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Coordinate expression of Ca 2+ ‐ATPase slow‐twitch isoform and of β calmodulin‐dependent protein kinase in phospholamban‐deficient sarcoplasmic reticulum of rabbit masseter muscle
Author(s) -
Sacchetto Roberta,
Damiani Ernesto,
Pallanca Alessandra,
Margreth Alfredo
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01993-1
Subject(s) - phospholamban , endoplasmic reticulum , gene isoform , calmodulin , skeletal muscle , protein kinase a , atpase , chemistry , calcium atpase , cardiac muscle , biology , biochemistry , phosphorylation , microbiology and biotechnology , enzyme , endocrinology , gene
Modulation of sarcoplasmic reticulum (SR) Ca 2+ 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 Ca 2+ ‐ATPase isoform, both in limb muscle and in the masseter.