Full activation without calmodulin of calmodulin‐dependent cyclic nucleotide phosphodiesterase by acidic glycosphingolipids: GM3, sialosylneolactotetraosylceramide and sulfatide

FEBS Letters

Higashi, Hideyoshi¹  Yamagata, Tatsuya¹ 

[1] Laboratory of Glycoconjugate Research, Mitsubishi Kasei Institute of Life Sciences, 11 Minamiooya, Machida, Tokyo 194, Japan

关键词: GM3;    LM1;    Sulfatide;    Ganglioside;    Calmodulin;    cAMP-phosphodiesterase;    CaM;    calmodulin;    dansyl;    5-dimethylaminonaphthalene-1-sulfonyl;    PDE;    cyclic nucleotide phosphodiesterase. Abbreviations by Svennerholm [1] for gangliosides and IUPAC-IUB Recommendations for lipids [2] were used;    GD1b;    II3(NeuAca2-8NeuAc)-Gg4Cer;    LM1;    sialosylneolactotetraosylceramide;    IV3Sialyl-nLc4Cer. Structures of the other glycosphingolipids are shown in Table I;   

DOI  :  10.1016/0014-5793(92)81460-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Among calmodulin-non-binding glycosphingolipids, GM3, sialosylneolactotetraosylceramide (LM1), and sulfatide potently activated calmodulin-dependent cyclic nucleotide phosphodiesterase with or without Ca²⁺ showing ED₅₀ 1–5 μM. In contrast to calmodulin-binding gangliosides, these glycosphingolipids activated the enzyme up to the maximum level achieved by Ca²⁺/calmodulin and did not inhibit the activity at higher concentrations. Competition studies with GD1b that bind both to calmodulin and the enzyme suggest that the calmodulin-non-binding glycosphingolipids activate the enzyme through interaction with the same site of the enzyme as GD1b interacts.

【 授权许可】

Unknown