The thermotropic behavior (studied by high-sensitivity differential scanning calorimetry) and susceptibility to Vibrio cholerae sialidase hydrolysis of large unilamellar vesicles of dipalmitoyl-phosphatidylcholine, containing native GD1a ganglioside or the molecular species of GD1a containing C18:1 or C20:1 long-chain base (C18:1 GD1a; C20:1 GD1a), were studied. Vesicles containing ganglioside (10% in molar terms) showed the presence in the heat capacity function of a second minor peak besides the phospholipid main transition peak. The presence of a second peak is much more evident with C20:1 GD1a than with C18:1 GD1a, the difference being potentiated by Ca2+ and indicating a different tendency of the CD1a molecular species to undergo lateral phase separation. The scans of vesicles containing native GD1a showed the features of those obtained with C18:1 GD1a and C20:1 GD1a, indicating that the main components of native GD1a, C18:1 GD1a and C20:1 GD1a, maintain their individual aggregative properties. V. cholerae sialidase affects vesicle-bound GD1a at a much higher rate (17-25-fold) than it does micellar GD1a, the activation by Ca2+ being 3- and 2-fold, respectively. The Vmax values were identical on C18:1 GD1a and C20:1 GD1a in micellar dispersions, whereas they were markedly higher (from 20 to 50%) on C18:1 GD1a than on C20:1 GD1a in vesicular dispersions. Exhaustive sialidase hydrolysis of vesicles carrying native GD1a produced C18:1 GM1 and C20:1 GM1 in the same proportion as the C18:1 and C20:1 species present in native GD1a (53.9% and 46.1%).(ABSTRACT TRUNCATED AT 250 WORDS)
Masserini, M., Palestini, P., Venerando, B., Fiorilli, A., Acquotti, D., Tettamanti, G. (1988). Interactions of proteins with ganglioside-enriched microdomains on the membrane: the lateral phase separation of molecular species of GD1a ganglioside, having homogeneous long-chain base composition, is recognized by Vibrio cholerae sialidase. BIOCHEMISTRY, 27(20), 7973-7978 [10.1021/bi00420a057].
Interactions of proteins with ganglioside-enriched microdomains on the membrane: the lateral phase separation of molecular species of GD1a ganglioside, having homogeneous long-chain base composition, is recognized by Vibrio cholerae sialidase
MASSERINI, MASSIMO ERNESTO;PALESTINI, PAOLA NOVERINA ADA;
1988
Abstract
The thermotropic behavior (studied by high-sensitivity differential scanning calorimetry) and susceptibility to Vibrio cholerae sialidase hydrolysis of large unilamellar vesicles of dipalmitoyl-phosphatidylcholine, containing native GD1a ganglioside or the molecular species of GD1a containing C18:1 or C20:1 long-chain base (C18:1 GD1a; C20:1 GD1a), were studied. Vesicles containing ganglioside (10% in molar terms) showed the presence in the heat capacity function of a second minor peak besides the phospholipid main transition peak. The presence of a second peak is much more evident with C20:1 GD1a than with C18:1 GD1a, the difference being potentiated by Ca2+ and indicating a different tendency of the CD1a molecular species to undergo lateral phase separation. The scans of vesicles containing native GD1a showed the features of those obtained with C18:1 GD1a and C20:1 GD1a, indicating that the main components of native GD1a, C18:1 GD1a and C20:1 GD1a, maintain their individual aggregative properties. V. cholerae sialidase affects vesicle-bound GD1a at a much higher rate (17-25-fold) than it does micellar GD1a, the activation by Ca2+ being 3- and 2-fold, respectively. The Vmax values were identical on C18:1 GD1a and C20:1 GD1a in micellar dispersions, whereas they were markedly higher (from 20 to 50%) on C18:1 GD1a than on C20:1 GD1a in vesicular dispersions. Exhaustive sialidase hydrolysis of vesicles carrying native GD1a produced C18:1 GM1 and C20:1 GM1 in the same proportion as the C18:1 and C20:1 species present in native GD1a (53.9% and 46.1%).(ABSTRACT TRUNCATED AT 250 WORDS)
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