Nogues M, Cuenda A, Henao F, Gutiérrez-Merino C
Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura, Badajoz, Spain.
Z Naturforsch C J Biosci. 1996 Jul-Aug;51(7-8):591-8.
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.
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。