Structure, heterologous expression, and adhesive properties of the P0‐like myelin glycoprotein IP1 of trout CNS
- 15 March 2001
- journal article
- Published by Wiley in Microscopy Research and Technique
- Vol. 52 (6) , 637-644
- https://doi.org/10.1002/jemt.1048
Abstract
The IP1 protein of trout CNS myelin as well as an IP1/P0 chimeric protein were stably expressed in CHO cells. Successful targeting of the recombinant proteins to the membrane surface was verified by immunofluorescence staining. Full‐length expression of IP1 could be confirmed by Western blot analysis of proteins extracted from stably transfected CHO‐cells. The adhesive properties of IP1 were studied by an in vitro aggregation assay in which microscopic examination was combined with electronic particle counting. While IP1 conveyed only a weak increase in cell aggregation of transfected CHO cells, the IP1/P0 chimera was much more effective. In the presence of specific antibodies, cell aggregation was strongly reduced. The adhesive properties of P0‐like proteins are discussed considering recent crystallographic data on the atomic structure of the extracellular domain of mammalian P0. Microsc. Res. Tech. 52:637–644, 2001.Keywords
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