English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
 
 
DownloadE-Mail
  Open pore block of connexin26 and connexin32 hemichannels by neutral, acidic, and basic glycoconjugates

Locke, D. G., Wang, L.-X., Bevans, C. G., Lee, Y. C., & Harris, A. L. (2003). Open pore block of connexin26 and connexin32 hemichannels by neutral, acidic, and basic glycoconjugates. Cell Communication and Adhesion, 10(4-6), 239-244. doi:10.1080/cac.10.4-6.239.244.

Item is

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Locke, Darren G.1, Author
Wang, Lai-Xi2, Author
Bevans, Carville G.3, Author              
Lee, Yuan C.4, Author
Harris, Andrew L.1, Author
Affiliations:
1Department of Pharmacology and Physiology, New Jersey Medical School, Newark, NJ, USA, ou_persistent22              
2Institute of Human Virology, University of Maryland Biotechnology Institute, Baltimore, MD, USA, ou_persistent22              
3Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
4Department of Biology, Johns Hopkins University, Baltimore, MD, USA, ou_persistent22              

Content

show
hide
Free keywords: Anthranilic acid; channel; connexin; glycoconjugate; maltosaccharide; open-pore block
 Abstract: The mechanisms of molecular discrimination by connexin channels are of acute biological and medical importance. The availability of affinity or open-pore blocking reagents for reliable and specific study of the connexin permeability pathway, would make possible the rigorous cellular and physiological studies required to inform, in molecular terms, the underlying role of intercellular communication pathways in development and disease. Previous work utilized a series of glucosaccharides labeled with an uncharged fluorescent aminopyridine (PA-) group to establish steric constraints to permeability through connexin hemichannels. In that work, the smallest probe permeable through homomeric Cx26 and heteromeric Cx26-Cx32 channels was the PA-disaccharide, and the smallest probe permeable through homomeric Cx32 channels was the PA-trisaccharide. The larger impermeable probes did not block permeation of the smaller probes. Building on this work, a new set of glucosaccharide probes was developed in which the label was one of a homologous series of novel anthranilic acid derivatives (ABG) that carry negative or positive formal charge or remain neutral at physiological pH. When the PA-label of the smallest impermeant PA-derivatized oligosaccharides was replaced by ABG label, the resulting probes acted as reversible, high-affinity inhibitors of large molecule permeation through connexin pores in a size and connexin-specific

Details

show
hide
Language(s): eng - English
 Dates: 2009-07-112003-07
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1080/cac.10.4-6.239.244
PMID: 14681023
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Cell Communication and Adhesion
  Other : Cell Commun. Adhes.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Yverdon, Switzerland : Harwood Academic Publishers
Pages: - Volume / Issue: 10 (4-6) Sequence Number: - Start / End Page: 239 - 244 Identifier: ISSN: 1061-5385
CoNE: https://pure.mpg.de/cone/journals/resource/991042728191368