Schwann cell expression of a major myelin glycoprotein in the absence of myelin assembly

J. F. Poduslo, C. T. Berg, Peter J Dyck

Research output: Contribution to journalArticle

25 Citations (Scopus)

Abstract

Quiescent Schwann cells in the distal segment of the permanently transected nerve produced basal levels of the major myelin glycoprotein, P0, in the absence of myelin assembly. Low levels of P0 could be detected at 35 days after transection by autoradiographic analysis of radioiodinated lectin binding after protein separation by high-resolution sodium dodecyl sulfate pore gradient electrophoresis and by fluorographic analysis after electrophoresis of [3H]fucose-and [3H]mannose-labeled glycoproteins after incorporation into endoneurial slices. Immunoreactivity to P0 in the transected nerve could also be demonstrated with antisera against P0 as evaluated by direct 'immune overlay' after electrophoresis. These results indicate that the requirement for continuing signals from appropriate axons to make detectable amounts of myelin-specific proteins and glycolipids is not absolute. Schwann cells, therefore, like oligodendrocytes, can synthesize myelin components in the absence of neuronal influence, although information from neuronal elements probably is required for myelin assembly by Schwann cells and for myelin compaction by oligodendrocytes.

Original languageEnglish (US)
Pages (from-to)1864-1866
Number of pages3
JournalProceedings of the National Academy of Sciences of the United States of America
Volume81
Issue number6 I
StatePublished - 1984

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Schwann Cells
Myelin Sheath
Glycoproteins
Electrophoresis
Oligodendroglia
Myelin P0 Protein
Myelin Proteins
Fucose
Glycolipids
Mannose
Lectins
Sodium Dodecyl Sulfate
Axons
Immune Sera
Carrier Proteins

ASJC Scopus subject areas

  • General
  • Genetics

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Schwann cell expression of a major myelin glycoprotein in the absence of myelin assembly. / Poduslo, J. F.; Berg, C. T.; Dyck, Peter J.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 81, No. 6 I, 1984, p. 1864-1866.

Research output: Contribution to journalArticle

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N2 - Quiescent Schwann cells in the distal segment of the permanently transected nerve produced basal levels of the major myelin glycoprotein, P0, in the absence of myelin assembly. Low levels of P0 could be detected at 35 days after transection by autoradiographic analysis of radioiodinated lectin binding after protein separation by high-resolution sodium dodecyl sulfate pore gradient electrophoresis and by fluorographic analysis after electrophoresis of [3H]fucose-and [3H]mannose-labeled glycoproteins after incorporation into endoneurial slices. Immunoreactivity to P0 in the transected nerve could also be demonstrated with antisera against P0 as evaluated by direct 'immune overlay' after electrophoresis. These results indicate that the requirement for continuing signals from appropriate axons to make detectable amounts of myelin-specific proteins and glycolipids is not absolute. Schwann cells, therefore, like oligodendrocytes, can synthesize myelin components in the absence of neuronal influence, although information from neuronal elements probably is required for myelin assembly by Schwann cells and for myelin compaction by oligodendrocytes.

AB - Quiescent Schwann cells in the distal segment of the permanently transected nerve produced basal levels of the major myelin glycoprotein, P0, in the absence of myelin assembly. Low levels of P0 could be detected at 35 days after transection by autoradiographic analysis of radioiodinated lectin binding after protein separation by high-resolution sodium dodecyl sulfate pore gradient electrophoresis and by fluorographic analysis after electrophoresis of [3H]fucose-and [3H]mannose-labeled glycoproteins after incorporation into endoneurial slices. Immunoreactivity to P0 in the transected nerve could also be demonstrated with antisera against P0 as evaluated by direct 'immune overlay' after electrophoresis. These results indicate that the requirement for continuing signals from appropriate axons to make detectable amounts of myelin-specific proteins and glycolipids is not absolute. Schwann cells, therefore, like oligodendrocytes, can synthesize myelin components in the absence of neuronal influence, although information from neuronal elements probably is required for myelin assembly by Schwann cells and for myelin compaction by oligodendrocytes.

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