| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
|
|
|
|||||||
|
|||||||||
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
1 Internal Medicine, Division of Endocrinology, Clinical Nutrition and Vascular Medicine, University of Calfornia, Davis, Davis, California, United States
2 Veterinary Medicine, Department of Pathology Microbiology and Immunology, University of California, Davis, Davis, California, United States
3 Veterinary Medicine, Department of Molecular Biosciences, University of California, Davis, Davis, California, United States
* To whom correspondence should be addressed. E-mail: dwwilson{at}ucdavis.edu.
Products generated from lipoprotein lipase (LpL)-mediated hydrolysis of triglyceride-rich lipoproteins (TGRL) are reported to increase endothelial layer permeability. We hypothesize that these increases in permeability result from the active rearrangement and dissolution of the junctional barrier in human aortic endothelial cells (HAEC), as well as induction of the apoptotic cascade. HAEC were treated with TGRL lipolysis products generated from co-incubation of human TGRL plus LpL. Measurement of transendothelial electrical resistance (TEER) demonstrated a time-dependent decrease in endothelial barrier function in response to TGRL lipolysis products. Immunofluorescent localization of ZO-1 showed radical rearrangement along cell borders after 1.5 hours of treatment with lipolysis products. A concurrent redistribution of F-actin from the cell body to the cell margins was observed via rhodamine phalloidin staining. Immunofluorescent imaging for occludin and VE-cadherin showed that these proteins relocalize as well, but that these changes are less prominent than for ZO-1. Western analysis of cells exposed to lipolysis products for 3 hours revealed the fragmentation of ZO-1, a reduction in occludin, and no change of VE-cadherin. Lipolysis products also increased caspase-3 activity and induced nuclear fragmentation. Treatments did not cause oncosis in cells at any point during the incubation. These results demonstrate that TGRL lipolysis products play an important role in the regulation of endothelial permeability, the organization of the actin cytoskeleton, the localization and expression of junctional proteins, especially ZO-1, and the induction of apoptosis.
This article has been cited by other articles:
|
|
 |
|
  L. Wang, R. Gill, T. L. Pedersen, L. J. Higgins, J. W. Newman, and J. C. Rutledge Triglyceride-rich lipoprotein lipolysis releases neutral and oxidized FFAs that induce endothelial cell inflammation J. Lipid Res., February 1, 2009; 50(2): 204 - 213. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
M. Artwohl, A. Lindenmair, V. Sexl, C. Maier, G. Rainer, A. Freudenthaler, N. Huttary, M. Wolzt, P. Nowotny, A. Luger, et al. Different mechanisms of saturated versus polyunsaturated FFA-induced apoptosis in human endothelial cells J. Lipid Res., December 1, 2008; 49(12): 2627 - 2640. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. B. N. Lee, N. Jamgotchian, S. G. Allen, M. B. Abeles, and H. J. Ward A lipid-protein hybrid model for tight junction Am J Physiol Renal Physiol, December 1, 2008; 295(6): F1601 - F1612. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 L. Wang, A. R. Sapuri-Butti, H. H. Aung, A. N. Parikh, and J. C. Rutledge Triglyceride-rich lipoprotein lipolysis increases aggregation of endothelial cell membrane microdomains and produces reactive oxygen species Am J Physiol Heart Circ Physiol, July 1, 2008; 295(1): H237 - H244. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH |
| Visit Other APS Journals Online |
