Single-molecule force spectroscopy of the Aplysia cell adhesion molecule reveals two homophilic bonds.
Single-molecule force spectroscopy of the Aplysia cell adhesion molecule reveals two homophilic bonds.
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DOI:
10.1016/j.bpj.2012.07.004
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发表时间:
2012-08
影响因子:
3.4
通讯作者:
Elena Martines;Jian Zhong;Julien Muzard;Aih Cheun Lee;B. Akhremitchev;Daniel M. Suter;Gil U. Lee
中科院分区:
文献类型:
--
作者:
Elena Martines;Jian Zhong;Julien Muzard;Aih Cheun Lee;B. Akhremitchev;Daniel M. Suter;Gil U. Lee
Aplysia californicaneurons comprise a powerful model system for quantitative analysis of cellular and biophysical properties that are essential for neuronal development and function. TheAplysiacell adhesion molecule (apCAM), a member of the immunoglobulin superfamily of cell adhesion molecules, is present in the growth cone plasma membrane and involved in neurite growth, synapse formation, and synaptic plasticity. apCAM has been considered to be theAplysiahomolog of the vertebrate neural cell adhesion molecule (NCAM); however, whether apCAM exhibits similar binding properties and neuronal functions has not been fully established because of the lack of detailed binding data for the extracellular portion of apCAM. In this work, we used the atomic force microscope to perform single-molecule force spectroscopy of the extracellular region of apCAM and show for the first time (to our knowledge) that apCAM, like NCAM, is indeed a homophilic cell adhesion molecule. Furthermore, like NCAM, apCAM exhibits two distinct bonds in thetransconfiguration, although the kinetic and structural parameters of the apCAM bonds are quite different from those of NCAM. In summary, these single-molecule analyses further indicate that apCAM and NCAM are species homologs likely performing similar functions.