Direct Demonstration of Association of the Blood-Brain Barrier Proteins ZO-1 and Occludin Using Surface Plasmon Resonance Spectroscopy; Effect of SIN-1

Anke Schmidt, Darkhan I. Utepbergenov, Gerd Krause, Ingolf F. Blasig

Research output: Chapter in Book/Report/Conference proceedingChapter

2 Citations (Scopus)

Abstract

Surface plasmon resonance (SPR) spectroscopy was applied for the first time to study online the association of the blood-brain barrier proteins ZO-1 (zona occludens protein 1) and occludin. The GuK motif of ZO-1 (amino acids 644-812) was identified as the sequence domain that bound to the cytosolic, C-terminal tail of occludin (amino acids 378-521). The nitric oxide (·NO) liberator SIN-1 (3-morpholinosydnonimine) reduced the binding affinity of ZO-1 to occludin, indicating a direct effect of ·NO and NO-related species on the tight junction proteins sealing the blood-brain barrier. We propose that SPR spectroscopy is a novel approach for investigating the interactions of tight junction proteins directly and continuously for pharmacological studies.

Original languageEnglish
Title of host publicationBlood-Spinal Cord and Brain Barriers in Health and Disease
PublisherElsevier
Pages11-17
Number of pages7
ISBN (Electronic)9780080528229
ISBN (Print)9780126390117
DOIs
Publication statusPublished - Jan 1 2004

Keywords

  • NO, SIN-1
  • Occludin
  • Protein interaction
  • SPR
  • Tight junctions
  • ZO-1

ASJC Scopus subject areas

  • Medicine(all)
  • Neuroscience(all)

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