Coordinate expression of Ca2+‐ATPase slow‐twitch isoform and of β calmodulin‐dependent protein kinase in phospholamban‐deficient sarcoplasmic reticulum of rabbit masseter muscle

FEBS Letters

Pallanca, Alessandra¹  Sacchetto, Roberta¹  Margreth, Alfredo¹  Damiani, Ernesto¹ 

[1] NRC Unit for Muscle Biology and Physiopathology, Department of Experimental Biomedical Sciences, University of Padua, viale G. Colombo 3, 35121 Padua, Italy

关键词: Phospholamban;    Calmodulin protein kinase;    Sarcoplasmic reticulum;    Rabbit masseter;    Skeletal muscle;    CaM K II;    calmodulin-dependent protein kinase II;    SERCA;    sarcoendoplasmic reticulum Ca2+-ATPase;    MHC;    myosin heavy chain;    MHCI-α;    α-cardiac-like myosin heavy chain;    PLB;    phospholamban;    SR;    sarcoplasmic reticulum;   

DOI  :  10.1016/S0014-5793(00)01993-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Modulation of sarcoplasmic reticulum (SR) Ca²⁺ transport by endogenous calmodulin-dependent protein kinase II (CaM K II) involves covalent changes of regulatory protein phospholamban (PLB), as a common, but not the only mechanism, in limb slow-twitch muscles of certain mammalian species, such as the rabbit. Here, using immunofluorescent techniques in situ, and biochemical and immunological methods on the isolated SR, we have demonstrated that rabbit masseter, a muscle with a distinct embryological origin, lacks PLB. Accommodating embryological heterogeneity in the paradigm of neural-dependent expression of specific isogenes in skeletal muscle fibers, our results provide novel evidence for the differential expression in the SR of 72 kDa β components of CaM K II, together with the expression of a slow-twitch sarcoendoplasmic reticulum Ca²⁺-ATPase isoform, both in limb muscle and in the masseter.

【 授权许可】

Unknown