CALMODULIN IN NATURAL AND RECONSTITUTED CALCIUM TRANSPORTING SYSTEMS *
CALMODULIN IN NATURAL AND RECONSTITUTED CALCIUM TRANSPORTING SYSTEMS *
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天然和重构钙运输系统中的钙调蛋白 *
DOI：
10.1111/j.1749-6632.1980.tb29616.x
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发表时间：
1980
影响因子：
5.2
通讯作者：
P. Caroni
中科院分区：
文献类型：
--
作者：
E. Carafoli;V. Niggli;K. Malmström;P. Caroni
跨生物膜的高效运输是Ca信使功能的要求”（集：Carafoli & Crompton '供审查）。这种信使功能的独特重要性被存在于不同的膜系统和不同的机制中的Ca "转运系统的多样性所强调。这些系统的监管是该领域的一个模糊方面，但很明显，监管机制的存在将提高信使功能的效率。在这方面，Gopinath、Vincenzi、Jarrett和Penniston3对钙调素刺激红细胞膜[Ca2+ +Mg+] - atp酶的最初观察，以及Katz和Remtulla4最近对心脏肌浆网Ca泵送系统的类似作用的观察，都是非常有趣的。目前，钙转运系统已在以下细胞膜中被描述：在线粒体中，存在钙摄取和钙释放的独立且机械不同的途径；在不同细胞的质膜中，已经描述了用于Ca2+内流的“缓慢CaZ+通道”，用于Ca2+外排的CaZ ' - atp酶和Na+/Ca ' +交换系统（可能在任何方向上使用）；在肌浆网中。它具有特定的Ca2+泵送atp酶，现在已经在分子细节上进行了研究；在内质网，其中一个特定的atp依赖性Ca2+泵送系统已被记录；在一些细菌中，已经证明了Ca2+特异性atp酶和Ca ' +/H+交换。红细胞膜的Ca2 '泵送atp酶已被Niggli等纯化，并在磷脂双层囊泡中重组（Carafoli等01.~）。它与钙调素的相互作用现在可以在分离和重组的系统中进行研究：这里将描述工作的某些方面。肌浆网Ca2 ' -A？Pase也以纯化的形式存在了很长时间，但迄今为止还没有关于钙调素和纯化的（和重组的）ATPase之间相互作用的报道。然而，最初关于钙调蛋白4刺激心脏肌浆网钙转运的观察最近被LePeuch等人扩展。和令人信服的证据表明，钙调素的作用不是直接的，而是通过磷酸化-去磷酸化系统介导的。目前的工作还包括来自随意肌的肌浆网钙调蛋白的数据。到目前为止，还没有迹象表明钙调素在上述任何其他钙转运系统中的作用，甚至没有迹象表明钙调素的存在。的
Efficient transport across biological membranes is a requirement for the messenger function of Ca” (set: Carafoli & Crompton’ for review]. The unique importance of this messenger function is underscored by the existence of a multiplicity of Ca” transporting systems, located in different membrane systems, and different in mechanism. The regulation of these systems is one obscure aspect of the field, but it is clear that the efficiency of the messenger function would be heightened by the existence of regulatory mechanisms. In this respect, the original observation by Gopinath and Vincenzi’ and Jarrett and Penniston3 of a stimulation by calmodulin of the [Ca2+ +Mg+)-ATPase of the erythrocyte membrane, and the more recent observation by Katz and Remtulla4 of similar effects on the Ca” pumping system of heart sarcoplasmic reticulum, are of great interest. At the present date, Ca” transporting systems have been described in the following membranes: in mitochondria, where separate, and mechanistically different, routes for Ca’’ uptake and Ca“ release exist; in the plasma membrane of different cells, where a “slow CaZ+ channel” for Ca2+ influx, a CaZ’-ATPase for Ca2+ efflux, and a Na+/Ca’+ exchange system (that is probably used in either direction] have been described; in sarcoplasmic reticulum. which possesses a specific Ca2+-pumping ATPase, which has now been studied in great molecular detail; in endoplasmic reticulum, in which a specific ATP-dependent Ca2+ pumping system has been documented; and in several bacteria, in which a Ca2+-specific ATPase, and a Ca‘+/H+ exchange, have been demonstrated. The Ca2’ -pumping ATPase of the erythrocyte membrane has been purified by Niggli et a).,’ and reconstituted in phospholipid bilayer vesicles (Carafoli et 01.~). Its interaction with calmodulin can now be studied in the isolated and reconstituted system: some aspects of the work will be described here. The sarcoplasmic reticulum Ca2’-A?’Pase has also been available in purified form for a long time, hut no work on the interaction between calmodulin and the purified [and reconstituted) ATPase has been reported so far. However, the original observation on the stimulation of the Ca” transport in heart sarcoplasmic reticulum by calmodulin4 has recently been extended by LePeuch et oJ.,~ and convincing evidence has been provided that the effect of calmodulin is not direct, but is mediated through a phosphorylation-dephosphorylation system. The present work also includes data on calmodulin in sarcoplasmic reticulum from voluntary muscle. No indications have so far tieen given for the role, or even the presence, of calmodulin in any of the other Ca’’ transporting systems mentioned above. The