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Ganglioside–basic protein interaction: Protection of gangliosides against neuraminidase action

  • H. C. Yohe
    ,
  • Ronald I. Jacobson
    ,
  • Robert K. Yu(corresponding author)
*Corresponding author for this work
  • Yale University
    ,
  • University of Minnesota Twin Cities
Scholary Output:
Contribution to journal
Article
Peer-review

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

Scholary Output:
Contribution to journal
Article
Peer-review

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

Published - 1983

ISSN

0360-4012

Publication IDs

  • Scopus: 0020570607
  • PubMed: 6192246

Publication metrics

Metrics

Scopus
citations
Fractional count
1
Fractional count
0.33
Fractional count
2
Fractional count
0.67
Fractional count
1
Fractional count
1

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Captures
7
Citation count
48

Funding Details

FunderFunding number
NINDS
R01NS011853