Imaging and force spectroscopy on desmoglein 1 using atomic force microscopy reveal multivalent Ca2+-dependent, low-affinity trans-interaction

Jens Waschke, Carlos Menendez-Castro, Paola Bruggeman, Rainer Koob, Masayuki Amagai, Hermann J. Gruber, Detlev Drenckhahn, Werner Baumgartner

研究成果: Article査読

28 被引用数 (Scopus)

抄録

Desmoglein 1 is a desmosomal member of the cadherin family expressed in stratified epithelia. Desmoglein 1 is the target adhesion molecule of severe blistering skin diseases such as pemphigus or bullous impetigo. However, despite this enormous pathological relevance, the molecular binding properties of desmoglein 1 are largely unknown. Using atomic force microscopic imaging, we found that desmoglein 1 molecules displayed Ca2+-dependent conformational changes of the extracellular domains. By single-molecule force-distance cycles, we provide evidence that desmoglein 1 undergoes Ca 2+-dependent (K d = 0.8 mm Ca2+) homophilic trans-interaction, which is highly relevant for the contribution of desmoglein 1 homophilic binding to keratinocyte cohesion in distinct epidermal layers. Moreover, while the single-unit unbinding force is comparable to other cadherins (∼40 pN at retrace velocity of 300 nm/s), apparent differences with respect to multivalency of interaction and lifetime of single bonds (0.17 s) were observed. Thus, besides the biophysical characterization of desmoglein 1, a main outcome of the study is that desmoglein 1 differs from other members of the cadherin family in terms of some molecular binding properties.

本文言語English
ページ(範囲)83-92
ページ数10
ジャーナルJournal of Membrane Biology
216
2-3
DOI
出版ステータスPublished - 2007 4 1

ASJC Scopus subject areas

  • Biophysics
  • Physiology
  • Cell Biology

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