Structure, heterologous expression, and adhesive properties of the P-0-like myelin glycoprotein IP1 of trout CNS
Autor(en): | Lanwert, C Jeserich, G |
Stichwörter: | Anatomy & Morphology; Biology; bony fish; CELL-ADHESION; CYTOPLASMIC DOMAIN; EXTRACELLULAR DOMAIN; FISH; LEADS; Life Sciences & Biomedicine - Other Topics; membrane adhesion; Microscopy; MOLECULAR-CLONING; myelin; P-0-like protein; PERIPHERAL NERVOUS-SYSTEM; PO PROTEIN; RECOGNITION; TISSUE | Erscheinungsdatum: | 2001 | Herausgeber: | WILEY-LISS | Journal: | MICROSCOPY RESEARCH AND TECHNIQUE | Volumen: | 52 | Ausgabe: | 6 | Startseite: | 637 | Seitenende: | 644 | Zusammenfassung: | The IP1 protein of trout CNS myelin as well as an IP1/P-0 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 P-0-like proteins are discussed considering recent crystallographic data on the atomic structure of the extracellular domain of mammalian P-0. (C) 2001 Wiley-Liss, Inc. |
ISSN: | 1059910X | DOI: | 10.1002/jemt.1048 |
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