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大鼠骨骼肌糖原分解性肌浆网复合体中与糖原磷酸解偶联的钙离子摄取

Ca2+ uptake coupled to glycogen phosphorolysis in the glycogenolytic-sarcoplasmic reticulum complex from rat skeletal muscle.

作者信息

Nogues M, Cuenda A, Henao F, Gutiérrez-Merino C

机构信息

Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.

出版信息

Z Naturforsch C J Biosci. 1996 Jul-Aug;51(7-8):591-8.

PMID:8810099
Abstract

The glycogenolytic-sarcoplasmic reticulum complex from rat skeletal muscle accumulates Ca2+ upon stimulation of glycogen phosphorolysis in the absence of added ATP. It is shown that an efficient Ca2+ uptake involves the sequential action of glycogen phosphorylase, phosphoglucomutase and hexokinase, which generate low concentrations of ATP (approximately 1-2 microM) compartmentalized in the immediate vicinity of the sarcoplasmic reticulum Ca2+, Mg(2+)-ATPase (the Ca2+ pump). The Ca2+ uptake supported by glycogenolysis in this subcellular structure is strongly stimulated by micromolar concentrations of AMP, showing that the glycogen phosphorylase associated with this complex is in the dephosphorylated b form. The results point out that the flux through this compartmentalized metabolic pathway should be enhanced in physiological conditions leading to increased AMP concentrations in the sarcoplasm, such as long-lasting contractions and in ischemic muscle.

摘要

来自大鼠骨骼肌的糖原分解-肌浆网复合体在无外加ATP的情况下,受糖原磷酸解刺激时会积累Ca2+。结果表明,高效的Ca2+摄取涉及糖原磷酸化酶、磷酸葡萄糖变位酶和己糖激酶的顺序作用,它们在肌浆网Ca2+、Mg(2+)-ATP酶(Ca2+泵)紧邻区域产生低浓度的ATP(约1-2 microM)。该亚细胞结构中糖原分解所支持的Ca2+摄取受到微摩尔浓度AMP的强烈刺激,表明与该复合体相关的糖原磷酸化酶处于去磷酸化的b形式。结果指出,在导致肌浆中AMP浓度增加的生理条件下,如长时间收缩和缺血肌肉中,通过这种区域化代谢途径的通量应会增强。

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