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Am J Physiol Regul Integr Comp Physiol 274: R1203-R1211, 1998;
0363-6119/98 $5.00
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Vol. 274, Issue 5, R1203-R1211, May 1998

Gelatinase B modulates selective opening of the blood-brain barrier during inflammation

Sheila Mun-Bryce and Gary A. Rosenberg

Departments of Neurology and Cell Biology and Physiology, University of New Mexico School of Medicine, Albuquerque, New Mexico 87131

Matrix metalloproteinases (MMPs) are associated with neuroinflammatory diseases, and blood-brain barrier damage is a pathophysiological consequence of central nervous system inflammation. We examined whether an increase in MMP production is coupled with the breakdown of blood-brain barrier integrity in the lipopolysaccharide (LPS)-injured brain. Rat brain stimulated with LPS showed a significant rise in gelatinase B (MMP-9) production at 24 h compared with either tumor necrosis factor-alpha (TNF-alpha ) or saline-injected controls. Latent 92-kDa gelatinase B was detected by 4 h, peaked at 8 h, and persisted for 24 h after LPS injection. Production of the active 84-kDa form of gelatinase B was less pronounced, but paralleled 92-kDa enzyme expression. Breakdown in blood-brain barrier integrity, measured by the infiltration of radiolabeled exogenous markers into the brain, was significant to [14C]sucrose (molecular mass 342 Da) and [14C]dextran (molecular mass 50-90 kDa) molecules in LPS-injected animals compared with saline-injected controls. The extent of MMP involvement in barrier permeability was examined in animals treated with the MMP inhibitor BB-1101. A significant drop in gelatinase A and B production was detected in LPS-injured animals receiving BB-1101 compared with untreated animals. This MMP inhibitor also reduced [14C]sucrose uptake in LPS-injected animals, but had no effect on [14C]dextran uptake. MMP production is upregulated in LPS-injured brain tissue and is instrumental in regulating the size-differentiated opening of the blood-brain barrier during acute neuroinflammation.

basal lamina; lipopolysaccharide; matrix metalloproteinases; metalloproteinase inhibitor; neuroinflammation


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