain of murine occludin could be phosphorylated by purified protein kinase C. Ser(338) of occludin was identified as an in vitro protein kinase C phosphorylation site using peptide mass fingerprint analysis and electrospray ionization tandem mass spectroscopy. These findings indicate that protein kinase C is involved in the regulation of occludin function at tight junctions.
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Cites
Occludin: a novel integral membrane protein localizing at tight junctions.
Furuse, M., Hirase, T., Itoh, M., Nagafuchi, A., Yonemura, S., Tsukita, S., & Tsukita, S. (1993) · The Journal of cell biology · doi:10.1083/jcb.123.6.1777 · Cited by 2,580
Complex Phenotype of Mice Lacking Occludin, a Component of Tight Junction Strands
Saitou, M., Furuse, M., Sasaki, H., Schulzke, J.-D., Fromm, M., Takano, H., Noda, T., & Tsukita, S. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4131 · Cited by 1,195
Cited by
The blood-brain barrier/neurovascular unit in health and disease
Hawkins, B. T., & Davis, T. P. (2005) · Pharmacological Reviews · doi:10.1124/pr.57.2.4 · Cited by 2,661
González-Mariscal, L., Betanzos, A., Nava, P., & Jaramillo, B. E. (2003) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(02)00037-8 · Cited by 1,160
Blood-brain barrier tight junction permeability and ischemic stroke
Sandoval, K. E., & Witt, K. A. (2008) · Neurobiology of Disease · doi:10.1016/j.nbd.2008.08.005 · Cited by 964
Blood–brain Barrier: Structural Components and Function Under Physiologic and Pathologic Conditions
Persidsky, Y., Ramirez, S. H., Haorah, J., & Kanmogne, G. D. (2006) · Journal of Neuroimmune Pharmacology · doi:10.1007/s11481-006-9025-3 · Cited by 922
Crosstalk of tight junction components with signaling pathways
González-Mariscal, L., Tapia, R., & Chamorro, D. (2008) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2007.08.018 · Cited by 759
Metadata
- Authors
- Andreeva, A. Y., Krause, E., Müller, E.-C., Blasig, I. E., & Utepbergenov, D. I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-10
- Volume
- 276
- Issue
- 42
- Pages
- 38480-38486
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2015679476
- Cited by
- 200
- References
- 2
- FWCI
- 5.24
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Andreeva, A. Y., Krause, E., Müller, E.-C., Blasig, I. E., & Utepbergenov, D. I. (2001). Protein Kinase C Regulates the Phosphorylation and Cellular Localization of Occludin. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m104923200
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