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Regulates Early Fibroblast Responses to Myocardial Infarction
Author(s) -
McCurdy Sarah M.,
Dai Qiuxia,
Bradshaw Amy D.,
Lindsey Merry L.
Publication year - 2010
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.24.1_supplement.600.1
Subject(s) - ctgf , matricellular protein , fibroblast , myocardial infarction , cyr61 , wound healing , extracellular matrix
Secreted protein, acidic, and rich in cysteine (SPARC) is a matricellular protein that helps collagen fibrils assemble. Collagen deposition to form a scar is a key event following a myocardial infarction (MI). Accordingly, we examined wild type (WT; n=22) and SPARC deficient (SPARC‐null; n=25) mice at day 3 post‐MI. Day 0 unoperated WT (n=28) and SPARC‐null (n=20) mice served as controls. Infarct size was similar between the two groups (52±2% for WT and 47±2% for SPARC‐null; p=n.s.). WT mice increased end diastolic volumes, but SPARC‐null mice showed increased end diastolic volumes to a lesser extent, indicating reduced remodeling. Interestingly, collagen levels in the SPARC‐null mice were 66% of the wild type values, indicating reduced collagen deposition in the absence of SPARC. Fibroblasts isolated from the infarct region of the null mice showed differential expression of several ECM genes, including MMP‐3, TIMP‐2, CTGF, and TGFβ. Our data suggests that SPARC deletion is beneficial in the early time post MI by regulating fibroblast activation, but whether this benefit persists through longer times needs to be examined. In conclusion, SPARC plays a major role in cardiac wound healing by regulating fibroblast function.