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The possible role of serum from septic mice in dystrophin proteolysis in cultured newborn mice cardiomyocytes
Author(s) -
Malvestio Lygia Maria Mouri,
Prado Cibele Maria,
Celes Mara Rúbia Nunes,
Campos Erica Carolina,
Ferezin Patricia Mara,
Rossi Marcos Antonio
Publication year - 2013
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.27.1_supplement.1085.2
Subject(s) - dystrophin , sarcolemma , calpain , proteolysis , blot , chemistry , sepsis , myocyte , medicine , andrology , endocrinology , microbiology and biotechnology , duchenne muscular dystrophy , biology , biochemistry , gene , enzyme
Previous results from our laboratory demonstrated reduced dystrophin expression in hearts of septic mice. Dystrophin is responsible to protect the sarcolemma from mechanical stress during cycles of muscle contraction and relaxation. The loss of dystrophin turns the sarcolemma fragile leading to membrane disruption. This study evaluated the dystrophin expression in cultured newborn cardiomyocytes stimulated with serum of mice subjected to experimental sepsis induced by cecal ligation and puncture (CLP) and its relation with calpain and NF‐κB levels. Cardiomyocytes were incubated 5 days after their first spontaneous beating with sera from sham‐operated and septic mice for 24 hs. Serum from septic mice was obtained from male C57Bl/6 6 hs after CLP. Imunofluorescent (IF) staining and western blotting (WB) were performed for evaluation of dystrophin, calpain, and NF‐κB concentration. The cardiomyocytes stimulated with serum from septic mice presented decreased levels of dystrophin and increased levels of calpain and NF‐κB in comparison with cells incubated with sham serum. These results clearly demonstrate that septic serum causes dystrophin proteolysis in cultured newborn cardiomyocytes. This decrease possibly is related to proteolytic action of calpain that could be activate to NF‐κB overexpression contributing to dystrophin damage (supported by FAPESP).