title: Surface behavior of axolemma monolayers: physico-chemical characterization and use as supported planar membranes for cultured Schwann cells.
abstract: The axolemma membrane forms a stable and reproducible monomolecular layer at the air-aqueous interface. The major lipids and proteins are present in this monolayer in molar ratios similar to the original membrane. Acetylcholinesterase and Na-K-ATPase activities are preserved in the monolayer to levels of 64% and 25%, respectively. The total lipid fraction forms a homogeneously mixed phase. The presence of proteins in the monolayer introduces surface inhomogeneties. Among other features, this is revealed by the presence of two values of lateral pressure at which the monolayer shows partial or total collapse: a broad partial collapse at surface pressures between 13 to 30 mN/m and a sharp collapse point at 46 mN/m. The average molecular areas, the broad collapse point, and the variation of the surface potential per molecule suggest the relocation of protein components at surface pressures between 13 to 30 mN/m. The behavior is consistent with the extrusion and exposure of proteins toward the aqueous medium that depends on the lateral pressure. Schwann cells grown on coverslips coated with axolemma monolayers at 13 mN/m (beginning of the broad collapse) and 34 mN/m (above the broad collapse) recognize the difference in the surface organization of axolemma caused by the lateral pressure which affects their proliferation, morphology, and spatial pattern of organization. Our results show for the first time that response of Schwann cells depends on the intermolecular organization of the axolemma surface with which they interact. These results suggest that the local expression of putative surface molecules of axolemma that may mediate membrane recognition and the signalling of morphological and proliferative changes can be modulated by long range supramolecular properties.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Medical College of Virginia, Virginia Commonwealth University, Richmond 23298-0614.
authors.forename: R O
authors.initials: RO
authors.lastname: Calderon
authors.forename: B
authors.initials: B
authors.lastname: Maggio
authors.forename: T J
authors.initials: TJ
authors.lastname: Neuberger
authors.forename: G H
authors.initials: GH
authors.lastname: De Vries
mesh_terms: D000818:Animals; D001369:Axons / Q000737:chemistry* / Q000502:physiology; D002417:Cattle; D002462:Cell Membrane / Q000737:chemistry; D002478:Cells, Cultured; D055598:Chemical Phenomena; D002627:Chemistry, Physical; D008055:Lipids / Q000737:chemistry; D009419:Nerve Tissue Proteins / Q000737:chemistry; D051381:Rats; D012583:Schwann Cells / Q000502:physiology* / Q000648:ultrastructure; D013499:Surface Properties; D013936:Thymidine / Q000378:metabolism
chemical_list: D008055:Lipids; D009419:Nerve Tissue Proteins; D013936:Thymidine