Ganglioside–basic protein interaction: Protection of gangliosides against neuraminidase action
- H. C. Yohe,
- Ronald I. Jacobson,
- Robert K. Yu(corresponding author)
- Yale University,
- University of Minnesota Twin Cities
Abstract
The ability of acidic phospho‐ and sphingolipids to interact with basic proteins was studied by double diffusion analysis. The phospholipids, tri‐ and diphosphoinositide, and the sphingolipid, sulfatide, interacted with myelin basic protein as evidenced by precipitin line formation. Of the sialoglycosphingolipids (gangliosides) tested, only the myelin‐specific monosialoganglioside, GM4 , formed a precipitin line with myelin basic protein. In addition, myelin basic protein retarded the activity of Clostridium perfringens neuraminidase against GM4 and the disialoganglioside, GD1b. Examination of purified rat brain myelin suggested the presence of a neuraminidase activity intrinsic to myelin. This finding, in concert with ganglioside‐myelin basic protein complexes which selectively protect against neuraminidase, may provide a physiological explanation for the simplified ganglioside pattern found in myelin.
Publication Information
Output type
Original language
English (US)Pages from-to (Number of pages)
Pages 401-412 (12 pages)Journal (Volume, Issue Number)
Journal of Neuroscience Research (Volume 9, Issue 4)Publication milestones
- Published - 1983
Publication status
ISSN
0360-4012Publication IDs
- Scopus: 0020570607
- PubMed: 6192246
