JCB logo
BD Biosciences
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents
Published 1 April 2002. doi:10.1083/jcb1571iti1
This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?
© The Rockefeller University Press, 0021-9525/2002/4/10 $5.00
The Journal of Cell Biology, Volume 157, Number 1, April 1, 2002 10-10

In This Issue

 Peroxide perturbations
H2O2 and PECAM-1 work together to open a channel.

Injury triggers invasion of white blood cells into tissues. According to new results from Ji et al. (page 173), PECAM-1, an adhesion molecule on the endothelial cells (ECs) that line blood vessels, does double duty in this invasion process. Direct ligation of PECAM-1 is known to allow neutrophils to crawl between ECs. But, independent of this function in white cell invasion, PECAM-1 is now shown to activate an EC current that may prime cells by loosening their connections.

The messenger that triggers this current is the reactive oxygen species hydrogen peroxide (H2O2). Neutrophil-produced H2O2 signals increase the EC permeability by inducing cell depolarization and an increase in cytosolic Ca2+ concentration, but the mechanism behind these changes remained unknown.

Now, Ji et al. demonstrate that PECAM-1 is required to activate a nonselective cation channel in response to oxidants. The cytoplasmic domain of PECAM-1 is sufficient for activation, suggesting that peroxide-induced Ca2+ influx produced during transmigration does not require PECAM-1 binding between neutrophils and ECs. Phosphorylation of tyrosine residues in this domain is required for the H2O2-induced current, and probably allows interaction with other linker or channel proteins.

Although it is not known which channel is activated, inhibitor studies indicate that the calcium is coming from outside the cell, and not by activation of internal stores. The group plans to investigate the function of the PECAM-1–regulated channel from examining pathological responses in PECAM-1 knock-out mice. {blacksquare}

H2O2 and PECAM-1 work together to open a channel.



Nicole LeBrasseur

lebrasn{at}rockefeller.edu


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?

Related Article

PECAM-1 (CD31) regulates a hydrogen peroxide–activated nonselective cation channel in endothelial cells
Guangju Ji, Christopher D. O'Brien, Morris Feldman, Yefim Manevich, Poay Lim, Jing Sun, Steven M. Albelda, and Michael I. Kotlikoff
J. Cell Biol. 2002 157: 173-184. [Abstract] [Full Text] [PDF]




This Article
Right arrow PDF (Full Text)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by LeBrasseur, N.
Right arrow Search for Related Content
PubMed
Right arrow Articles by LeBrasseur, N.
Related Collections
Right arrowRelated Article
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents