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Calcium mobilization evoked by amyloid beta-protein involves inositol 1,4,5-triphosphate production in human platelets.

机译:淀粉样β蛋白诱发的钙动员涉及人血小板中肌醇1,4,5-三磷酸的产生。

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We examined the effects of amyloid beta-protein (A beta) on Ca2+ mobilization in human platelets. The addition of A beta fragments 25-35 (A beta 25-35) gradually increased the cytoplasmic free Ca2+ concentration ([Ca2+]i). After the maximum response, [Ca2+]i decreased and then reached a sustained, higher level of [Ca2+]i. Similar effects were also observed with A beta 1-40, whereas 1-28 , 12-28 and 31-35 did not affect the Ca2+ response. In the absence of extracellular Ca2+, A beta 25-35 caused a transient increase in [Ca2+]i, which returned to the resting level. U73122, a phospholipase C inhibitor, completely abolished Ca2+ mobilization induced by thrombin and A beta 25-35. Furthermore, A beta enhanced the production of inositol 1,4,5-trisphosphate (IP3) in platelets. These findings suggest that Ca2+ mobilization induced by A beta 25-35 is due to phospholipase C activation and IP3 production.
机译:我们检查了淀粉样蛋白β蛋白(A beta)对人类血小板中Ca2 +动员的影响。 A beta片段25-35(A beta 25-35)的添加逐渐增加了细胞质中游离Ca2 +的浓度([Ca2 +] i)。达到最大响应后,[Ca2 +] i降低,然后达到持续较高的[Ca2 +] i水平。使用A beta 1-40也观察到类似的效果,而1-28、12-28和31-35不会影响Ca2 +反应。在不存在细胞外Ca2 +的情况下,A beta 25-35导致[Ca2 +] i瞬时增加,并恢复到静止水平。磷脂酶C抑制剂U73122完全消除了凝血酶和A beta 25-35诱导的Ca2 +动员。此外,β增加了血小板中肌醇1,4,5-三磷酸(IP3)的产生。这些发现表明,A beta 25-35诱导的Ca2 +动员是由于磷脂酶C活化和IP3产生。

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