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  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.

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 Urheber:
Locke, Darren G.1, Autor
Wang, Lai-Xi2, Autor
Bevans, Carville G.3, Autor           
Lee, Yuan C.4, Autor
Harris, Andrew L.1, Autor
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              

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Schlagwörter: Anthranilic acid; channel; connexin; glycoconjugate; maltosaccharide; open-pore block
 Zusammenfassung: 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

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Sprache(n): eng - English
 Datum: 2009-07-112003-07
 Publikationsstatus: Erschienen
 Seiten: 7
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Expertenbegutachtung
 Identifikatoren: DOI: 10.1080/cac.10.4-6.239.244
PMID: 14681023
 Art des Abschluß: -

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Titel: Cell Communication and Adhesion
  Andere : Cell Commun. Adhes.
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: Yverdon, Switzerland : Harwood Academic Publishers
Seiten: - Band / Heft: 10 (4-6) Artikelnummer: - Start- / Endseite: 239 - 244 Identifikator: ISSN: 1061-5385
CoNE: https://pure.mpg.de/cone/journals/resource/991042728191368