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Ectodomain shedding of human Nogo-66 receptor homologue-1 by zinc metalloproteinases.

Walmsley, Adrian Robert and Mir, Anis Khusro and Frentzel, Stefan (2005) Ectodomain shedding of human Nogo-66 receptor homologue-1 by zinc metalloproteinases. Biochemical and Biophysical Research Communications, 327 (1). pp. 112-116. ISSN 0006-291X

Abstract

The Nogo-66 receptor (NgR) plays a pivotal role in the inhibition of neuroregeneration as the receptor for multiple neurite outgrowth inhibitors such as Nogo-A. We have previously shown that NgR undergoes zinc metalloproteinase-mediated ectodomain shedding in neuroblastoma cells. Here, we demonstrate that the NgR-related protein NgR homologue-1 is released from neuroblastoma cells as a full-length ectodomain (NgRH1-ecto) and an N-terminal fragment (NTF-NgRH1) containing the leucine-rich repeat region of the protein. Inhibitors of the major protease classes failed to block the release of NgRH1-ecto, suggesting that this occurs via a protease-independent mechanism, presumably by a phospholipase-like enzyme. The release of NTF-NgRH1 was blocked by a hydroxamate-based zinc metalloproteinase inhibitor and tissue inhibitor of metalloproteinases-2 and -3, but not -1, implicating the involvement of membrane-type matrix metalloproteinases in this process. Our findings thus highlight the parallels between the ectodomain shedding of NgRH1 and that previously described for NgR.

Item Type: Article
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Additional Information: author can archive post-print (ie final draft post-refereeing); Publisher's version/PDF cannot be used
Keywords: Ectodomain shedding; Neurite outgrowth inhibition; Nogo-66 receptor homologue-1; Zinc metalloproteinase
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Date Deposited: 14 Dec 2009 13:55
Last Modified: 31 Jan 2013 01:09
URI: https://oak.novartis.com/id/eprint/698

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