Open AccessActivity of MMP‐9 after repair of abdominal wall defects with acellular and crosslinked bovine pericardium in rabbit
Author(s) -
Singh Himani,
Kumar Naveen,
Sharma AK,
Kataria Meena,
Munjal Ashok,
Kumar Amit,
Dewangan Rukmani,
Kumar Vineet,
Devarathnam J,
Kumar Sachin
Publication year - 2014
Publication title -
international wound journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.867
H-Index - 63
eISSN - 1742-481X
pISSN - 1742-4801
DOI - 10.1111/j.1742-481x.2012.01031.x
Subject(s) - matrix metalloproteinase , gelatinase , medicine , in vivo , pericardium , zymography , glutaraldehyde , in vitro , gelatin , rabbit (cipher) , microbiology and biotechnology , pathology , anatomy , biochemistry , surgery , chemistry , biology , mathematics , statistics
This study was undertaken for the identification of matrix metalloproteinases (MMPs) in extracts obtained from native, acellular and crosslinked bovine pericardium (in vitro), as well as in the plasma after implantation of these biomaterials in rabbits (in vivo). Native pericardium (NP) expressed a 72 kDa (MMP‐2) band; whereas, in acellular pericardium (AP) two bands (10 kDa and 92 kDa) of MMPs were observed of which, 92 kDa band was very faint. AP crosslinked with glutaraldehyde did not show any gelatinase activity and thus reflects the creation of new additional chemical bonds between the collagen molecules which has been effectively removed. Gelatin zymography showed only one major band of 92 kDa in all the implanted and untreated rabbit plasma, but the relative amount of 92 kDa was 1–2 times higher in acellular bovine pericardium implanted rabbits as compared to crosslinked and native groups. In NP group, the 92 kDa band was the dullest among the three groups. This indicated that the level of MMP‐9 corresponds to the degree of collagen degradation.