The DOI matches its Crossref record; 4 of the 4 references it cites were found in a registry or an index.
Extracellular matrix, junctional integrity and matrix metalloproteinase interactions in endothelial permeability regulation*
Abstract
Vascular endothelial permeability is maintained by the regulated apposition of adherens and tight junctional proteins whose organization is controlled by several pharmacological and physiological mediators. Endothelial permeability changes are associated with: (1) the spatial redistribution of surface cadherins and occludin, (2) stabilization of focal adhesive bonds and (3) the progressive activation of matrix metalloproteinases (MMPs). In response to peroxide, histamine and EDTA, endothelial cells sequester VE‐cadherin and alter its cytoskeletal binding. Simultaneously, these mediators enhance focal adhesion to the substratum. Oxidants, cytokines and pharmacological mediators also trigger the activation of matrix metalloproteinases (MMPs) in a cytoskeleton and tyrosine phosphorylation dependent manner to degrade occludin, a well‐characterized tight junction element. These related in vitro phenomena appear to co‐operate during inflammation, to increase endothelial permeability, structurally stabilize cells while also remodelling cell junctions and substratum.
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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
Asahi, M., Wang, X., Mori, T., Sumii, T., Jung, J.-C., Moskowitz, M. A., Fini, M. E., & Lo, E. H. (2001) · The Journal of Neuroscience · doi:10.1523/jneurosci.21-19-07724.2001 · Cited by 1,004
The role of integrins in the maintenance of endothelial monolayer integrity.
Lampugnani, M. G., Resnati, M., Dejana, E., & Marchisio, P. C. (1991) · The Journal of cell biology · doi:10.1083/jcb.112.3.479 · Cited by 292 · cited 1×
“Lampugnani et al. (1991) have also reported that human endothelium treated with cAMP analogues show a diffuse distribution of β1 and β3 integrins, actin and vinculin, which correlated with an apparent enhancement of adhesion to the substrate.”
BackgroundAllport, J. R., Muller, W. A., & Luscinskas, F. W. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.1.203 · Cited by 199
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Michiels, C. (2003) · Journal of Cellular Physiology · doi:10.1002/jcp.10333 · Cited by 773
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Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742
Kalogeris, T., Baines, C. P., Krenz, M., & Korthuis, R. J. (2016) · Comprehensive Physiology · doi:10.1002/cphy.c160006 · Cited by 718
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Metadata
- Authors
- Alexander, J. S., & Elrod, J. W.
- Venue
- Journal of Anatomy
- Publisher
- Wiley
- Published
- 2002-06
- Volume
- 200
- Issue
- 6
- Pages
- 561-574
- ISSN
- 0021-8782 (ISSN-L)
- 1469-7580
- OpenAlex
- W1998402312
- Cited by
- 179
- References
- 4
- FWCI
- 5.00
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
