INTERACTION OF CALPONIN WITH PHOSPHOLIPIDS
INTERACTION OF CALPONIN WITH PHOSPHOLIPIDS
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DOI：
10.1093/oxfordjournals.jbchem.a124833
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发表时间：
1995-05-01
影响因子：
2.7
通讯作者：
KONDO, Y
中科院分区：
文献类型：
--
作者：
FUJII, T;YAMANA, K;KONDO, Y
通过沉降试验和亲和色谱法研究了鸡胗钙调蛋白和磷脂之间的相互作用。钙调蛋白与磷脂酰丝氨酸 (PS) 和磷脂酰肌醇 (PI) 囊泡一起沉淀，但不与磷脂酰胆碱 (PC) 囊泡一起沉淀。钙调蛋白对PS和PI的表观K-d值分别计算为1.3X10(6)和1.5X10(6)M(-1)，胰凝乳蛋白酶消化的结构域图谱表明磷脂结合位点位于N端22-kDa片段内，其中肌动蛋白、钙调蛋白、S100和原肌球蛋白也发生结合。 与 PS 和 PI 囊泡结合的钙调蛋白随着离子强度或 Ca2+ 浓度的增加而减少。钙调蛋白-PS 囊泡相互作用需要 MgCl2 的存在。钙调蛋白结合蛋白（包括肌动蛋白、钙调蛋白和 S100）以浓度依赖性方式抑制钙调蛋白与磷脂囊泡的结合，而原肌球蛋白对此结合影响不大。仅在存在 CaCl2 的情况下才发现钙调蛋白和 S100 的抑制作用。 caldesmon 和 SM22 都不影响结合。
The interaction between chicken gizzard calponin and phospholipids was examined by sedimentation assay and affinity chromatography. Calponin was sedimented with phosphatidylserine (PS) and phosphatidylinositol (PI) vesicles but not with phosphatidylcholine (PC) vesicles. The apparent K-d values of calponin to PS and PI were calculated to be 1.3X10(6) and 1.5X10(6) M(-1), respectively, Domain mapping with chymotryptic digestion showed that the phospholipid-binding site resided within the N-terminal 22-kDa fragment, in which the bindings of actin, calmodulin, S100, and tropomyosin also occur, The amount of calponin bound to PS and PI vesicles decreased with increasing ionic strength or Ca2+ concentrations. The presence of MgCl2 was needed for the calponin-PS vesicle interaction. Calponin-binding proteins including actin, calmodulin, and S100 inhibited calponin binding to the phospholipid vesicles in a concentration-dependent manner, while tropomyosin had little effect on the binding. The inhibitory effects of calmodulin and S100 were found only in the presence of CaCl2. Neither caldesmon nor SM22 affected the binding.