Activity of MMP‐9 after repair of abdominal wall defects with acellular and crosslinked bovine pericardium in rabbit. Issue 1 (22nd June 2012)

• Record Type: Journal Article
• Authors: Singh, Himani; Kumar, Naveen; Sharma, AK; Kataria, Meena; Munjal, Ashok; Kumar, Amit; Dewangan, Rukmani; Kumar, Vineet; Devarathnam, J; Kumar, Sachin
• Is Part Of: International wound journal. Volume 11:Issue 1(2014)
• Page Start: 5
• Page End: 13
• Publication Date: 2012-06-22
• Subjects: Wounds and injuries -- Treatment -- Periodicals; Wounds and injuries -- Periodicals; Wound healing -- Periodicals; 617.1005
• DOI: 10.1111/j.1742-481X.2012.01031.x
• Languages: English
• ISSNs: 1742-4801

Abstract

<abstract abstract-type="main" xml:lang="en"> <title> <x xml:space="preserve">Abstract</x> </title> <p>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.</p> </abstract>