Journal
JOURNAL OF MUSCLE RESEARCH AND CELL MOTILITY
Volume 36, Issue 2, Pages 195-203Publisher
SPRINGER
DOI: 10.1007/s10974-014-9403-z
Keywords
SERCA1b; SERCA1a; New-born muscle; Myotonic dystrophy; Duchenne muscular dystrophy; Diaphragm
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Funding
- European Union
- State of Hungary
- European Social Fund [TAMOP 4.2.4. A/2-11-1-2012-0001]
- [TAMOP-4.2.2/B-10/1-2010-0012]
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The sarcoplasmic/endoplasmic reticulum calcium ATPase 1 (SERCA1) has two muscle specific splice isoforms; SERCA1a in fast-type adult and SERCA1b in neonatal and regenerating skeletal muscles. At the protein level the only difference between these two isoforms is that SERCA1a has C-terminal glycine while SERCA1b has an octapeptide tail instead. This makes the generation of a SERCA1a specific antibody not feasible. The switch between the two isoforms is a hallmark of differentiation so we describe here a method based on the signal ratios of the SERCA1b specific and pan SERCA1 antibodies to estimate the SERCA1b/SERCA1a dominance on immunoblot of human muscles. Using this method we showed that unlike in mouse and rat, SERCA1b was only expressed in pre-matured infant leg and arm muscles; it was replaced by SERCA1a in more matured neonatal muscles and was completely absent in human foetal and neonatal diaphragms. Interestingly, only SERCA1a and no SERCA1b were detected in muscles of 7-12 years old boys with Duchenne, a degenerative-regenerative muscular dystrophy. However, in adult patients with myotonic dystrophy type 2 (DM2), the SERCA1b dominated over SERCA1a. Thus the human SERCA1b has a different expression pattern from that of rodents and it is associated with DM2.
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