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