The myelin-axolemmal complex: biochemical dissection and the role of galactosphingolipids

Krishna Menon, Matthew N Rasband, Christopher M Taylor, Peter Brophy, Rashmi Bansal, Steven E Pfeiffer

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

Myelin-axolemmal interactions regulate many cellular and molecular events, including gene expression, oligodendrocyte survival and ion channel clustering. Here we report the biochemical fractionation and enrichment of distinct subcellular domains from myelinated nerve fibers. Using antibodies against proteins found in compact myelin, non-compact myelin and axolemma, we show that a rigorous procedure designed to purify myelin also results in the isolation of the myelin-axolemmal complex, a high-affinity protein complex consisting of axonal and oligodendroglial components. Further, the isolation of distinct subcellular domains from galactolipid-deficient mice with disrupted axoglial junctions is altered in a manner consistent with the delocalization of axolemmal proteins observed in these animals. These results suggest a paradigm for identification of proteins involved in neuroglial signaling.
Original languageEnglish
Pages (from-to)995-1009
Number of pages15
JournalJournal of Neurochemistry
Volume87
Issue number4
Publication statusPublished - 2003

Fingerprint

Dive into the research topics of 'The myelin-axolemmal complex: biochemical dissection and the role of galactosphingolipids'. Together they form a unique fingerprint.

Cite this