Salvatori S, Furlan S, Millikin B, Sabbadini R, Betto R, Margreth A, Salviati G
CNR Unit for Muscle Biology and Physiopathology, University of Padova, Italy.
Biochem Biophys Res Commun. 1993 Nov 15;196(3):1073-80. doi: 10.1006/bbrc.1993.2360.
Membrane fractions enriched in transverse tubules, either predominantly free or junctional, sarcoplasmic reticulum subfractions and purified sarcolemmal preparations have been isolated from rabbit skeletal muscle and examined for their contents of protein kinase C. Using activity measurements and immunoblotting methods, we have been able to detect substantial amounts of endogenous protein kinase C in T-tubules membranes and to a lesser extent, in muscle sarcolemma. Protein kinase C was found to be highest in junctional T-tubules and to be virtually absent from sarcoplasmic reticulum-derived membrane fractions. Immunofluorescence staining of muscle fibers is consistent with a T-tubule localization of the kinase. The T-tubule-associated protein kinase C enzyme phosphorylates several potentially important membrane proteins.
富含横小管的膜组分,无论是主要游离的还是连接的,肌浆网亚组分以及纯化的肌膜制剂,均已从兔骨骼肌中分离出来,并检测了它们的蛋白激酶C含量。通过活性测量和免疫印迹方法,我们能够在横小管膜中检测到大量内源性蛋白激酶C,在肌膜中的含量则较少。发现蛋白激酶C在连接性横小管中含量最高,而在肌浆网衍生的膜组分中几乎不存在。肌纤维的免疫荧光染色与该激酶在横小管中的定位一致。与横小管相关的蛋白激酶C酶可使几种潜在重要的膜蛋白磷酸化。