Premium
Matrix metalloproteinase‐2 is not active in the diaphragm during mechanical ventilation
Author(s) -
Sollanek Kurt J,
Smuder Ashley J,
Hudson Matthew B,
Nelson W Bradley,
Carrigan Christopher T,
Urso Maria L,
Powers Scott K
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.lb779
Subject(s) - diaphragm (acoustics) , matrix metalloproteinase , messenger rna , mechanical ventilation , diaphragm muscle , atrophy , chemistry , diaphragmatic breathing , ventilation (architecture) , muscle atrophy , medicine , microbiology and biotechnology , endocrinology , biology , anatomy , respiratory system , pathology , biochemistry , gene , mechanical engineering , loudspeaker , engineering , physics , alternative medicine , acoustics
Prolonged mechanical ventilation (MV) results in diaphragmatic atrophy and contractile dysfunction, which occurs, in part, due to the activation of several proteolytic systems. New evidence shows matrix metalloproteinase‐2 (MMP‐2) can contribute to muscle fiber atrophy and contractile dysfunction in animal models of muscle disuse. Therefore, this experiment determined if prolonged MV alters mRNA expression and protein abundance of MMP‐2 and its regulators, TIMP‐2 and MT1‐MMP. Our results reveal that prolonged MV (12 hours) did not alter MMP‐2 mRNA expression or protein abundance in the diaphragm. Furthermore, prolonged MV did not promote an increase in mRNA expression of TIMP‐2 in the diaphragm. However, prolonged MV did result in a small increase in MT1‐MMP mRNA expression, but this increase may not be physiologically significant (<2‐fold). Finally, MV did not result in a significant change in diaphragmatic protein abundance for TIMP‐2 or MT1‐MMP. Collectively, our results demonstrate that MV does not activate MMP‐2 or its regulators. Supported by NIH RO1 HL087839 (SKP) and MRMC (MLU).