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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Ganglioside-modulated proteolysis by Ca2(+)-activated neutral proteinase ( CANP): a role of glycoconjugates in CANP regulation.

We examined ganglioside modulation of the activity of the millimolar Ca2(+)-sensitive form (mCANP) of calcium-activated neutral proteinase ( CANP), which is enriched in myelin, from brain. GM1, GD1a, GT1a, GM2, and GM4 produced a concentration-dependent increase of mCANP activity. GD1a stimulated the greatest increase of enzyme activity (107%), followed by GT1a, whereas GD1b was inhibitory (56%). GM1, GM2, and GM4 stimulated but less so than GD1a and GT1a. Free N-acetylneuraminic acid, asialo-GM1, GM3, and a ganglioside mixture containing GM1, GD3, GD1a, and GD1b had no effect. The ganglioside-mediated modulation was not affected by trifluoperazine and chlorpromazine (phospholipid-binding antagonists). The mCANP Ca2+ requirement was significantly reduced in the presence of stimulatory gangliosides, and this increased sensitivity varied (10-50-fold) with ganglioside structure. Gangliosides may interact with membrane mCANP and modulate its proteolytic action.[1]

References

  1. Ganglioside-modulated proteolysis by Ca2(+)-activated neutral proteinase (CANP): a role of glycoconjugates in CANP regulation. Chakrabarti, A.K., Dasgupta, S., Banik, N.L., Hogan, E.L. J. Neurochem. (1990) [Pubmed]
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