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Proceedings Paper

A molecular imaging analysis of Cx43 association with Cdo during skeletal myoblast differentiation
Author(s): Daniele Nosi; Raffaella Mercatelli; Flaminia Chellini; Silvia Soria; Alessandro Pini; Lucia Formigli; Franco Quercioli
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Paper Abstract

Cell-to-cell contacts are crucial for cell differentiation. The promyogenic cell surface protein, Cdo, functions as a component of multiprotein clusters to mediate cell adhesion signaling. Connexin43, the main connexin forming gap junctions, also plays a key role in myogenesis. At least part of its effects are independent of the intercellular channel function, but the mechanisms underlying are unknown. Here, using multiple optical approaches, we provided the first evidence that Cx43 physically interacts with Cdo to form dynamic complexes during myoblast differentiation, offering clues for considering this interaction a structural basis of the channel-independent function of Cx43.

Paper Details

Date Published: 28 February 2014
PDF: 10 pages
Proc. SPIE 8948, Multiphoton Microscopy in the Biomedical Sciences XIV, 89481N (28 February 2014); doi: 10.1117/12.2041667
Show Author Affiliations
Daniele Nosi, Univ. degli Studi di Firenze (Italy)
Raffaella Mercatelli, Istituto dei Sistemi Complessi, CNR (Italy)
Flaminia Chellini, Univ. degli Studi di Firenze (Italy)
Silvia Soria, Istituto di Fisica Applicata Nello Carrara, CNR (Italy)
Alessandro Pini, Univ. degli Studi di Firenze (Italy)
Lucia Formigli, Univ. degli Studi di Firenze (Italy)
Franco Quercioli, Istituto Nazionale di Ottica, CNR (Italy)

Published in SPIE Proceedings Vol. 8948:
Multiphoton Microscopy in the Biomedical Sciences XIV
Ammasi Periasamy; Peter T. C. So; Karsten König, Editor(s)

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