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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