![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
|
|
|
|
|
||
A more recent version of this article appeared on July 1, 2003
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Submitted on February 18, 2003
Revised on February 12, 2003
Accepted on March 3, 2003
1 Laboratory of Neurobiology and Genetics, The Rockefeller University, 1230 York Avenue, New York, NY 10021
2 Department of Pharmacology, MSTP Program, University at Stony Brook, Stony Brook, NY 11794-8651
* Corresponding author. E-mail address: strickland{at}rockefeller.edu.
Laminins are extracellular matrix (ECM) proteins that participate in neuronal development, survival, and regeneration. During excitotoxin challenge in the mouse hippocampus, neuron interaction with laminin-10 (
5,
1,
1) protects against neuronal death. To investigate how laminin is involved in neuronal viability, we infused laminin-1 (5,1,1) into the mouse hippocampus. This infusion specifically disrupted the endogenous laminin layer. This disruption was at least partially due to the interaction of the laminin-1 1 chain with endogenous laminin-10, since infusion of anti-laminin 1 antibody had the same effect. The disruption of the laminin layer by laminin-1 a) did not require the intact protein since infusion of plasmin-digested laminin-1 gave similar results; b) was post-transcriptional, since there was no effect on laminin mRNA expression, and c) occurred in both tPA-/- and plasminogen-/- mice, indicating that increased plasmin activity was not responsible. Finally, although tPA-/- mice are normally resistant to excitotoxin-induced neurodegeneration, disruption of the endogenous laminin layer by laminin-1 or anti-laminin 1 antibody renders the tPA-/- hippocampal neurons sensitive to kainate. These results demonstrate that neuron interactions with the deposited matrix are not necessarily recapitulated by interactions with soluble components, and that the laminin matrix is a dynamic structure amenable to modification by exogenous molecules.
This article has been cited by other articles:
|
|
 |
|
  G. N. M. Hajj, M. H. Lopes, A. F. Mercadante, S. S. Veiga, R. B. da Silveira, T. G. Santos, K. C. B. Ribeiro, M. A. Juliano, S. G. Jacchieri, S. M. Zanata, et al. Cellular prion protein interaction with vitronectin supports axonal growth and is compensated by integrins J. Cell Sci., June 1, 2007; 120(11): 1915 - 1926. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 M. Ito, T. Nagai, H. Kamei, N. Nakamichi, T. Nabeshima, K. Takuma, and K. Yamada Involvement of Tissue Plasminogen Activator-Plasmin System in Depolarization-Evoked Dopamine Release in the Nucleus Accumbens of Mice Mol. Pharmacol., November 1, 2006; 70(5): 1720 - 1725. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Monea, B. A. Jordan, S. Srivastava, S. DeSouza, and E. B. Ziff Membrane localization of membrane type 5 matrix metalloproteinase by AMPA receptor binding protein and cleavage of cadherins. J. Neurosci., February 22, 2006; 26(8): 2300 - 2312. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
Z. Gu, J. Cui, S. Brown, R. Fridman, S. Mobashery, A. Y. Strongin, and S. A. Lipton A Highly Specific Inhibitor of Matrix Metalloproteinase-9 Rescues Laminin from Proteolysis and Neurons from Apoptosis in Transient Focal Cerebral Ischemia J. Neurosci., July 6, 2005; 25(27): 6401 - 6408. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Conant, C. St. Hillaire, H. Nagase, R. Visse, D. Gary, N. Haughey, C. Anderson, J. Turchan, and A. Nath Matrix Metalloproteinase 1 Interacts with Neuronal Integrins and Stimulates Dephosphorylation of Akt J. Biol. Chem., February 27, 2004; 279(9): 8056 - 8062. [Abstract] [Full Text] [PDF]
|
|
