Structure, heterologous expression, and adhesive properties of the P(0)-like myelin glycoprotein IP1 of trout CNS.
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).
Lanwert
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C
University of Osnabrück, Department of Animal Physiology, Barbarastr.11, D-49069 Osnabrück, Germany.
Jeserich
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G
D000595:Amino Acid Sequence; D000818:Animals; D016466:CHO Cells; D002448:Cell Adhesion; D002490:Central Nervous System / Q000737:chemistry / Q000502:physiology*; D006224:Cricetinae; D029941:Fish Proteins; D008958:Models, Molecular; D008969:Molecular Sequence Data; D018993:Myelin P0 Protein / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology; D009186:Myelin Sheath / Q000737:chemistry*; D011993:Recombinant Fusion Proteins / Q000502:physiology; D014162:Transfection; D014337:Trout
D029941:Fish Proteins; D018993:Myelin P0 Protein; D011993:Recombinant Fusion Proteins