Differential modulation of the expression of axonal proteins by non-neuronal cells of the peripheral and central nervous system.

Sonderegger, P.; Lemkin, Peter F.; Lipkin, Lewis E.; Nelson, Phillip G.

doi:10.1002/j.1460-2075.1985.tb03792.x

Cited by 31 publications

(22 citation statements)

References 40 publications

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“…For aggregate formation, 2×10 6 cells in 4 ml spinal cord cell culture medium were transferred into 25 ml Erlenmeyer flasks and incubated for 20 h on a gyratory shaker (HT, Infors AG, Bottmingen, Switzerland) at 81 rpm under cell culture conditions (37°C and 95% air/5% CO 2 ). As cell culture medium we used Modified Minimum Essential Medium, supplemented with 2 mM glutamine, 5% heat-inactivated horse serum (all Invitrogen, CH), 2% chicken embryo extract, 1% nutrient mixture as described by Sonderegger et al [29] and 10% muscle cell conditioned medium (being the supernatant of embryonic chicken breast muscle cultures kept for 124 hours in this medium). Subsequently, cell reaggregates of optimal size (90–140 µm in diameter) were obtained.…”

Section: Methodsmentioning

confidence: 99%

Surface Microstructures on Planar Substrates and Textile Fibers Guide Neurite Outgrowth: A Scaffold Solution to Push Limits of Critical Nerve Defect Regeneration?

et al. 2012

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The treatment of critical size peripheral nerve defects represents one of the most serious problems in neurosurgery. If the gap size exceeds a certain limit, healing can't be achieved. Connection mismatching may further reduce the clinical success. The present study investigates how far specific surface structures support neurite outgrowth and by that may represent one possibility to push distance limits that can be bridged. For this purpose, growth cone displacement of fluorescent embryonic chicken spinal cord neurons was monitored using time-lapse video. In a first series of experiments, parallel patterns of polyimide ridges of different geometry were created on planar silicon oxide surfaces. These channel-like structures were evaluated with and without amorphous hydrogenated carbon (a-C:H) coating. In a next step, structured and unstructured textile fibers were investigated. All planar surface materials (polyimide, silicon oxide and a-C:H) proved to be biocompatible, i.e. had no adverse effect on nerve cultures and supported neurite outgrowth. Mean growth cone migration velocity measured on 5 minute base was marginally affected by surface structuring. However, surface structure variability, i.e. ridge height, width and inter-ridge spacing, significantly enhanced the resulting net velocity by guiding the growth cone movement. Ridge height and inter-ridge distance affected the frequency of neurites crossing over ridges. Of the evaluated dimensions ridge height, width, and inter-ridge distance of respectively 3, 10, and 10 µm maximally supported net axon growth. Comparable artificial grooves, fabricated onto the surface of PET fibers by using an excimer laser, showed similar positive effects. Our data may help to further optimize surface characteristics of artificial nerve conduits and bioelectronic interfaces.

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Section: Methodsmentioning

confidence: 99%

Surface Microstructures on Planar Substrates and Textile Fibers Guide Neurite Outgrowth: A Scaffold Solution to Push Limits of Critical Nerve Defect Regeneration?

et al. 2012

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“…Selective metabolic labelling of axonally secreted proteins in a compartmental cell culture system The compartmental cell culture system, originally devised by Campenot (1977,1979) was used in a version modified for selective metabolic labelling of axonally transported proteins (Sonderegger et al, 1983(Sonderegger et al, , 1984(Sonderegger et al, , 1985 and adapted for the study of the proteins released into the medium. A full description of the experimental details will be given in a separate paper (Stoeckli et al, 1989).…”

Section: Methodsmentioning

confidence: 99%

Purification of axonin-1, a protein that is secreted from axons during neurogenesis.

et al. 1989

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Using selective metabolic labelling in a compartmental cell culture system two proteins, denoted axonin‐1 and axonin‐2, were found to be secreted by axons of dorsal root ganglia neurons from chicken embryos. Based on its characteristic coordinates and spot morphology in two‐dimensional gel electrophoresis, axonin‐1 was detected in the cerebrospinal fluid and the vitreous fluid, axonin‐1 was purified 476‐fold to homogeneity by a four‐step chromatographic procedure. The identity of the purified protein as axonin‐1 was confirmed by immunological methods. Axonin‐1 is a glycoprotein that subdivides into at least 16 immunologically similar isoelectric variants; their molecular weight range extends from 132 to 140 kd and their pI range from 5.3 to 6.2. In the vitreous fluid of the embryo, axonin‐1 could first be detected on the embryonic day 5 and highest concentrations were measured during the second half of embryonic life; in the vitreous fluid of the adult chicken, concentrations were approximately 20 times lower. The early onset of secretion and the time course of expression suggest a role for axonin‐1 in the development of the nervous system.

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“…DRG neurons were dissected from 10-day-old chicken embryos and cultured essentially as described by Sonderegger and co-workers (46). Selective labeling of newly synthesized proteins was carried out essentially as described by Stoeckli and co-workers (47).…”

Section: Construction Of the Expression Vectors Pcns Pcns-c And Pcnmentioning

confidence: 99%

The Axonally Secreted Serine Proteinase Inhibitor, Neuroserpin, Inhibits Plasminogen Activators and Plasmin but Not Thrombin

Osterwalder

Cinelli

Baici³

et al. 1998

Journal of Biological Chemistry

128

112

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Neuroserpin is an axonally secreted serine proteinase inhibitor that is expressed in neurons during embryogenesis and in the adult nervous system. To identify target proteinases, we used a eucaryotic expression system based on the mouse myeloma cell line J558L and vectors including a promoter from an Ig--variable region, an Ig-enhancer, and the exon encoding the Igconstant region (C) and produced recombinant neuroserpin as a wild-type protein or as a fusion protein with C. We investigated the capability of recombinant neuroserpin to form SDS-stable complexes with, and to reduce the amidolytic activity of, a variety of serine proteinases in vitro. Consistent with its primary structure at the reactive site, neuroserpin exhibited inhibitory activity against trypsin-like proteinases. Although neuroserpin bound and inactivated plasminogen activators and plasmin, no interaction was observed with thrombin. A reactive site mutant of neuroserpin neither formed complexes with nor inhibited the amidolytic activity of any of the tested proteinases. Kinetic analysis of the inhibitory activity revealed neuroserpin to be a slow binding inhibitor of plasminogen activators and plasmin. Thus, we postulate that neuroserpin could represent a regulatory element of extracellular proteolytic events in the nervous system mediated by plasminogen activators or plasmin.Extracellular proteolysis exerted by serine proteinases has been implicated in a variety of processes in the nervous system during development and in adulthood. Among the serine proteinases recently reported to play a role in neural development and function, there are several well known proteins that had previously been found and characterized in nonneuronal functions, in particular blood coagulation and fibrinolysis. For example, tissue-type plasminogen activator (tPA) 1 and urokinase plasminogen activator (uPA) were found to be expressed in the nervous system (1, 2), and they have been demonstrated to be engaged in developmental processes such as cerebellar granule cell migration (3, 4), Schwann cell migration, and wrapping of axons (5), or neuromuscular synapse elimination (6). In the period of neurite outgrowth, plasminogen activators (PAs) have been found to be secreted at the growth cones of cultured neurons or neuronal cell lines (7,8), and they were demonstrated to modify the molecular composition of the neurites' substrata in vitro (9). In the adult nervous system, tPA is induced in the hippocampus after seizure, kindling, and long term potentiation (LTP) (10) and in the cerebellum after motor learning tasks (11), and mice lacking the gene for tPA (12) show a different form of hippocampal LTP (13,14). Furthermore, tPA has been demonstrated to be involved in excitotoxin-induced neuronal cell death in the murine hippocampus by converting locally secreted plasminogen to active plasmin (15, 16). Thrombin, which has been extensively characterized due to its important function in the blood clotting system, has been reported to be expressed in the nervous system (17). I...

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Differential modulation of the expression of axonal proteins by non-neuronal cells of the peripheral and central nervous system.

Cited by 31 publications

References 40 publications

Surface Microstructures on Planar Substrates and Textile Fibers Guide Neurite Outgrowth: A Scaffold Solution to Push Limits of Critical Nerve Defect Regeneration?

Surface Microstructures on Planar Substrates and Textile Fibers Guide Neurite Outgrowth: A Scaffold Solution to Push Limits of Critical Nerve Defect Regeneration?

Purification of axonin-1, a protein that is secreted from axons during neurogenesis.

The Axonally Secreted Serine Proteinase Inhibitor, Neuroserpin, Inhibits Plasminogen Activators and Plasmin but Not Thrombin

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